331 results on '"Dye, John M."'
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2. Author Correction: Two point mutations in protocadherin-1 disrupt hantavirus recognition and afford protection against lethal infection
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Slough, Megan M., Li, Rong, Herbert, Andrew S., Lasso, Gorka, Kuehne, Ana I., Monticelli, Stephanie R., Bakken, Russell R., Liu, Yanan, Ghosh, Agnidipta, Moreau, Alicia M., Zeng, Xiankun, Rey, Félix A., Guardado-Calvo, Pablo, Almo, Steven C., Dye, John M., Jangra, Rohit K., Wang, Zhongde, and Chandran, Kartik
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- 2023
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3. Two point mutations in protocadherin-1 disrupt hantavirus recognition and afford protection against lethal infection
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Slough, Megan M., Li, Rong, Herbert, Andrew S., Lasso, Gorka, Kuehne, Ana I., Monticelli, Stephanie R., Bakken, Russell R., Liu, Yanan, Ghosh, Agnidipta, Moreau, Alicia M., Zeng, Xiankun, Rey, Félix A., Guardado-Calvo, Pablo, Almo, Steven C., Dye, John M., Jangra, Rohit K., Wang, Zhongde, and Chandran, Kartik
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- 2023
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4. Crimean-Congo hemorrhagic fever survivors elicit protective non-neutralizing antibodies that target 11 overlapping regions on glycoprotein GP38
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Shin, Olivia S., Monticelli, Stephanie R., Hjorth, Christy K., Hornet, Vladlena, Doyle, Michael, Abelson, Dafna, Kuehne, Ana I., Wang, Albert, Bakken, Russell R., Mishra, Akaash K., Middlecamp, Marissa, Champney, Elizabeth, Stuart, Lauran, Maurer, Daniel P., Li, Jiannan, Berrigan, Jacob, Barajas, Jennifer, Balinandi, Stephen, Lutwama, Julius J., Lobel, Leslie, Zeitlin, Larry, Walker, Laura M., Dye, John M., Chandran, Kartik, Herbert, Andrew S., Pauli, Noel T., and McLellan, Jason S.
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- 2024
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5. Anticancer pan-ErbB inhibitors reduce inflammation and tissue injury and exert broad-spectrum antiviral effects
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Saul, Sirle, Karim, Marwah, Ghita, Luca, Huang, Pei-Tzu, Chiu, Winston, Duran, Veronica, Lo, Chieh-Wen, Kumar, Sathish, Bhalla, Nishank, Leyssen, Pieter, Alem, Farhang, Boghdeh, Niloufar A., Tran, Do H.N., Cohen, Courtney A., Brown, Jacquelyn A., Huie, Kathleen E., Tindle, Courtney, Sibai, Mamdouh, Ye, Chengjin, Khalil, Ahmed Magdy, Chiem, Kevin, Martinez-Sobrido, Luis, Dye, John M., Pinsky, Benjamin A., Ghosh, Pradipta, Das, Soumita, Solow-Cordero, David E., Jin, Jing, Wikswo, John P., Jochmans, Dirk, Neyts, Johan, De Jonghe, Steven, Narayanan, Aarthi, and Einav, Shirit
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Inflammation -- Drug therapy ,Antiviral agents -- Research ,Drug discovery ,Pharmaceutical research ,Health care industry - Abstract
Targeting host factors exploited by multiple viruses could offer broad-spectrum solutions for pandemic preparedness. Seventeen candidates targeting diverse functions emerged in a screen of 4,413 compounds for SARS-CoV-2 inhibitors. We demonstrated that lapatinib and other approved inhibitors of the ErbB family of receptor tyrosine kinases suppress replication of SARS-CoV-2, Venezuelan equine encephalitis virus (VEEV), and other emerging viruses with a high barrier to resistance. Lapatinib suppressed SARS-CoV-2 entry and later stages of the viral life cycle and showed synergistic effect with the directacting antiviral nirmatrelvir. We discovered that ErbB1, ErbB2, and ErbB4 bind SARS-CoV-2 S1 protein and regulate viral and ACE2 internalization, and they are required for VEEV infection. In human lung organoids, lapatinib protected from SARSCoV-2-induced activation of ErbB-regulated pathways implicated in non-infectious lung injury, proinflammatory cytokine production, and epithelial barrier injury. Lapatinib suppressed VEEV replication, cytokine production, and disruption of bloodbrain barrier integrity in microfluidics-based human neurovascular units, and reduced mortality in a lethal infection murine model. We validated lapatinib-mediated inhibition of ErbB activity as an important mechanism of antiviral action. These findings reveal regulation of viral replication, inflammation, and tissue injury via ErbBs and establish a proof of principle for a repurposed, ErbB-targeted approach to combat emerging viruses., Introduction Acute emerging viral infections can cause epidemics and pandemics and thus pose major threats to human health. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has spread Authorship note: SS [...]
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- 2023
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6. 2021 Taxonomic update of phylum Negarnaviricota (Riboviria: Orthornavirae), including the large orders Bunyavirales and Mononegavirales
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Kuhn, Jens H., Adkins, Scott, Agwanda, Bernard R., Al Kubrusli, Rim, Alkhovsky, Sergey V., Amarasinghe, Gaya K., Avšič-Županc, Tatjana, Ayllón, María A., Bahl, Justin, Balkema-Buschmann, Anne, Ballinger, Matthew J., Basler, Christopher F., Bavari, Sina, Beer, Martin, Bejerman, Nicolas, Bennett, Andrew J., Bente, Dennis A., Bergeron, Éric, Bird, Brian H., Blair, Carol D., Blasdell, Kim R., Blystad, Dag-Ragnar, Bojko, Jamie, Borth, Wayne B., Bradfute, Steven, Breyta, Rachel, Briese, Thomas, Brown, Paul A., Brown, Judith K., Buchholz, Ursula J., Buchmeier, Michael J., Bukreyev, Alexander, Burt, Felicity, Büttner, Carmen, Calisher, Charles H., Cao, Mengji, Casas, Inmaculada, Chandran, Kartik, Charrel, Rémi N., Cheng, Qi, Chiaki, Yuya, Chiapello, Marco, Choi, Il-Ryong, Ciuffo, Marina, Clegg, J. Christopher S., Crozier, Ian, Dal Bó, Elena, de la Torre, Juan Carlos, de Lamballerie, Xavier, de Swart, Rik L., Debat, Humberto, Dheilly, Nolwenn M., Di Cicco, Emiliano, Di Paola, Nicholas, Di Serio, Francesco, Dietzgen, Ralf G., Digiaro, Michele, Dolnik, Olga, Drebot, Michael A., Drexler, J. Felix, Dundon, William G., Duprex, W. Paul, Dürrwald, Ralf, Dye, John M., Easton, Andrew J., Ebihara, Hideki, Elbeaino, Toufic, Ergünay, Koray, Ferguson, Hugh W., Fooks, Anthony R., Forgia, Marco, Formenty, Pierre B. H., Fránová, Jana, Freitas-Astúa, Juliana, Fu, Jingjing, Fürl, Stephanie, Gago-Zachert, Selma, Gāo, George Fú, García, María Laura, García-Sastre, Adolfo, Garrison, Aura R., Gaskin, Thomas, Gonzalez, Jean-Paul J., Griffiths, Anthony, Goldberg, Tony L., Groschup, Martin H., Günther, Stephan, Hall, Roy A., Hammond, John, Han, Tong, Hepojoki, Jussi, Hewson, Roger, Hong, Jiang, Hong, Ni, Hongo, Seiji, Horie, Masayuki, Hu, John S., Hu, Tao, Hughes, Holly R., Hüttner, Florian, Hyndman, Timothy H., Ilyas, M., Jalkanen, Risto, Jiāng, Dàohóng, Jonson, Gilda B., Junglen, Sandra, Kadono, Fujio, Kaukinen, Karia H., Kawate, Michael, Klempa, Boris, Klingström, Jonas, Kobinger, Gary, Koloniuk, Igor, Kondō, Hideki, Koonin, Eugene V., Krupovic, Mart, Kubota, Kenji, Kurath, Gael, Laenen, Lies, Lambert, Amy J., Langevin, Stanley L., Lee, Benhur, Lefkowitz, Elliot J., Leroy, Eric M., Li, Shaorong, Li, Longhui, Lǐ, Jiànróng, Liu, Huazhen, Lukashevich, Igor S., Maes, Piet, de Souza, William Marciel, Marklewitz, Marco, Marshall, Sergio H., Marzano, Shin-Yi L., Massart, Sebastien, McCauley, John W., Melzer, Michael, Mielke-Ehret, Nicole, Miller, Kristina M., Ming, Tobi J., Mirazimi, Ali, Mordecai, Gideon J., Mühlbach, Hans-Peter, Mühlberger, Elke, Naidu, Rayapati, Natsuaki, Tomohide, Navarro, José A., Netesov, Sergey V., Neumann, Gabriele, Nowotny, Norbert, Nunes, Márcio R. T., Olmedo-Velarde, Alejandro, Palacios, Gustavo, Pallás, Vicente, Pályi, Bernadett, Papa, Anna, Paraskevopoulou, Sofia, Park, Adam C., Parrish, Colin R., Patterson, David A., Pauvolid-Corrêa, Alex, Pawęska, Janusz T., Payne, Susan, Peracchio, Carlotta, Pérez, Daniel R., Postler, Thomas S., Qi, Liying, Radoshitzky, Sheli R., Resende, Renato O., Reyes, Carina A., Rima, Bertus K., Luna, Gabriel Robles, Romanowski, Víctor, Rota, Paul, Rubbenstroth, Dennis, Rubino, Luisa, Runstadler, Jonathan A., Sabanadzovic, Sead, Sall, Amadou Alpha, Salvato, Maria S., Sang, Rosemary, Sasaya, Takahide, Schulze, Angela D., Schwemmle, Martin, Shi, Mang, Shí, Xiǎohóng, Shí, Zhènglì, Shimomoto, Yoshifumi, Shirako, Yukio, Siddell, Stuart G., Simmonds, Peter, Sironi, Manuela, Smagghe, Guy, Smither, Sophie, Song, Jin-Won, Spann, Kirsten, Spengler, Jessica R., Stenglein, Mark D., Stone, David M., Sugano, Jari, Suttle, Curtis A., Tabata, Amy, Takada, Ayato, Takeuchi, Shigeharu, Tchouassi, David P., Teffer, Amy, Tesh, Robert B., Thornburg, Natalie J., Tomitaka, Yasuhiro, Tomonaga, Keizō, Tordo, Noël, Torto, Baldwyn, Towner, Jonathan S., Tsuda, Shinya, Tu, Changchun, Turina, Massimo, Tzanetakis, Ioannis E., Uchida, Janice, Usugi, Tomio, Vaira, Anna Maria, Vallino, Marta, van den Hoogen, Bernadette, Varsani, Arvind, Vasilakis, Nikos, Verbeek, Martin, von Bargen, Susanne, Wada, Jiro, Wahl, Victoria, Walker, Peter J., Wang, Lin-Fa, Wang, Guoping, Wang, Yanxiang, Wang, Yaqin, Waqas, Muhammad, Wèi, Tàiyún, Wen, Shaohua, Whitfield, Anna E., Williams, John V., Wolf, Yuri I., Wu, Jiangxiang, Xu, Lei, Yanagisawa, Hironobu, Yang, Caixia, Yang, Zuokun, Zerbini, F. Murilo, Zhai, Lifeng, Zhang, Yong-Zhen, Zhang, Song, Zhang, Jinguo, Zhang, Zhe, and Zhou, Xueping
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- 2021
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7. Correction to: 2021 Taxonomic update of phylum Negarnaviricota (Riboviria: Orthornavirae), including the large orders Bunyavirales and Mononegavirales
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Kuhn, Jens H., Adkins, Scott, Agwanda, Bernard R., Al Kubrusli, Rim, Alkhovsky, Sergey V., Amarasinghe, Gaya K., Avšič-Županc, Tatjana, Ayllón, María A., Bahl, Justin, Balkema-Buschmann, Anne, Ballinger, Matthew J., Basler, Christopher F., Bavari, Sina, Beer, Martin, Bejerman, Nicolas, Bennett, Andrew J., Bente, Dennis A., Bergeron, Éric, Bird, Brian H., Blair, Carol D., Blasdell, Kim R., Blystad, Dag-Ragnar, Bojko, Jamie, Borth, Wayne B., Bradfute, Steven, Breyta, Rachel, Briese, Thomas, Brown, Paul A., Brown, Judith K., Buchholz, Ursula J., Buchmeier, Michael J., Bukreyev, Alexander, Burt, Felicity, Büttner, Carmen, Calisher, Charles H., Cao, Mengji, Casas, Inmaculada, Chandran, Kartik, Charrel, Rémi N., Cheng, Qi, Chiaki, Yuya, Chiapello, Marco, Choi, Il-Ryong, Ciuffo, Marina, Clegg, J. Christopher S., Crozier, Ian, Dal Bó, Elena, de la Torre, Juan Carlos, de Lamballerie, Xavier, de Swart, Rik L., Debat, Humberto, Dheilly, Nolwenn M., Di Cicco, Emiliano, Di Paola, Nicholas, Di Serio, Francesco, Dietzgen, Ralf G., Digiaro, Michele, Dolnik, Olga, Drebot, Michael A., Drexler, J. Felix, Dundon, William G., Duprex, W. Paul, Dürrwald, Ralf, Dye, John M., Easton, Andrew J., Ebihara, Hideki, Elbeaino, Toufic, Ergünay, Koray, Ferguson, Hugh W., Fooks, Anthony R., Forgia, Marco, Formenty, Pierre B. H., Fránová, Jana, Freitas-Astúa, Juliana, Fu, Jingjing, Fürl, Stephanie, Gago-Zachert, Selma, Gāo, George Fú, García, María Laura, García-Sastre, Adolfo, Garrison, Aura R., Gaskin, Thomas, Gonzalez, Jean-Paul J., Griffiths, Anthony, Goldberg, Tony L., Groschup, Martin H., Günther, Stephan, Hall, Roy A., Hammond, John, Han, Tong, Hepojoki, Jussi, Hewson, Roger, Hong, Jiang, Hong, Ni, Hongo, Seiji, Horie, Masayuki, Hu, John S., Hu, Tao, Hughes, Holly R., Hüttner, Florian, Hyndman, Timothy H., Ilyas, M., Jalkanen, Risto, Jiāng, Dàohóng, Jonson, Gilda B., Junglen, Sandra, Kadono, Fujio, Kaukinen, Karia H., Kawate, Michael, Klempa, Boris, Klingström, Jonas, Kobinger, Gary, Koloniuk, Igor, Kondō, Hideki, Koonin, Eugene V., Krupovic, Mart, Kubota, Kenji, Kurath, Gael, Laenen, Lies, Lambert, Amy J., Langevin, Stanley L., Lee, Benhur, Lefkowitz, Elliot J., Leroy, Eric M., Li, Shaorong, Li, Longhui, Lǐ, Jiànróng, Liu, Huazhen, Lukashevich, Igor S., Maes, Piet, de Souza, William Marciel, Marklewitz, Marco, Marshall, Sergio H., Marzano, Shin-Yi L., Massart, Sebastien, McCauley, John W., Melzer, Michael, Mielke-Ehret, Nicole, Miller, Kristina M., Ming, Tobi J., Mirazimi, Ali, Mordecai, Gideon J., Mühlbach, Hans-Peter, Mühlberger, Elke, Naidu, Rayapati, Natsuaki, Tomohide, Navarro, José A., Netesov, Sergey V., Neumann, Gabriele, Nowotny, Norbert, Nunes, Márcio R. T., Olmedo-Velarde, Alejandro, Palacios, Gustavo, Pallás, Vicente, Pályi, Bernadett, Papa, Anna, Paraskevopoulou, Sofia, Park, Adam C., Parrish, Colin R., Patterson, David A., Pauvolid-Corrêa, Alex, Pawęska, Janusz T., Payne, Susan, Peracchio, Carlotta, Pérez, Daniel R., Postler, Thomas S., Qi, Liying, Radoshitzky, Sheli R., Resende, Renato O., Reyes, Carina A., Rima, Bertus K., Luna, Gabriel Robles, Romanowski, Víctor, Rota, Paul, Rubbenstroth, Dennis, Rubino, Luisa, Runstadler, Jonathan A., Sabanadzovic, Sead, Sall, Amadou Alpha, Salvato, Maria S., Sang, Rosemary, Sasaya, Takahide, Schulze, Angela D., Schwemmle, Martin, Shi, Mang, Shí, Xiǎohóng, Shí, Zhènglì, Shimomoto, Yoshifumi, Shirako, Yukio, Siddell, Stuart G., Simmonds, Peter, Sironi, Manuela, Smagghe, Guy, Smither, Sophie, Song, Jin-Won, Spann, Kirsten, Spengler, Jessica R., Stenglein, Mark D., Stone, David M., Sugano, Jari, Suttle, Curtis A., Tabata, Amy, Takada, Ayato, Takeuchi, Shigeharu, Tchouassi, David P., Teffer, Amy, Tesh, Robert B., Thornburg, Natalie J., Tomitaka, Yasuhiro, Tomonaga, Keizō, Tordo, Noël, Torto, Baldwyn, Towner, Jonathan S., Tsuda, Shinya, Tu, Changchun, Turina, Massimo, Tzanetakis, Ioannis E., Uchida, Janice, Usugi, Tomio, Vaira, Anna Maria, Vallino, Marta, van den Hoogen, Bernadette, Varsani, Arvind, Vasilakis, Nikos, Verbeek, Martin, von Bargen, Susanne, Wada, Jiro, Wahl, Victoria, Walker, Peter J., Wang, Lin-Fa, Wang, Guoping, Wang, Yanxiang, Wang, Yaqin, Waqas, Muhammad, Wèi, Tàiyún, Wen, Shaohua, Whitfield, Anna E., Williams, John V., Wolf, Yuri I., Wu, Jiangxiang, Xu, Lei, Yanagisawa, Hironobu, Yang, Caixia, Yang, Zuokun, Zerbini, F. Murilo, Zhai, Lifeng, Zhang, Yong-Zhen, Zhang, Song, Zhang, Jinguo, Zhang, Zhe, and Zhou, Xueping
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- 2021
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8. Long-term Sudan Virus Ebola Survivors Maintain Multiple Antiviral Defense Mechanisms.
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Sobarzo, Ariel, Moné, Yves, Lang, Steven, Gelkop, Sigal, Brangel, Polina, Kuehne, Ana I, McKendry, Rachel A, Mell, Joshua Chang, Ahmed, Azad, Davis, Claytus, Dye, John M, Lutwama, Julius Julian, Lobel, Leslie, Veas, Francisco, and Ehrlich, Garth D
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MONONUCLEAR leukocytes ,IMMUNOLOGIC memory ,IMMUNE response ,EBOLA virus ,NATURAL immunity - Abstract
Background The critical issues of sustained memory immunity following ebolavirus disease among long-term survivors are still unclear. Methods Here, we examine virus-specific immune and inflammatory responses following in vitro challengd in 12 Sudan virus (SUDV) long-term survivors from Uganda's 2000–2001 Gulu outbreak, 15 years after recovery. Total RNA from isolated SUDV-stimulated and unstimulated peripheral blood mononuclear cells was extracted and analyzed. Matched serum samples were also collected to determine SUDV IgG levels and functionality. Results We detected persistent humoral (58%, 7 of 12) and cellular (33%, 4 of 12) immune responses in SUDV long-term survivors and identified critical molecular mechanisms of innate and adaptive immunity. Gene expression in immune pathways, the interferon signaling system, antiviral defense response, and activation and regulation of T- and B-cell responses were observed. SUDV long-term survivors also maintained robust virus-specific IgG antibodies capable of polyfunctional responses, including neutralizing and innate Fc effector functions. Conclusions Data integration identified significant correlations among humoral and cellular immune responses and pinpointed a specific innate and adaptive gene expression signature associated with long-lasting immunity. This could help identify natural and vaccine correlates of protection against ebolavirus disease. [ABSTRACT FROM AUTHOR]
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- 2024
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9. Development of an antibody cocktail for treatment of Sudan virus infection
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Herbert, Andrew S., Froude, Jeffery W., Ortiz, Ramon A., Kuehne, Ana I., Dorosky, Danielle E., Bakken, Russell R., Zak, Samantha E., Josleyn, Nicole M., Musiychuk, Konstantin, Jones, R. Mark, Green, Brian, Streatfield, Stephen J., Wec, Anna Z., Bohorova, Natasha, Bohorov, Ognian, Kim, Do H., Pauly, Michael H., Velasco, Jesus, Whaley, Kevin J., Stonier, Spencer W., Bornholdt, Zachary A., Chandran, Kartik, Zeitlin, Larry, Sampey, Darryl, Yusibov, Vidadi, and Dye, John M.
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- 2020
10. Convalescent plasma anti-SARS-CoV-2 spike protein ectodomain and receptor-binding domain IgG correlate with virus neutralization
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Salazar, Eric, Kuchipudi, Suresh V., Christensen, Paul A., Eagar, Todd, Yi, Xin, Zhao, Picheng, Jin, Zhicheng, Long, S. Wesley, Olsen, Randall J., Chen, Jian, Castillo, Brian, Leveque, Christopher, Towers, Dalton, Lavinder, Jason, Gollihar, Jimmy, Cardona, Jose, Ippolito, Gregory, Nissly, Ruth, Bird, Ian, Greenawalt, Denver, Rossi, Randall M., Gontu, Abhinay, Srinivasan, Sreenidhi, Poojary, Indira, Cattadori, Isabella M., Hudson, Peter J., Josleyn, Nicole M., Prugar, Laura, Huie, Kathleen, Herbert, Andrew, Bernard, David W., Dye, John M., Kapur, Vivek, and Musser, James M.
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Viral proteins -- Health aspects ,Epidemics -- Control -- United States ,COVID-19 -- Control ,Immunoglobulin G -- Health aspects ,Health care industry - Abstract
The newly emerged severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) highlights the urgent need for assays that detect protective levels of neutralizing antibodies. We studied the relationship among anti-spike ectodomain (anti-ECD), antireceptor-binding domain (anti-RBD) IgG titers, and SARS-CoV-2 virus neutralization (VN) titers generated by 2 in vitro assays using convalescent plasma samples from 68 patients with COVID-19. We report a strong positive correlation between both plasma anti-RBD and anti-ECD IgG titers and in vitro VN titers. The probability of a VN titer of [greater than or equal to] 160, the FDA-recommended level for convalescent plasma used for COVID-19 treatment, was [greater than or equal to] 80% when anti-RBD or anti-ECD titers were [greater than or equal to] 1:1350. Of all donors, 37% lacked VN titers of [greater than or equal to] 160. Dyspnea, hospitalization, and disease severity were significantly associated with higher VN titer. Frequent donation of convalescent plasma did not significantly decrease VN or IgG titers. Analysis of 2814 asymptomatic adults found 73 individuals with anti-ECD IgG titers of [greater than or equal to] 1:50 and strong positive correlation with anti-RBD and VN titers. Fourteen of these individuals had VN titers of [greater than or equal to] 1:160, and all of them had anti-RBD titers of [greater than or equal to] 1:1350. We conclude that anti-RBD or anti-ECD IgG titers can serve as a surrogate for VN titers to identify suitable plasma donors. Plasma anti-RBD or anti-ECD titers of [greater than or equal to] 1:1350 may provide critical information about protection against COVID-19 disease., Introduction The recently emerged severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a novel coronavirus that causes coronavirus disease 2019 (COVID-19) disease, has spread globally and is now responsible for massive [...]
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- 2020
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11. Design and characterization of protective pan-ebolavirus and pan-filovirus bispecific antibodies.
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Wirchnianski, Ariel S., Nyakatura, Elisabeth K., Herbert, Andrew S., Kuehne, Ana I., Abbasi, Shawn A., Florez, Catalina, Storm, Nadia, McKay, Lindsay G. A., Dailey, Leandrew, Kuang, Erin, Abelson, Dafna M., Wec, Anna Z., Chakraborti, Srinjoy, Holtsberg, Frederick W., Shulenin, Sergey, Bornholdt, Zachary A., Aman, M. Javad, Honko, Anna N., Griffiths, Anthony, and Dye, John M.
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BISPECIFIC antibodies ,MARBURG virus ,EBOLA virus ,HEMORRHAGIC fever ,FILOVIRIDAE ,PROTEIN engineering - Abstract
Monoclonal antibodies (mAbs) are an important class of antiviral therapeutics. MAbs are highly selective, well tolerated, and have long in vivo half-life as well as the capacity to induce immune-mediated virus clearance. Their activities can be further enhanced by integration of their variable fragments (Fvs) into bispecific antibodies (bsAbs), affording simultaneous targeting of multiple epitopes to improve potency and breadth and/or to mitigate against viral escape by a single mutation. Here, we explore a bsAb strategy for generation of pan-ebolavirus and pan-filovirus immunotherapeutics. Filoviruses, including Ebola virus (EBOV), Sudan virus (SUDV), and Marburg virus (MARV), cause severe hemorrhagic fever. Although there are two FDA-approved mAb therapies for EBOV infection, these do not extend to other filoviruses. Here, we combine Fvs from broad ebolavirus mAbs to generate novel pan-ebolavirus bsAbs that are potently neutralizing, confer protection in mice, and are resistant to viral escape. Moreover, we combine Fvs from pan-ebolavirus mAbs with those of protective MARV mAbs to generate pan-filovirus protective bsAbs. These results provide guidelines for broad antiviral bsAb design and generate new immunotherapeutic candidates. Author summary: Filoviruses, such as Ebola virus and Marburg virus (EBOV and MARV, respectively), cause severe hemorrhagic fever with a high mortality rate in humans. Monoclonal antibodies (mAbs) are effective treatments for filovirus infection, but current therapies have limited breadth. Furthermore, a single mAb is susceptible to development of resistance. Here, we used protein engineering to create "bispecific" antibodies in which activities of two different mAbs were combined into one. These bispecific antibodies had broad activity, in one case providing protection against lethal challenge by two distant clades of filoviruses (EBOV and MARV). The bispecific antibodies were also less susceptible to resistance mutations. This work provides a roadmap for development of new bispecific antibody therapies for filoviruses. [ABSTRACT FROM AUTHOR]
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- 2024
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12. 2020 taxonomic update for phylum Negarnaviricota (Riboviria: Orthornavirae), including the large orders Bunyavirales and Mononegavirales
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Kuhn, Jens H., Adkins, Scott, Alioto, Daniela, Alkhovsky, Sergey V., Amarasinghe, Gaya K., Anthony, Simon J., Avšič-Županc, Tatjana, Ayllón, María A., Bahl, Justin, Balkema-Buschmann, Anne, Ballinger, Matthew J., Bartonička, Tomáš, Basler, Christopher, Bavari, Sina, Beer, Martin, Bente, Dennis A., Bergeron, Éric, Bird, Brian H., Blair, Carol, Blasdell, Kim R., Bradfute, Steven B., Breyta, Rachel, Briese, Thomas, Brown, Paul A., Buchholz, Ursula J., Buchmeier, Michael J., Bukreyev, Alexander, Burt, Felicity, Buzkan, Nihal, Calisher, Charles H., Cao, Mengji, Casas, Inmaculada, Chamberlain, John, Chandran, Kartik, Charrel, Rémi N., Chen, Biao, Chiumenti, Michela, Choi, Il-Ryong, Clegg, J. Christopher S., Crozier, Ian, da Graça, John V., Dal Bó, Elena, Dávila, Alberto M. R., de la Torre, Juan Carlos, de Lamballerie, Xavier, de Swart, Rik L., Di Bello, Patrick L., Di Paola, Nicholas, Di Serio, Francesco, Dietzgen, Ralf G., Digiaro, Michele, Dolja, Valerian V., Dolnik, Olga, Drebot, Michael A., Drexler, Jan Felix, Dürrwald, Ralf, Dufkova, Lucie, Dundon, William G., Duprex, W. Paul, Dye, John M., Easton, Andrew J., Ebihara, Hideki, Elbeaino, Toufic, Ergünay, Koray, Fernandes, Jorlan, Fooks, Anthony R., Formenty, Pierre B. H., Forth, Leonie F., Fouchier, Ron A. M., Freitas-Astúa, Juliana, Gago-Zachert, Selma, Gāo, George Fú, García, María Laura, García-Sastre, Adolfo, Garrison, Aura R., Gbakima, Aiah, Goldstein, Tracey, Gonzalez, Jean-Paul J., Griffiths, Anthony, Groschup, Martin H., Günther, Stephan, Guterres, Alexandro, Hall, Roy A., Hammond, John, Hassan, Mohamed, Hepojoki, Jussi, Hepojoki, Satu, Hetzel, Udo, Hewson, Roger, Hoffmann, Bernd, Hongo, Seiji, Höper, Dirk, Horie, Masayuki, Hughes, Holly R., Hyndman, Timothy H., Jambai, Amara, Jardim, Rodrigo, Jiāng, Dàohóng, Jin, Qi, Jonson, Gilda B., Junglen, Sandra, Karadağ, Serpil, Keller, Karen E., Klempa, Boris, Klingström, Jonas, Kobinger, Gary, Kondō, Hideki, Koonin, Eugene V., Krupovic, Mart, Kurath, Gael, Kuzmin, Ivan V., Laenen, Lies, Lamb, Robert A., Lambert, Amy J., Langevin, Stanley L., Lee, Benhur, Lemos, Elba R. S., Leroy, Eric M., Li, Dexin, Lǐ, Jiànróng, Liang, Mifang, Liú, Wénwén, Liú, Yàn, Lukashevich, Igor S., Maes, Piet, Marciel de Souza, William, Marklewitz, Marco, Marshall, Sergio H., Martelli, Giovanni P., Martin, Robert R., Marzano, Shin-Yi L., Massart, Sébastien, McCauley, John W., Mielke-Ehret, Nicole, Minafra, Angelantonio, Minutolo, Maria, Mirazimi, Ali, Mühlbach, Hans-Peter, Mühlberger, Elke, Naidu, Rayapati, Natsuaki, Tomohide, Navarro, Beatriz, Navarro, José A., Netesov, Sergey V., Neumann, Gabriele, Nowotny, Norbert, Nunes, Márcio R. T., Nylund, Are, Økland, Arnfinn L., Oliveira, Renata C., Palacios, Gustavo, Pallas, Vicente, Pályi, Bernadett, Papa, Anna, Parrish, Colin R., Pauvolid-Corrêa, Alex, Pawęska, Janusz T., Payne, Susan, Pérez, Daniel R., Pfaff, Florian, Radoshitzky, Sheli R., Rahman, Aziz-ul, Ramos-González, Pedro L., Resende, Renato O., Reyes, Carina A., Rima, Bertus K., Romanowski, Víctor, Robles Luna, Gabriel, Rota, Paul, Rubbenstroth, Dennis, Runstadler, Jonathan A., Ruzek, Daniel, Sabanadzovic, Sead, Salát, Jiří, Sall, Amadou Alpha, Salvato, Maria S., Sarpkaya, Kamil, Sasaya, Takahide, Schwemmle, Martin, Shabbir, Muhammad Z., Shí, Xiǎohóng, Shí, Zhènglì, Shirako, Yukio, Simmonds, Peter, Širmarová, Jana, Sironi, Manuela, Smither, Sophie, Smura, Teemu, Song, Jin-Won, Spann, Kirsten M., Spengler, Jessica R., Stenglein, Mark D., Stone, David M., Straková, Petra, Takada, Ayato, Tesh, Robert B., Thornburg, Natalie J., Tomonaga, Keizō, Tordo, Noël, Towner, Jonathan S., Turina, Massimo, Tzanetakis, Ioannis, Ulrich, Rainer G., Vaira, Anna Maria, van den Hoogen, Bernadette, Varsani, Arvind, Vasilakis, Nikos, Verbeek, Martin, Wahl, Victoria, Walker, Peter J., Wang, Hui, Wang, Jianwei, Wang, Xifeng, Wang, Lin-Fa, Wèi, Tàiyún, Wells, Heather, Whitfield, Anna E., Williams, John V., Wolf, Yuri I., Wú, Zhìqiáng, Yang, Xin, Yáng, Xīnglóu, Yu, Xuejie, Yutin, Natalya, Zerbini, F. Murilo, Zhang, Tong, Zhang, Yong-Zhen, Zhou, Guohui, and Zhou, Xueping
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- 2020
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13. Ebola Virus VP40 Modulates Cell Cycle and Biogenesis of Extracellular Vesicles
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Pleet, Michelle L., Erickson, James, DeMarino, Catherine, Barclay, Robert A., Cowen, Maria, Lepene, Benjamin, Liang, Janie, Kuhn, Jens H., Prugar, Laura, Stonier, Spencer W., Dye, John M., Zhou, Weidong, Liotta, Lance A., Aman, M. Javad, and Kashanchi, Fatah
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- 2018
14. Multiple viral proteins and immune response pathways act to generate robust long-term immunity in Sudan virus survivors
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Sobarzo, Ariel, Stonier, Spencer W., Radinsky, Olga, Gelkop, Sigal, Kuehne, Ana I., Edri, Avishay, Herbert, Andrew S., Fedida-Metula, Shlomit, Lutwama, Julius Julian, Yavelsky, Victoria, Davis, Claytus, Porgador, Angel, Dye, John M., and Lobel, Leslie
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- 2019
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15. SARS-CoV-2 Aerosol and Intranasal Exposure Models in Ferrets.
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Zumbrun, Elizabeth E., Zak, Samantha E., Lee, Eric D., Bowling, Philip A., Ruiz, Sara I., Zeng, Xiankun, Koehler, Jeffrey W., Delp, Korey L., Bakken, Russel R., Hentschel, Shannon S., Bloomfield, Holly A., Ricks, Keersten M., Clements, Tamara L., Babka, April M., Dye, John M., and Herbert, Andrew S.
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SARS-CoV-2 ,MICROBIOLOGICAL aerosols ,FERRET ,TURBINATE bones ,VIRAL antigens - Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the worldwide COVID-19 pandemic. Animal models are extremely helpful for testing vaccines and therapeutics and for dissecting the viral and host factors that contribute to disease severity and transmissibility. Here, we report the assessment and comparison of intranasal and small particle (~3 µm) aerosol SARS-CoV-2 exposure in ferrets. The primary endpoints for analysis were clinical signs of disease, recovery of the virus in the upper respiratory tract, and the severity of damage within the respiratory tract. This work demonstrated that ferrets were productively infected with SARS-CoV-2 following either intranasal or small particle aerosol exposure. SARS-CoV-2 infection of ferrets resulted in an asymptomatic disease course following either intranasal or small particle aerosol exposure, with no clinical signs, significant weight loss, or fever. In both aerosol and intranasal ferret models, SARS-CoV-2 replication, viral genomes, and viral antigens were detected within the upper respiratory tract, with little to no viral material detected in the lungs. The ferrets exhibited a specific IgG immune response to the SARS-CoV-2 full spike protein. Mild pathological findings included inflammation, necrosis, and edema within nasal turbinates, which correlated to positive immunohistochemical staining for the SARS-CoV-2 virus. Environmental sampling was performed following intranasal exposure of ferrets, and SARS-CoV-2 genomic material was detected on the feeders and nesting areas from days 2–10 post-exposure. We conclude that both intranasal and small particle aerosol ferret models displayed measurable parameters that could be utilized for future studies, including transmission studies and testing SARS-CoV-2 vaccines and therapeutics. [ABSTRACT FROM AUTHOR]
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- 2023
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16. Anti–Ebola Virus Antibody Levels in Convalescent Plasma and Viral Load After Plasma Infusion in Patients With Ebola Virus Disease
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Brown, Jerry F., Dye, John M., Tozay, Sam, Jeh-Mulbah, Gertrude, Wohl, David A., Fischer, William A., Cunningham, Coleen K., Rowe, Kathleen, Zacharias, Peter, van Hasselt, James, Norwood, David A., Thielman, Nathan M., Zak, Samantha E., and Hoover, David L.
- Published
- 2018
17. Enhancement of Ebola virus infection by seminal amyloid fibrils
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Bart, Stephen M., Cohen, Courtney, Dye, John M., Shorter, James, and Bates, Paul
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- 2018
18. Recombinant proteins of Zaire ebolavirus induce potent humoral and cellular immune responses and protect against live virus infection in mice
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Lehrer, Axel T., Wong, Teri-Ann S., Lieberman, Michael M., Humphreys, Tom, Clements, David E., Bakken, Russell R., Hart, Mary Kate, Pratt, William D., and Dye, John M.
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- 2018
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19. Taxonomy of the order Mononegavirales: update 2019
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Amarasinghe, Gaya K., Ayllón, María A., Bào, Yīmíng, Basler, Christopher F., Bavari, Sina, Blasdell, Kim R., Briese, Thomas, Brown, Paul A., Bukreyev, Alexander, Balkema-Buschmann, Anne, Buchholz, Ursula J., Chabi-Jesus, Camila, Chandran, Kartik, Chiapponi, Chiara, Crozier, Ian, de Swart, Rik L., Dietzgen, Ralf G., Dolnik, Olga, Drexler, Jan F., Dürrwald, Ralf, Dundon, William G., Duprex, W. Paul, Dye, John M., Easton, Andrew J., Fooks, Anthony R., Formenty, Pierre B. H., Fouchier, Ron A. M., Freitas-Astúa, Juliana, Griffiths, Anthony, Hewson, Roger, Horie, Masayuki, Hyndman, Timothy H., Jiāng, Dàohóng, Kitajima, Elliott W., Kobinger, Gary P., Kondō, Hideki, Kurath, Gael, Kuzmin, Ivan V., Lamb, Robert A., Lavazza, Antonio, Lee, Benhur, Lelli, Davide, Leroy, Eric M., Lǐ, Jiànróng, Maes, Piet, Marzano, Shin-Yi L., Moreno, Ana, Mühlberger, Elke, Netesov, Sergey V., Nowotny, Norbert, Nylund, Are, Økland, Arnfinn L., Palacios, Gustavo, Pályi, Bernadett, Pawęska, Janusz T., Payne, Susan L., Prosperi, Alice, Ramos-González, Pedro Luis, Rima, Bertus K., Rota, Paul, Rubbenstroth, Dennis, Shī, Mǎng, Simmonds, Peter, Smither, Sophie J., Sozzi, Enrica, Spann, Kirsten, Stenglein, Mark D., Stone, David M., Takada, Ayato, Tesh, Robert B., Tomonaga, Keizō, Tordo, Noël, Towner, Jonathan S., van den Hoogen, Bernadette, Vasilakis, Nikos, Wahl, Victoria, Walker, Peter J., Wang, Lin-Fa, Whitfield, Anna E., Williams, John V., Zerbini, F. Murilo, Zhāng, Tāo, Zhang, Yong-Zhen, and Kuhn, Jens H.
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- 2019
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20. Taxonomy of the order Mononegavirales: second update 2018
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Maes, Piet, Amarasinghe, Gaya K., Ayllón, María A., Basler, Christopher F., Bavari, Sina, Blasdell, Kim R., Briese, Thomas, Brown, Paul A., Bukreyev, Alexander, Balkema-Buschmann, Anne, Buchholz, Ursula J., Chandran, Kartik, Crozier, Ian, de Swart, Rik L., Dietzgen, Ralf G., Dolnik, Olga, Domier, Leslie L., Drexler, Jan F., Dürrwald, Ralf, Dundon, William G., Duprex, W. Paul, Dye, John M., Easton, Andrew J., Fooks, Anthony R., Formenty, Pierre B. H., Fouchier, Ron A. M., Freitas-Astúa, Juliana, Ghedin, Elodie, Griffiths, Anthony, Hewson, Roger, Horie, Masayuki, Hurwitz, Julia L., Hyndman, Timothy H., Jiāng, Dàohóng, Kobinger, Gary P., Kondō, Hideki, Kurath, Gael, Kuzmin, Ivan V., Lamb, Robert A., Lee, Benhur, Leroy, Eric M., Lǐ, Jiànróng, Marzano, Shin-Yi L., Mühlberger, Elke, Netesov, Sergey V., Nowotny, Norbert, Palacios, Gustavo, Pályi, Bernadett, Pawęska, Janusz T., Payne, Susan L., Rima, Bertus K., Rota, Paul, Rubbenstroth, Dennis, Simmonds, Peter, Smither, Sophie J., Song, Qisheng, Song, Timothy, Spann, Kirsten, Stenglein, Mark D., Stone, David M., Takada, Ayato, Tesh, Robert B., Tomonaga, Keizō, Tordo, Noël, Towner, Jonathan S., van den Hoogen, Bernadette, Vasilakis, Nikos, Wahl, Victoria, Walker, Peter J., Wang, David, Wang, Lin-Fa, Whitfield, Anna E., Williams, John V., Yè, Gōngyín, Zerbini, F. Murilo, Zhang, Yong-Zhen, and Kuhn, Jens H.
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- 2019
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21. Structural basis of broad ebolavirus neutralization by a human survivor antibody
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West, Brandyn R., Wec, Anna Z., Moyer, Crystal L., Fusco, Marnie L., Ilinykh, Philipp A., Huang, Kai, Wirchnianski, Ariel S., James, Rebekah M., Herbert, Andrew S., Hui, Sean, Goodwin, Eileen, Howell, Katie A., Kailasan, Shweta, Aman, M. Javad, Walker, Laura M., Dye, John M., Bukreyev, Alexander, Chandran, Kartik, and Saphire, Erica Ollmann
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- 2019
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22. Protocadherin-1 is essential for cell entry by New World hantaviruses
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Jangra, Rohit K., Herbert, Andrew S., Li, Rong, Jae, Lucas T., Kleinfelter, Lara M., Slough, Megan M., Barker, Sarah L., Guardado-Calvo, Pablo, Román-Sosa, Gleyder, Dieterle, M. Eugenia, Kuehne, Ana I., Muena, Nicolás A., Wirchnianski, Ariel S., Nyakatura, Elisabeth K., Fels, J. Maximilian, Ng, Melinda, Mittler, Eva, Pan, James, Bharrhan, Sushma, Wec, Anna Z., Lai, Jonathan R., Sidhu, Sachdev S., Tischler, Nicole D., Rey, Félix A., Moffat, Jason, Brummelkamp, Thijn R., Wang, Zhongde, Dye, John M., and Chandran, Kartik
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- 2018
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23. Possibility and Challenges of Conversion of Current Virus Species Names to Linnaean Binomials
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Postler, Thomas S., Clawson, Anna N., Amarasinghe, Gaya K., Basler, Christopher F., Bavari, Sbina, Benkő, Mária, Blasdell, Kim R., Briese, Thomas, Buchmeier, Michael J., Bukreyev, Alexander, Calisher, Charles H., Chandran, Kartik, Charrel, Rémi, Clegg, Christopher S., Collins, Peter L., de la Torre, Juan Carlos, DeRisi, Joseph L., Dietzgen, Ralf G., Dolnik, Olga, Dürrwald, Ralf, Dye, John M., Easton, Andrew J., Emonet, Sébastian, Formenty, Pierre, Fouchier, Ron A. M., Ghedin, Elodie, Gonzalez, Jean-Paul, Harrach, Balázs, Hewson, Roger, Horie, Masayuki, Jiāng, Dàohóng, Kobinger, Gary, Kondo, Hideki, Kropinski, Andrew M., Krupovic, Mart, Kurath, Gael, Lamb, Robert A., Leroy, Eric M., Lukashevich, Igor S., Maisner, Andrea, Mushegian, Arcady R., Netesov, Sergey V., Nowotny, Norbert, Patterson, Jean L., Payne, Susan L., Paweska, Janusz T., Peters, Clarence J., Radoshitzky, Sheli R., Rima, Bertus K., Romanowski, Victor, Rubbenstroth, Dennis, Sabanadzovic, Sead, Sanfaçon, Hélène, Salvato, Maria S., Schwemmle, Martin, Smither, Sophie J., Stenglein, Mark D., Stone, David M., Takada, Ayato, Tesh, Robert B., Tomonaga, Keizo, Tordo, Noël, Towner, Jonathan S., Vasilakis, Nikos, Volchkov, Viktor E., Wahl-Jensen, Victoria, Walker, Peter J., Wang, Lin-Fa, Varsani, Arvind, Whitfield, Anna E., Zerbini, F. Murilo, and Kuhn, Jens H.
- Published
- 2017
24. A "Trojan horse" bispecific-antibody strategy for broad protection against ebolaviruses
- Author
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Wec, Anna Z., Nyakatura, Elisabeth K., Herbert, Andrew S., Howell, Katie A., Holtsberg, Frederick W., Bakken, Russell R., Mittler, Eva, Christin, John R., Shulenin, Sergey, Jangra, Rohit K., Bharrhan, Sushma, Kuehne, Ana I., Bornholdt, Zachary A., Flyak, Andrew I., Saphire, Erica Ollmann, Crowe, James E., Aman, M. Javad, Dye, John M., Lai, Jonathan R., and Chandran, Kartik
- Published
- 2016
25. Post-exposure immunotherapy for two ebolaviruses and Marburg virus in nonhuman primates
- Author
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Brannan, Jennifer M., He, Shihua, Howell, Katie A., Prugar, Laura I., Zhu, Wenjun, Vu, Hong, Shulenin, Sergey, Kailasan, Shweta, Raina, Henna, Wong, Gary, Rahim, Md Niaz, Banadyga, Logan, Tierney, Kevin, Zhao, Xuelian, Li, Yuxing, Holtsberg, Frederick W., Dye, John M., Qiu, Xiangguo, and Aman, M. Javad
- Published
- 2019
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26. Dengue fever and chikungunya virus infections: identification in travelers in Uganda – 2017
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Kayiwa, John T., Nankya, Annet M., Ataliba, Irene, Nassuna, Charity A., Omara, Isaac E., Koehler, Jeffrey W., Dye, John M., Mossel, Eric C., and Lutwama, Julius J.
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- 2019
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27. Taxonomy of the order Mononegavirales: update 2018
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Amarasinghe, Gaya K., Aréchiga Ceballos, Nidia G., Banyard, Ashley C., Basler, Christopher F., Bavari, Sina, Bennett, Andrew J., Blasdell, Kim R., Briese, Thomas, Bukreyev, Alexander, Caì, Yíngyún, Calisher, Charles H., Campos Lawson, Cristine, Chandran, Kartik, Chapman, Colin A., Chiu, Charles Y., Choi, Kang-Seuk, Collins, Peter L., Dietzgen, Ralf G., Dolja, Valerian V., Dolnik, Olga, Domier, Leslie L., Dürrwald, Ralf, Dye, John M., Easton, Andrew J., Ebihara, Hideki, Echevarría, Juan E., Fooks, Anthony R., Formenty, Pierre B. H., Fouchier, Ron A. M., Freuling, Conrad M., Ghedin, Elodie, Goldberg, Tony L., Hewson, Roger, Horie, Masayuki, Hyndman, Timothy H., Jiāng, Dàohóng, Kityo, Robert, Kobinger, Gary P., Kondō, Hideki, Koonin, Eugene V., Krupovic, Mart, Kurath, Gael, Lamb, Robert A., Lee, Benhur, Leroy, Eric M., Maes, Piet, Maisner, Andrea, Marston, Denise A., Mor, Sunil Kumar, Müller, Thomas, Mühlberger, Elke, Ramírez, Víctor Manuel Neira, Netesov, Sergey V., Ng, Terry Fei Fan, Nowotny, Norbert, Palacios, Gustavo, Patterson, Jean L., Pawęska, Janusz T., Payne, Susan L., Prieto, Karla, Rima, Bertus K., Rota, Paul, Rubbenstroth, Dennis, Schwemmle, Martin, Siddell, Stuart, Smither, Sophie J., Song, Qisheng, Song, Timothy, Stenglein, Mark D., Stone, David M., Takada, Ayato, Tesh, Robert B., Thomazelli, Luciano Matsumiya, Tomonaga, Keizō, Tordo, Noël, Towner, Jonathan S., Vasilakis, Nikos, Vázquez-Morón, Sonia, Verdugo, Claudio, Volchkov, Viktor E., Wahl, Victoria, Walker, Peter J., Wang, David, Wang, Lin-Fa, Wellehan, James F. X., Wiley, Michael R., Whitfield, Anna E., Wolf, Yuri I., Yè, Gōngyín, Zhāng, Yǒng-Zhèn, and Kuhn, Jens H.
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- 2018
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28. Novel Small Molecule Entry Inhibitors of Ebola Virus
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Basu, Arnab, Mills, Debra M., Mitchell, Daniel, Ndungo, Esther, Williams, John D., Herbert, Andrew S., Dye, John M., Moir, Donald T., Chandran, Kartik, Patterson, Jean L., Rong, Lijun, and Bowlin, Terry L.
- Published
- 2015
29. Interferon α/β Receptor-Deficient Mice as a Model for Ebola Virus Disease
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Brannan, Jennifer M., Froude, Jeffery W., Prugar, Laura I., Bakken, Russell R., Zak, Samantha E., Daye, Sharon P., Wilheimsen, Catherine E., and Dye, John M.
- Published
- 2015
30. Structural and mechanistic basis of neutralization by a pan-hantavirus protective antibody.
- Author
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Mittler, Eva, Serris, Alexandra, Esterman, Emma S., Florez, Catalina, Polanco, Laura C., O'Brien, Cecilia M., Slough, Megan M., Tynell, Janne, Gröning, Remigius, Sun, Yan, Abelson, Dafna M., Wec, Anna Z., Haslwanter, Denise, Keller, Markus, Ye, Chunyan, Bakken, Russel R., Jangra, Rohit K., Dye, John M., Ahlm, Clas, and Rappazzo, C. Garrett
- Subjects
MONOCLONAL antibodies ,HANTAVIRUS diseases ,VACCINE approval ,HETERODIMERS ,IMMUNOGLOBULINS ,HANTAVIRUSES ,VIRUS diseases - Abstract
Emerging rodent-borne hantaviruses cause severe diseases in humans with no approved vaccines or therapeutics. We recently isolated a monoclonal broadly neutralizing antibody (nAb) from a Puumala virus–experienced human donor. Here, we report its structure bound to its target, the Gn/Gc glycoprotein heterodimer comprising the viral fusion complex. The structure explains the broad activity of the nAb: It recognizes conserved Gc fusion loop sequences and the main chain of variable Gn sequences, thereby straddling the Gn/Gc heterodimer and locking it in its prefusion conformation. We show that the nAb's accelerated dissociation from the divergent Andes virus Gn/Gc at endosomal acidic pH limits its potency against this highly lethal virus and correct this liability by engineering an optimized variant that sets a benchmark as a candidate pan-hantavirus therapeutic. Editor's summary: Infection with hantaviruses can cause severe disease in humans, and virus-specific therapeutics and vaccines are urgently needed. Neutralizing antibodies represent a promising therapeutic option, but most antibodies fail to neutralize evolutionarily divergent hantaviruses, limiting their utility. To address this, Mittler et al. performed structural analysis on a recently identified broadly neutralizing antibody isolated from an individual who recovered from infection with an Old World hantavirus, Puumala virus. Using structural information and complementary binding, neutralization, and functional studies, the authors engineered an optimized variant of this patient-derived antibody that could protect against infection by Puumala virus and lethal challenge by Andes virus, a New World hantavirus, in rodent models. This broadly neutralizing antibody, ADI-65534, represents a potential therapeutic candidate to treat hantavirus infections. —Courtney Malo [ABSTRACT FROM AUTHOR]
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- 2023
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31. Anticancer kinase inhibitors impair intracellular viral trafficking and exert broad-spectrum antiviral effects
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Bekerman, Elena, Neveu, Gregory, Shulla, Ana, Brannan, Jennifer, Pu, Szu-Yuan, Wang, Stanley, Xiao, Fei, Barouch-Bentov, Rina, Bakken, Russell R., Mateo, Roberto, Govero, Jennifer, Nagamine, Claude M., Diamond, Michael S., De Jonghe, Steven, Herdewijn, Piet, Dye, John M., Randall, Glenn, and Einav, Shirit
- Subjects
Host-virus relationships ,Enzyme regulation -- Health aspects ,Virus diseases -- Drug therapy ,Antineoplastic agents -- Patient outcomes ,Health care industry - Abstract
Global health is threatened by emerging viral infections, which largely lack effective vaccines or therapies. Targeting host pathways that are exploited by multiple viruses could offer broad-spectrum solutions. We previously reported that AAK1 and GAK, kinase regulators of the host adaptor proteins AP1 and AP2, are essential for hepatitis C virus (HCV) infection, but the underlying mechanism and relevance to other viruses or in vivo infections remained unknown. Here, we have discovered that AP1 and AP2 cotraffic with HCV particles in live cells. Moreover, we found that multiple viruses, including dengue and Ebola, exploit AAK1 and GAK during entry and infectious virus production. In cultured cells, treatment with sunitinib and erlotinib, approved anticancer drugs that inhibit AAK1 or GAK activity, or with more selective compounds inhibited intracellular trafficking of HCV and multiple unrelated RNA viruses with a high barrier to resistance. In murine models of dengue and Ebola infection, sunitinib/erlotinib combination protected against morbidity and mortality. We validated sunitinib- and erlotinib-mediated inhibition of AAK1 and GAK activity as an important mechanism of antiviral action. Additionally, we revealed potential roles for additional kinase targets. These findings advance our understanding of virus-host interactions and establish a proof of principle for a repurposed, host-targeted approach to combat emerging viruses., Introduction A major threat to human health is posed by emerging viruses, such as dengue (DENV) and Ebola (EBOV). Dengue is estimated to infect 390 million people annually in over [...]
- Published
- 2017
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32. Taxonomy of the order Mononegavirales: update 2017
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Amarasinghe, Gaya K., Bào, Yīmíng, Basler, Christopher F., Bavari, Sina, Beer, Martin, Bejerman, Nicolás, Blasdell, Kim R., Bochnowski, Alisa, Briese, Thomas, Bukreyev, Alexander, Calisher, Charles H., Chandran, Kartik, Collins, Peter L., Dietzgen, Ralf G., Dolnik, Olga, Dürrwald, Ralf, Dye, John M., Easton, Andrew J., Ebihara, Hideki, Fang, Qi, Formenty, Pierre, Fouchier, Ron A. M., Ghedin, Elodie, Harding, Robert M., Hewson, Roger, Higgins, Colleen M., Hong, Jian, Horie, Masayuki, James, Anthony P., Jiāng, Dàohóng, Kobinger, Gary P., Kondo, Hideki, Kurath, Gael, Lamb, Robert A., Lee, Benhur, Leroy, Eric M., Li, Ming, Maisner, Andrea, Mühlberger, Elke, Netesov, Sergey V., Nowotny, Norbert, Patterson, Jean L., Payne, Susan L., Paweska, Janusz T., Pearson, Michael N., Randall, Rick E., Revill, Peter A., Rima, Bertus K., Rota, Paul, Rubbenstroth, Dennis, Schwemmle, Martin, Smither, Sophie J., Song, Qisheng, Stone, David M., Takada, Ayato, Terregino, Calogero, Tesh, Robert B., Tomonaga, Keizo, Tordo, Noël, Towner, Jonathan S., Vasilakis, Nikos, Volchkov, Viktor E., Wahl-Jensen, Victoria, Walker, Peter J., Wang, Beibei, Wang, David, Wang, Fei, Wang, Lin-Fa, Werren, John H., Whitfield, Anna E., Yan, Zhichao, Ye, Gongyin, and Kuhn, Jens H.
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- 2017
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33. Lassa virus entry requires a trigger-induced receptor switch
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Jae, Lucas T., Raaben, Matthijs, Herbert, Andrew S., Kuehne, Ana I., Wirchnianski, Ariel S., Soh, Timothy K., Stubbs, Sarah H., Janssen, Hans, Damme, Markus, Saftig, Paul, Whelan, Sean P., Dye, John M., and Brummelkamp, Thijn R.
- Published
- 2014
34. Taxonomy of the order Mononegavirales: update 2016
- Author
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Afonso, Claudio L., Amarasinghe, Gaya K., Bányai, Krisztián, Bào, Yīmíng, Basler, Christopher F., Bavari, Sina, Bejerman, Nicolás, Blasdell, Kim R., Briand, François-Xavier, Briese, Thomas, Bukreyev, Alexander, Calisher, Charles H., Chandran, Kartik, Chéng, Jiāsēn, Clawson, Anna N., Collins, Peter L., Dietzgen, Ralf G., Dolnik, Olga, Domier, Leslie L., Dürrwald, Ralf, Dye, John M., Easton, Andrew J., Ebihara, Hideki, Farkas, Szilvia L., Freitas-Astúa, Juliana, Formenty, Pierre, Fouchier, Ron A. M., Fù, Yànpíng, Ghedin, Elodie, Goodin, Michael M., Hewson, Roger, Horie, Masayuki, Hyndman, Timothy H., Jiāng, Dàohóng, Kitajima, Elliot W., Kobinger, Gary P., Kondo, Hideki, Kurath, Gael, Lamb, Robert A., Lenardon, Sergio, Leroy, Eric M., Li, Ci-Xiu, Lin, Xian-Dan, Liú, Lìjiāng, Longdon, Ben, Marton, Szilvia, Maisner, Andrea, Mühlberger, Elke, Netesov, Sergey V., Nowotny, Norbert, Patterson, Jean L., Payne, Susan L., Paweska, Janusz T., Randall, Rick E., Rima, Bertus K., Rota, Paul, Rubbenstroth, Dennis, Schwemmle, Martin, Shi, Mang, Smither, Sophie J., Stenglein, Mark D., Stone, David M., Takada, Ayato, Terregino, Calogero, Tesh, Robert B., Tian, Jun-Hua, Tomonaga, Keizo, Tordo, Noël, Towner, Jonathan S., Vasilakis, Nikos, Verbeek, Martin, Volchkov, Viktor E., Wahl-Jensen, Victoria, Walsh, John A., Walker, Peter J., Wang, David, Wang, Lin-Fa, Wetzel, Thierry, Whitfield, Anna E., Xiè, Jiǎtāo, Yuen, Kwok-Yung, Zhang, Yong-Zhen, and Kuhn, Jens H.
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- 2016
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35. Toll-like receptor 4 mediates blood-brain barrier permeability and disease in C3H mice during Venezuelan equine encephalitis virus infection
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Hollidge, Bradley S., Cohen, Courtney A., Akuoku Frimpong, Justice, Badger, Catherine V., Dye, John M., and Schmaljohn, Connie S.
- Subjects
veev ,Mice, Inbred C3H ,Venezuelan equine encephalitis virus ,toll-like receptor 4 ,Brain ,Encephalomyelitis, Venezuelan Equine ,blood-brain barrier ,tlr4 ,Virus Replication ,Permeability ,Encephalitis Virus, Venezuelan Equine ,Disease Models, Animal ,Mice ,Animals ,Female ,Research Article ,Research Paper - Abstract
Venezuelan equine encephalitis virus (VEEV) is an encephalitic alphavirus that can cause debilitating, acute febrile illness and potentially result in encephalitis. Currently, there are no FDA-licensed vaccines or specific therapeutics for VEEV. Previous studies have demonstrated that VEEV infection results in increased blood-brain barrier (BBB) permeability that is mediated by matrix metalloproteinases (MMPs). Furthermore, after subarachnoid hemorrhage in mice, MMP-9 is upregulated in the brain and mediates BBB permeability in a toll-like receptor 4 (TLR4)-dependent manner. Here, we demonstrate that disease in C3H mice during VEEV TC-83 infection is dependent on TLR4 because intranasal infection of C3H/HeN (TLR4WT) mice with VEEV TC-83 resulted in mortality as opposed to survival of TLR4-defective C3H/HeJ (TLR4mut) mice. In addition, BBB permeability was induced to a lesser extent in TLR4mut mice compared with TLR4WT mice during VEEV TC-83 infection as determined by sodium fluorescein and fluorescently-conjugated dextran extravasation. Moreover, MMP-9, MMP-2, ICAM-1, CCL2 and IFN-γ were all induced to significantly lower levels in the brains of infected TLR4mut mice compared with infected TLR4WT mice despite the absence of significantly different viral titers or immune cell populations in the brains of infected TLR4WT and TLR4mut mice. These data demonstrate the critical role of TLR4 in mediating BBB permeability and disease in C3H mice during VEEV TC-83 infection, which suggests that TLR4 is a potential target for the development of therapeutics for VEEV.
- Published
- 2021
36. Rapid detection of an Ebola biomarker with optical microring resonators
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Qavi, Abraham J., Meserve, Krista, Aman, M. Javad, Vu, Hong, Zeitlin, Larry, Dye, John M., Froude, Jeffrey W., Leung, Daisy W., Yang, Lan, Holtsberg, Frederick W., Bailey, Ryan C., and Amarasinghe, Gaya K.
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- 2022
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37. Profile and Persistence of the Virus-Specific Neutralizing Humoral Immune Response in Human Survivors of Sudan Ebolavirus (Gulu)
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Sobarzo, Ariel, Groseth, Allison, Dolnik, Olga, Becker, Stephan, Lutwama, Julius Julian, Perelman, Eddie, Yavelsky, Victoria, Muhammad, Majidat, Kuehne, Ana I., Marks, Robert S., Dye, John M., and Lobel, Leslie
- Published
- 2013
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38. Convalescent Plasma and the Dose of Ebola Virus Antibodies
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Burnouf, Thierry, Dye, John M., and Abayomi, Akin
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- 2017
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39. How to turn competitors into collaborators
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Saphire, Erica Ollmann, Dye, John M., Kobinger, Gary P., Zeitlin, Larry, Chandran, Kartik, and Garry, Robert F.
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- 2017
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40. Postexposure antibody prophylaxis protects nonhuman primates from filovirus disease
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Dye, John M., Herbert, Andrew S., Kuehne, Ana I., Barth, James F., Muhammad, Majidat A., Zak, Samantha E., Ortiz, Ramon A., Prugar, Laura I., and Pratt, William D.
- Published
- 2012
41. A nonreplicating subunit vaccine protects mice against lethal Ebola virus challenge
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Phoolcharoen, Waranyoo, Dye, John M., Kilbourne, Jacquelyn, Piensook, Khanrat, Pratt, William D., Arntzen, Charles J., Chen, Qiang, Mason, Hugh S., and Herbst-Kralovetz, Melissa M.
- Published
- 2011
42. Discovery of pan-ErbB inhibitors protecting from SARS-CoV-2 replication, inflammation, and lung injury by a drug repurposing screen
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Saul, Sirle, Karim, Marwah, Huang, Pei-Tzu, Ghita, Luca, Chiu, Winston, Kumar, Sathish, Bhalla, Nishank, Leyssen, Pieter, Cohen, Courtney A., Huie, Kathleen, Tindle, Courtney, Sibai, Mamdouh, Pinsky, Benjamin A., Das, Soumita, Ghosh, Pradipta, Dye, John M., Solow-Cordero, David E., Jin, Jing, Jochmans, Dirk, Neyts, Johan, Narayanan, Aarthi, De Jonghe, Steven, and Einav, Shirit
- Subjects
viruses ,skin and connective tissue diseases ,Article - Abstract
Effective therapies are needed to combat emerging viruses. Seventeen candidates that rescue cells from SARS-CoV-2-induced lethality and target diverse functions emerged in a screen of 4,413 compounds. Among the hits was lapatinib, an approved inhibitor of the ErbB family of receptor tyrosine kinases. Lapatinib and other pan-ErbB inhibitors suppress replication of SARS-CoV-2 and unrelated viruses with a high barrier to resistance. ErbB4, but not lapatinib's cancer targets ErbB1 and ErbB2, is required for SARS-CoV-2 entry and encephalitis alphavirus infection and is a molecular target mediating lapatinib's antiviral effect. In human lung organoids, lapatinib protects from SARS-CoV-2-induced activation of pathways implicated in non-infectious acute lung injury and fibrosis downstream of ErbBs (p38-MAPK, MEK/ERK, and AKT/mTOR), pro-inflammatory cytokine production, and epithelial barrier injury. These findings reveal regulation of viral infection, inflammation, and lung injury via ErbBs and propose approved candidates to counteract these effects with implications for pandemic coronaviruses and unrelated viruses.
- Published
- 2021
43. Virus nomenclature below the species level: a standardized nomenclature for filovirus strains and variants rescued from cDNA
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Kuhn, Jens H., Bào, Yīmíng, Bavari, Sina, Becker, Stephan, Bradfute, Steven, Brauburger, Kristina, Rodney Brister, J., Bukreyev, Alexander A., Caì, Yíngyún, Chandran, Kartik, Davey, Robert A., Dolnik, Olga, Dye, John M., Enterlein, Sven, Gonzalez, Jean-Paul, Formenty, Pierre, Freiberg, Alexander N., Hensley, Lisa E., Hoenen, Thomas, Honko, Anna N., Ignatyev, Georgy M., Jahrling, Peter B., Johnson, Karl M., Klenk, Hans-Dieter, Kobinger, Gary, Lackemeyer, Matthew G., Leroy, Eric M., Lever, Mark S., Mühlberger, Elke, Netesov, Sergey V., Olinger, Gene G., Palacios, Gustavo, Patterson, Jean L., Paweska, Janusz T., Pitt, Louise, Radoshitzky, Sheli R., Ryabchikova, Elena I., Saphire, Erica Ollmann, Shestopalov, Aleksandr M., Smither, Sophie J., Sullivan, Nancy J., Swanepoel, Robert, Takada, Ayato, Towner, Jonathan S., van der Groen, Guido, Volchkov, Viktor E., Volchkova, Valentina A., Wahl-Jensen, Victoria, Warren, Travis K., Warfield, Kelly L., Weidmann, Manfred, and Nichol, Stuart T.
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- 2014
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44. Discussions and decisions of the 2012–2014 International Committee on Taxonomy of Viruses (ICTV) Filoviridae Study Group, January 2012–June 2013
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Bukreyev, Alexander A., Chandran, Kartik, Dolnik, Olga, Dye, John M., Ebihara, Hideki, Leroy, Eric M., Mühlberger, Elke, Netesov, Sergey V., Patterson, Jean L., Paweska, Janusz T., Saphire, Erica Ollmann, Smither, Sophie J., Takada, Ayato, Towner, Jonathan S., Volchkov, Viktor E., Warren, Travis K., and Kuhn, Jens H.
- Published
- 2014
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45. Phosphatidylserine clustering by the Ebola virus matrix protein is a critical step in viral budding.
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Husby, Monica L, Amiar, Souad, Prugar, Laura I, David, Emily A, Plescia, Caroline B, Huie, Kathleen E, Brannan, Jennifer M, Dye, John M, Pienaar, Elsje, and Stahelin, Robert V
- Abstract
Phosphatidylserine (PS) is a critical lipid factor in the assembly and spread of numerous lipid‐enveloped viruses. Here, we describe the ability of the Ebola virus (EBOV) matrix protein eVP40 to induce clustering of PS and promote viral budding in vitro, as well as the ability of an FDA‐approved drug, fendiline, to reduce PS clustering and subsequent virus budding and entry. To gain mechanistic insight into fendiline inhibition of EBOV replication, multiple in vitro assays were run including imaging, viral budding and viral entry assays. Fendiline lowers PS content in mammalian cells and PS in the plasma membrane, where the ability of VP40 to form new virus particles is greatly lower. Further, particles that form from fendiline‐treated cells have altered particle morphology and cannot significantly infect/enter cells. These complementary studies reveal the mechanism by which EBOV matrix protein clusters PS to enhance viral assembly, budding, and spread from the host cell while also laying the groundwork for fundamental drug targeting strategies. Synopsis: The Ebola virus matrix protein VP40 clusters phosphatidylserine at the plasma membrane inner leaflet for efficient matrix layer formation and virus budding. The drug fendiline diminishes PS levels and clustering, reducing EBOV budding and spread. VP40 clusters phosphatidylserine (PS) in the plasma membrane of cells.VP40 PS clustering requires PS‐binding residues and VP40 oligomerization.FDA‐approved fendiline reduces PS levels and clustering.Fendiline greatly reduces VP40 oligomerization, EBOV budding and subsequent viral entry. [ABSTRACT FROM AUTHOR]
- Published
- 2022
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46. An introduction to the Marburg virus vaccine consortium, MARVAC.
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Cross, Robert W., Longini, Ira M., Becker, Stephan, Bok, Karin, Boucher, David, Carroll, Miles W., Díaz, Janet V., Dowling, William E., Draghia-Akli, Ruxandra, Duworko, James T., Dye, John M., Egan, Michael A., Fast, Patricia, Finan, Amy, Finch, Courtney, Fleming, Thomas R., Fusco, Joan, Geisbert, Thomas W., Griffiths, Anthony, and Günther, Stephan
- Subjects
MARBURG virus ,VIRAL vaccines ,CONSORTIA ,VACCINE development ,COMMUNICABLE diseases - Abstract
The emergence of Marburg virus (MARV) in Guinea and Ghana triggered the assembly of the MARV vaccine "MARVAC" consortium representing leaders in the field of vaccine research and development aiming to facilitate a rapid response to this infectious disease threat. Here, we discuss current progress, challenges, and future directions for MARV vaccines. [ABSTRACT FROM AUTHOR]
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- 2022
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47. Design and characterization of ebolavirus GP prehairpin intermediate mimics as drug targets
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Clinton, Tracy R., Weinstock, Matthew T., Jacobsen, Michael T., Szabo-Fresnais, Nicolas, Pandya, Maya J., Whitby, Frank G., Herbert, Andrew S., Prugar, Laura I., McKinnon, Rena, Hill, Christopher P., Welch, Brett D., Dye, John M., Eckert, Debra M., and Kay, Michael S.
- Published
- 2015
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48. Egg-Derived Anti-SARS-CoV-2 Immunoglobulin Y (IgY) With Broad Variant Activity as Intranasal Prophylaxis Against COVID-19.
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Frumkin, Lyn R., Lucas, Michaela, Scribner, Curtis L., Ortega-Heinly, Nastassja, Rogers, Jayden, Yin, Gang, Hallam, Trevor J., Yam, Alice, Bedard, Kristin, Begley, Rebecca, Cohen, Courtney A., Badger, Catherine V., Abbasi, Shawn A., Dye, John M., McMillan, Brian, Wallach, Michael, Bricker, Traci L., Joshi, Astha, Boon, Adrianus C. M., and Pokhrel, Suman
- Subjects
SARS-CoV-2 ,COVID-19 ,NEUTRALIZATION tests ,SARS-CoV-2 Delta variant ,SARS-CoV-2 Omicron variant ,INTRANASAL administration - Abstract
COVID-19 emergency use authorizations and approvals for vaccines were achieved in record time. However, there remains a need to develop additional safe, effective, easy-to-produce, and inexpensive prevention to reduce the risk of acquiring SARS-CoV-2 infection. This need is due to difficulties in vaccine manufacturing and distribution, vaccine hesitancy, and, critically, the increased prevalence of SARS-CoV-2 variants with greater contagiousness or reduced sensitivity to immunity. Antibodies from eggs of hens (immunoglobulin Y; IgY) that were administered the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein were developed for use as nasal drops to capture the virus on the nasal mucosa. Although initially raised against the 2019 novel coronavirus index strain (2019-nCoV), these anti-SARS-CoV-2 RBD IgY surprisingly had indistinguishable enzyme-linked immunosorbent assay binding against variants of concern that have emerged, including Alpha (B.1.1.7), Beta (B.1.351), Delta (B.1.617.2), and Omicron (B.1.1.529). This is different from sera of immunized or convalescent patients. Culture neutralization titers against available Alpha, Beta, and Delta were also indistinguishable from the index SARS-CoV-2 strain. Efforts to develop these IgY for clinical use demonstrated that the intranasal anti-SARS-CoV-2 RBD IgY preparation showed no binding (cross-reactivity) to a variety of human tissues and had an excellent safety profile in rats following 28-day intranasal delivery of the formulated IgY. A double-blind, randomized, placebo-controlled phase 1 study evaluating single-ascending and multiple doses of anti-SARS-CoV-2 RBD IgY administered intranasally for 14 days in 48 healthy adults also demonstrated an excellent safety and tolerability profile, and no evidence of systemic absorption. As these antiviral IgY have broad selectivity against many variants of concern, are fast to produce, and are a low-cost product, their use as prophylaxis to reduce SARS-CoV-2 viral transmission warrants further evaluation. Clinical Trial Registration: https://www.clinicaltrials.gov/ct2/show/NCT04567810 , identifier NCT04567810. [ABSTRACT FROM AUTHOR]
- Published
- 2022
- Full Text
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49. Virus nomenclature below the species level: a standardized nomenclature for laboratory animal-adapted strains and variants of viruses assigned to the family Filoviridae
- Author
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Kuhn, Jens H., Bao, Yiming, Bavari, Sina, Becker, Stephan, Bradfute, Steven, Brister, J. Rodney, Bukreyev, Alexander A., Caì, Yíngyún, Chandran, Kartik, Davey, Robert A., Dolnik, Olga, Dye, John M., Enterlein, Sven, Gonzalez, Jean-Paul, Formenty, Pierre, Freiberg, Alexander N., Hensley, Lisa E., Honko, Anna N., Ignatyev, Georgy M., Jahrling, Peter B., Johnson, Karl M., Klenk, Hans-Dieter, Kobinger, Gary, Lackemeyer, Matthew G., Leroy, Eric M., Lever, Mark S., Lofts, Loreen L., Mühlberger, Elke, Netesov, Sergey V., Olinger, Gene G., Palacios, Gustavo, Patterson, Jean L., Paweska, Janusz T., Pitt, Louise, Radoshitzky, Sheli R., Ryabchikova, Elena I., Saphire, Erica Ollmann, Shestopalov, Aleksandr M., Smither, Sophie J., Sullivan, Nancy J., Swanepoel, Robert, Takada, Ayato, Towner, Jonathan S., van der Groen, Guido, Volchkov, Viktor E., Wahl-Jensen, Victoria, Warren, Travis K., Warfield, Kelly L., Weidmann, Manfred, and Nichol, Stuart T.
- Published
- 2013
- Full Text
- View/download PDF
50. Virus nomenclature below the species level: a standardized nomenclature for natural variants of viruses assigned to the family Filoviridae
- Author
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Kuhn, Jens H., Bao, Yiming, Bavari, Sina, Becker, Stephan, Bradfute, Steven, Brister, J. Rodney, Bukreyev, Alexander A., Chandran, Kartik, Davey, Robert A., Dolnik, Olga, Dye, John M., Enterlein, Sven, Hensley, Lisa E., Honko, Anna N., Jahrling, Peter B., Johnson, Karl M., Kobinger, Gary, Leroy, Eric M., Lever, Mark S., Mühlberger, Elke, Netesov, Sergey V., Olinger, Gene G., Palacios, Gustavo, Patterson, Jean L., Paweska, Janusz T., Pitt, Louise, Radoshitzky, Sheli R., Saphire, Erica Ollmann, Smither, Sophie J., Swanepoel, Robert, Towner, Jonathan S., van der Groen, Guido, Volchkov, Viktor E., Wahl-Jensen, Victoria, Warren, Travis K., Weidmann, Manfred, and Nichol, Stuart T.
- Published
- 2013
- Full Text
- View/download PDF
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