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1. List of contributors

Author

Aizawa, Shin-Ichi, primary, Alberdi, Pilar, additional, Alexander, David C., additional, Alía, Alberto, additional, Allison, D.G., additional, Amyes, Sebastian G.B., additional, An, Haoran, additional, Andrade, María J., additional, Antelmann, Haike, additional, Arias, Cesar A., additional, Asensio, Miguel A., additional, Axell-House, Dierdre B., additional, Bae, Hee-Won, additional, Baena, Laura Muñoz, additional, Baig, Abdul Mannan, additional, Bailey, Spenser O., additional, Baize, Sylvain, additional, Baldi, Pablo C., additional, Barbosa, Angela Silva, additional, Barbuddhe, Sukhadeo B., additional, Bard, Emilie, additional, Barry, Eileen M., additional, Basarab, Gregory S., additional, Beloborodova, N.V, additional, Bermúdez, Elena, additional, Bidmos, Fadil A., additional, Bisgaard, Magne, additional, Blakely, Garry W., additional, Bloch, Evan, additional, Boesen, Thias Oberg, additional, Bose, Dipayan, additional, Botero, Javier Enrique, additional, Bouabe, Hicham, additional, Bouchard, Michael J., additional, Bozue, Joel A., additional, Bradbury, Richard S., additional, Brett Moreau, G., additional, Cabezas-Cruz, Alejandro, additional, Cai, Rong-Jun, additional, Calderón, Enrique J., additional, Cao, Boyang, additional, Carmena, David, additional, Carvalho, Eneas, additional, Caulfield, Amanda D., additional, Cen, Shan, additional, Chai, Jong-Yil, additional, Chamberland, Robin R., additional, Champredon, David, additional, Chan, Edward D., additional, Charbon, Godefroid, additional, Chato, Connor, additional, Chelomina, G.N., additional, Chen, Jingyu, additional, Chen, Min, additional, Chen, Shuyu, additional, Chen, Suilin, additional, Chen, Yanfei, additional, Chen, Zhaoyuan, additional, Cheng, Aimin, additional, Cheng, Keding, additional, Chiu, Charles Y., additional, Cho, You-Hee, additional, Christensen, Henrik, additional, Chrtdernevskaya, E.A., additional, Contreras, Adolfo, additional, Contreras, Marinela, additional, Córdoba, Juan J., additional, Córdoba, María G., additional, Costa, Rita, additional, Cote, Christopher K., additional, Cui, Xiangling, additional, Cui, Yujun, additional, Dacal, Elena, additional, Dammann, Allison N., additional, Das, Shubhagata, additional, Dashti, Alejandro, additional, de la Fuente, José, additional, de la Garza, Mireya, additional, Delgado, Josué, additional, Delgado-Cuesta, Juan, additional, Deng, Haiteng, additional, Deng, Li, additional, Dey, Debajit, additional, Dhama, Kuldeep, additional, Diego, Juan García-Bernalt, additional, Ding, Hao, additional, Doern, Christopher D., additional, Dorman, Charles J., additional, Du, Zongmin, additional, Dunbar, Sherry A., additional, Duthie, Malcolm, additional, Dybvig, Kevin F., additional, Eakin, Ann E., additional, Eallonardo, Samuel J., additional, Eberly, Allison R., additional, Echeverry, Adriana Jaramillo, additional, Egland, Paul G., additional, El Zowalaty, Mohamed E., additional, Endsley, Janice Jones, additional, Eom, Keeseon S., additional, Evans, Benjamin A., additional, Falkinham, Joseph O., additional, Feng, Siwei, additional, Feng, Yaoyu, additional, Feng, Zongdi, additional, Fernández-Soto, Pedro, additional, Ferreira, Roux-Cil, additional, Flores-Huerta, Nadia, additional, Foster, Timothy J., additional, Fox-Moon, Sandra M., additional, Fraga, Tatiana Rodrigues, additional, Fredricks, David N., additional, Freitag, Nancy E., additional, Frimodt-Møller, Jakob, additional, Fuller, Risa, additional, Ganesh, Balasubramanian, additional, Gao, Ning, additional, García-Carnero, Laura C., additional, Garzetti, Debora, additional, Geoghegan, Joan A., additional, Ghenim, Raed, additional, Giambartolomei, Guillermo H., additional, Gilbert, Nicole M., additional, Gillis, Thomas Phillip, additional, Gladstone, Camilla A., additional, Gómez-Gaviria, Manuela, additional, Gómez-Marín, Jorge E., additional, Gong, Tengfang, additional, González, Ramón A., additional, Gray-Owen, Scott D., additional, Gu, Bing, additional, Guzmán-Téllez, Paula, additional, Hajal, Caroline, additional, Han, Yanping, additional, Hao, Yi, additional, Harrington, Amanda T., additional, Harris, Jason B., additional, Harvill, Eric T., additional, Hasan, S. Saif, additional, He, Guang-Jun, additional, He, Yongqun, additional, Heffron, Jared D., additional, Hidalgo, Paloma, additional, Hindiyeh, Musa Y., additional, Hreha, Teri N., additional, Hu, Xiaoyu, additional, Huang, Guanghua, additional, Huang, Jiangqing, additional, Huang, Liang, additional, Huang, Shifeng, additional, Huang, Xingxu, additional, Huang, Xueting, additional, Huang, Yilun, additional, Huffman, Anthony, additional, Humphreys, Tricia L., additional, Hunstad, David A., additional, Inglis, Timothy J.J., additional, Isaac, Lourdes, additional, Jacobs, Samantha E., additional, Janowicz, Diane M., additional, Jeon, Hyeong-Kyu, additional, Ji, Quanjiang, additional, Jia, Qi, additional, Jia, Wei, additional, Jin, Shouguang, additional, Jneidi, Lama, additional, Jose, Shinsmon, additional, Jung, Bong-Kwang, additional, Kattan, Randa, additional, Kaushik, Rahul, additional, Khare, Reeti, additional, Kim, Eun Sook, additional, Kirn, Thomas J., additional, Koo, Hyun, additional, Köster, Pamela C., additional, Krause, Peter J., additional, Kumar, Sanjai, additional, Kupz, Andreas, additional, Lambert, P.A., additional, Lamont, Richard J., additional, Langford, Paul R., additional, Lebeaux, David, additional, Legname, Giuseppe, additional, Li, Bin, additional, Li, Chunhao, additional, Li, Fen, additional, Li, Jun, additional, Li, Lanjuan, additional, Li, Ruofan, additional, Li, Ruoyu, additional, Li, Ting, additional, Li, Yang-Yang, additional, Li, Yanhua, additional, Li, Zhuorong, additional, Liang, Xiaomeng, additional, Liao, Guojian, additional, Lin, Ping, additional, Ling, Yun, additional, Liu, Bo, additional, Liu, Dongyou, additional, Liu, Guohua, additional, Liu, Huidi, additional, Liu, Jiafeng, additional, Liu, Jintao, additional, Liu, Qi, additional, Liu, Shu-Lin, additional, Liu, Taiping, additional, Liu, Tongbao, additional, Liu, Wei, additional, Liu, Yan, additional, Liu, Yanni, additional, Liu, Yisong, additional, Liu, Yuan, additional, Løbner-Olesen, Anders, additional, Loeffelholz, Michael, additional, Lu, Hongzhou, additional, Luna, Brian, additional, Ma, Bingting, additional, Ma, Chengying, additional, Ma, Shuang, additional, Ma, TianLi, additional, Madan, Rajat, additional, Mahle, Rachael E., additional, Mahlen, Steven D., additional, Malik, Satya Veer Singh, additional, Malik, Yashpal Singh, additional, Malvy, Denis, additional, Mann, Barbara J., additional, Marasini, Daya, additional, Maris, Alexander S., additional, Marjomäki, Varpu, additional, Marjuki, Henju, additional, Martín, Alberto, additional, Martín, Irene, additional, Martínez-Castillo, Moisés, additional, Martínez-Pabón, María Cecilia, additional, Mathison, Blaine A., additional, Ma’ayeh, Showgy, additional, McDowell, Andrew, additional, McLaughlin, Stephanie E., additional, McSheffrey, Gordon G., additional, Medrano, Francisco J., additional, Meehan, Conor J., additional, Mehta, Dhwani, additional, Mejía-Oquendo, Manuela, additional, Melo-Cristino, José, additional, Mendoza-Barberá, Elena, additional, Meng, Xinan, additional, Merino, Susana, additional, Merritt, Adam J., additional, Miller, Steve, additional, Miller, William R., additional, Minamino, Tohru, additional, Mirzaei, Mohammadali Khan, additional, Mora-Montes, Héctor M., additional, Mortensen, Joel, additional, Mostafa, Heba H., additional, Muhsen, Khitam, additional, Mujahed, Ahlam, additional, Muro, Antonio, additional, Murphy, Olwen C., additional, Newton, Hayley J., additional, Nguyen, April H., additional, Nichols, Wright W., additional, Niu, Siqiang, additional, Núñez, Félix, additional, Obregon, Dasiel, additional, Okamoto, Akira, additional, Okutani, Akiko, additional, Olabode, Abayomi, additional, Omar, Muna, additional, Ong, Edison, additional, Ouyang, Zhiming, additional, Pacak, Christina A., additional, Pacheco-Yépez, Judith, additional, Palmer, John, additional, Pang, Xiaoli, additional, Paredes-Sabja, Daniel, additional, Peng, Zhong, additional, Peng, Zonggen, additional, Pérez-Nevado, Francisco, additional, Poon, Art, additional, Pospíšilová, Petra, additional, Potts, Caelin C., additional, Pu, Qinqin, additional, Pujic, Petar, additional, Qi, Rui, additional, Qian, Chenyun, additional, Qian, Liu, additional, Qin, Aiping, additional, Qu, Fen, additional, Rakin, Alexander, additional, Ramesh, Ashwin, additional, Ramirez, Mario, additional, Rao, Yu, additional, Ratner, Adam J., additional, Rawool, Deepak B., additional, Rehman, Asma, additional, Ren, Jie, additional, Ren, Ping, additional, Retchless, Adam C., additional, Robertson, Erle S., additional, Rodríguez, Alicia, additional, Rodriguez, Azucena, additional, Rodríguez-Medina, Carolina, additional, Rodriguez-Nava, Veronica, additional, Rohde, Manfred, additional, Romero-Rodríguez, Alba, additional, Rosales-Morgan, Gabriela, additional, Rosenkranz, Andrea L., additional, Ruiz-Moyano, Santiago, additional, Ruokolainen, Visa, additional, Sabateen, Ali, additional, Sahu, Radhakrishna, additional, Sails, Andrew, additional, Sang, Yu, additional, Santana, Clarissa H., additional, Santos, Jesus A., additional, Santos, Renato L., additional, Schmitz, Jonathan E., additional, Serrano-Luna, Jesús, additional, Shen, Jianzhong, additional, Shen, Zhangqi, additional, Shibayama, Mineko, additional, Shirtliff, Mark E., additional, Silva-Costa, Catarina, additional, Silva-Olivares, Angélica, additional, Singh, Niraj Kumar, additional, Šmajs, David, additional, Smith, Robert P., additional, Smith, Sophie, additional, Snyder, Lori A.S., additional, Song, Yinggai, additional, Soro, Aurea Simon, additional, Spearman, Paul, additional, Spellberg, Brad, additional, Sprague, Lisa D., additional, Stratton, Charles W., additional, Strenk, Susan M., additional, Strugnell, Richard A., additional, Sun, Keer, additional, Suo, Xun, additional, Suzuki-Hatano, Silveli, additional, Svärd, Staffan, additional, Talbot, Elizabeth A., additional, Tamez-Castrellón, Alma K., additional, Tan, Nie, additional, Tang, Cynthia Y., additional, Tang, Yi-Wei, additional, Tao, Jia, additional, Tao, Lili, additional, Terrero-Salcedo, David, additional, Tharmalingam, Jayaraman, additional, Thwe, Phyu M., additional, Tiamani, Kawtar, additional, Tomás, Juan M., additional, Topaz, Nadav, additional, Tsai, Ang-Chen, additional, Tsalik, Ephraim L., additional, Tuomanen, Elaine I., additional, Turenne, Christine Y., additional, Tyagi, Anuj, additional, Uprety, Priyanka, additional, Valour, Florent, additional, van Hensbergen, Vincent P., additional, Venkatesan, Arun, additional, Vergis, Jess, additional, Villar, Margarita, additional, Vollmer, Waldemar, additional, Waites, Ken B., additional, Wan, Xiu-Feng, additional, Wang, Guiqing, additional, Wang, Lijun, additional, Wang, Lin, additional, Wang, Linqi, additional, Wang, Xiangru, additional, Wang, Xin, additional, Wang, Xinjie, additional, Wang, Ya-Ting, additional, Wang, Yang, additional, Wang, Yating, additional, Weil, Ana A., additional, Welkos, Susan L., additional, Wengenack, Nancy L., additional, Westblade, Lars F., additional, Whitfield, Chris, additional, Wu, Hui, additional, Wu, Lijuan, additional, Wu, Min, additional, Wu, Yarong, additional, Wu, Zhaowei, additional, Xiang, Ye, additional, Xiao, Di, additional, Xiao, Li, additional, Xiao, Lihua, additional, Xu, Tao, additional, Xu, Wenyue, additional, Xu, Xinping, additional, Xue, Jinling, additional, Yadav, Jay Prakash, additional, Yan, Junxiang, additional, Yan, Yixin, additional, Yang, Changmei, additional, Yang, Ruifu, additional, Yang, Ying, additional, Yao, Kaihu, additional, Yao, Yu-Feng, additional, Yeakle, Kyle C., additional, Yu, Demin, additional, Yu, Hao, additional, Yu, Xue-Jie, additional, Yuan, Zhenghong, additional, Zai, Wenjing, additional, Zhang, Jianzhong, additional, Zhang, Jing-Ren, additional, Zhang, Lanyue, additional, Zhang, Lijie, additional, Zhang, Qiwei, additional, Zhang, Wenbao, additional, Zhang, Wenhong, additional, Zhang, Xinxin, additional, Zhao, Youbao, additional, Zhou, Chuanmin, additional, Zhu, Feng, additional, Zhu, Jingting, additional, and Zhu, Yongqun, additional

Published
2024
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3. Murepavadin promotes the killing efficacies of aminoglycoside antibiotics against Pseudomonas aeruginosa by enhancing membrane potential

Author

Wei, Xiaoya, primary, Gao, Jiacong, additional, Zhou, Dandan, additional, Xu, Congjuan, additional, Chen, Ping, additional, Chen, Shuiping, additional, Zhang, Yanhong, additional, Liu, Xuehua, additional, Li, Guanxian, additional, Zhu, Guangbo, additional, Liu, Huimin, additional, Li, Jinjin, additional, Geng, Bin, additional, Gao, Linlin, additional, Cheng, Zhihui, additional, Lamont, Iain L., additional, Pletzer, Daniel, additional, Jin, Yongxin, additional, Jin, Shouguang, additional, and Wu, Weihui, additional

Published
2024
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4. Host Cells Upregulate Phosphate Transporter PIT1 to Inhibit Ehrlichia chaffeensis Intracellular Growth.

Author

Li, Meifang, Yang, Nan, Li, Xiaoxiao, Duan, Nan, Qin, Shanhua, Wang, Mengyao, Zhou, Yuhong, Jin, Yongxin, Wu, Weihui, Jin, Shouguang, and Cheng, Zhihui

Subjects
EHRLICHIA, PENICILLIN-binding proteins, RECOMBINANT proteins, BACTERIAL growth, PHOSPHATES
Abstract

Ehrlichia chaffeensis infects and proliferates inside monocytes or macrophages and causes human monocytic ehrlichiosis (HME), an emerging life-threatening tick-borne zoonosis. After internalization, E. chaffeensis resides in specialized membrane-bound inclusions, E. chaffeensis-containing vesicles (ECVs), to evade from host cell innate immune responses and obtain nutrients. However, mechanisms exploited by host cells to inhibit E. chaffeensis growth in ECVs are still largely unknown. Here we demonstrate that host cells recognize E. chaffeensis Ech_1067, a penicillin-binding protein, and then upregulate the expression of PIT1, which is a phosphate transporter and transports phosphate from ECVs to the cytosol to inhibit bacterial growth. We found that host cells upregulate the PIT1 expression upon E. chaffeensis infection using transcriptome sequencing, qRT-PCR and Western blotting, and PIT1 is localized on the ECV membrane in infected THP-1 cells using confocal microscopy. Silence of PIT1 using shRNA enhances E. chaffeensis intracellular growth. Finally, we found that E. chaffeensis Ech_1067 induces the upregulation of PIT1 expression through the MyD88-NF-κB pathway using recombinant protein for stimulation and siRNA for silence. Our findings deepen the understanding of the innate immune responses of host cells to inhibit bacterial intracellular growth and facilitate the development of new therapeutics for HME. [ABSTRACT FROM AUTHOR]

Published
2024
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24. List of Contributors

Author

Abel-Santos, Ernesto, primary, Abraham, Soman N., additional, Aizawa, Shin-Ichi, additional, Aldape, Michael J., additional, Alexander, David C., additional, Allison, David G., additional, Amyes, Sebastian G.B., additional, Anderson, Burt E., additional, Anderson, Frank J., additional, Antelmann, Haike, additional, Austin, Frank W., additional, Ayllón, Nieves, additional, Bai, Fang, additional, Barbosa, Angela Silva, additional, Barer, Michael R., additional, Basarab, Gregory S., additional, Beaman, Blaine L., additional, Beard, Matthew, additional, Black, Carolyn M., additional, Blakely, Garry W., additional, Boiron, Patrick, additional, Bouabe, Hicham, additional, Bozue, Joel A., additional, Brinkman, Cassandra L., additional, Brubaker, Robert R., additional, Bryant, Amy E., additional, Cain, Robert J., additional, Calvo, Ana Cristina, additional, Carvalho, Eneas, additional, Capo, Christian, additional, Castillo-Ramirez, Santiago, additional, Chaddock, John A., additional, Chamberland, Robin R., additional, Clarridge, Jill E., additional, Cote, Christopher K., additional, Cox, Sarah L., additional, Cutler, Sally J., additional, Davidson, Donald J., additional, Day, Nicholas P.J., additional, de la Fuente, José, additional, De Jesus, Magdia, additional, Dorin, Julia R., additional, Dorman, Charles J., additional, Eakin, Ann E., additional, Egland, Paul G., additional, Ellis, Simon, additional, Enright, Mark C., additional, Evans, Benjamin A., additional, Everett, Jake A., additional, Falkinham, Joseph O., additional, Fan, Feinan, additional, Fan, Huizhou, additional, Faulds-Pain, Alexandra, additional, Feil, Edward J., additional, Figueroa, Cesar J., additional, Forsberg, Åke, additional, Foster, Timothy J., additional, Fox-Moon, Sandra M., additional, Fraga, Tatiana Rodrigues, additional, Fredricks, David N., additional, Freitag, Nancy E., additional, García-López, María-Luisa, additional, Garzetti, Debora, additional, Gemmell, Curtis G., additional, Geoghegan, Joan A., additional, Gillis, Thomas P., additional, Gilmore, Michael S., additional, Goldstone, Robert J., additional, Gray-Owen, Scott D., additional, Guiso, Nicole, additional, Hallstrom, Kelly N., additional, Harper, David R., additional, Harrington, Amanda T., additional, Harris, Jason B., additional, Hays, John P., additional, He, Yongqun, additional, Heffron, Jared D., additional, Heimer, Susan R., additional, High, Nicola J., additional, Hobot, Jan A., additional, Hultgren, Scott, additional, Humphreys, Tricia L., additional, Hunstad, David A., additional, Igietseme, Joseph U., additional, Inglis, Neil F., additional, Inglis, Tim J.J., additional, Isaac, Lourdes, additional, Janowicz, Diane M., additional, Jin, Shouguang, additional, Jin, Yongxin, additional, Johansson, Anna-Lena, additional, Johnston, Randal N., additional, Jones, Jessica L., additional, Justice, Sheryl S., additional, Kaakoush, Nadeem O., additional, Kalas, Vasilios, additional, Khare, Reeti, additional, Jordan, I. King, additional, Kobayashi, Keiko, additional, Kocan, Katherine M., additional, Könönen, Eija, additional, Kumar, Purnima S., additional, Lambert, Peter A., additional, Lamont, Richard J., additional, Lan, Ruiting, additional, Lang, Sue, additional, Lereclus, Didier, additional, Levett, Paul N., additional, Li, Xuefeng, additional, Liu, Dongyou, additional, Liu, Shu-Lin, additional, Ma, Lin, additional, Mahlen, Steven D., additional, Man, Si Ming, additional, Margolis, Elisa, additional, Marrie, Thomas J., additional, Martin, Melissa J., additional, Mayer, Leonard W., additional, McConville, Malcolm, additional, McCormick, Beth A., additional, McDowell, Andrew, additional, McHugh, Brian J., additional, McMullen, P. David, additional, McSheffrey, Gordon G., additional, Mege, Jean-Louis, additional, Merritt, Adam J., additional, Minnick, Michael F., additional, Mitchell, Hazel M., additional, Morrison, Donald, additional, Musser, Kimberlee A., additional, Nagahama, Masahiro, additional, Nagao, Prescilla Emy, additional, Nagy, István, additional, Salomonsson, Emelie Näslund, additional, Nazarian, Elizabeth J., additional, Nichols, Wright W., additional, Noppa, Laila, additional, Octavia, Sophie, additional, Oda, Masataka, additional, Ofek, Itzhak, additional, Oliver, James D., additional, Olson, Patrick D., additional, Omosun, Yusuf, additional, Ong, Edmund, additional, Osta, Rosario, additional, Otero, Andrés, additional, Oyston, Petra C.F., additional, Paris, Daniel H., additional, Patel, Robin, additional, Patrick, Sheila, additional, Pedra, Joao H.F., additional, Posteraro, Brunella, additional, Posteraro, Patrizia, additional, Poxton, Ian R., additional, Pujic, Petar, additional, Raffa, Brittany J., additional, Rakin, Alexander, additional, Ramarao, Nalini, additional, Ramirez, Mario, additional, Ravalison, Miora, additional, Reed, Kurt D., additional, Reglinski, Mark, additional, Richards, Allen L., additional, Riesbeck, Kristian, additional, Riley, Thomas V., additional, Rodríguez-Calleja, José-María, additional, Rodríguez-Nava, Verónica, additional, Rumbaugh, Kendra P., additional, Sanderson, Kenneth E., additional, Sanguinetti, Maurizio, additional, Santos, Jesús A., additional, Santos, Renato L., additional, Schaar, Viveka, additional, Scheld, W. Michael, additional, Schmitz, Jonathan E., additional, Schwartzman, Joseph D., additional, Severo, Maiara S., additional, Sharon, Nathan, additional, Shirtliff, Mark E., additional, Simner, Patricia J., additional, Šmajs, David, additional, Smith, David G.E., additional, Sorokin, Alexei, additional, Sprague, Lisa D., additional, Sriskandan, Shiranee, additional, Stevens, Dennis L., additional, Stratton, Charles W., additional, Strouhal, Michal, additional, Su, Yu Ching, additional, Sussman, Max, additional, Talbot, Elizabeth A., additional, Tang, Le, additional, Tang, Yi-Wei, additional, Taur, Ying, additional, Tessier, Jeffrey M., additional, Textoris, Julien, additional, Thirumalapura, Nagaraja R., additional, Tsuge, Hideaki, additional, Turenne, Christine Y., additional, Valvano, Miguel A., additional, Vázquez-Boland, José A., additional, Verhaegh, Suzanne J.C., additional, Volkan, Ender, additional, Vollmer, Waldemar, additional, Wade, William F., additional, Waites, Ken B., additional, Walker, Alan W., additional, Walker, David H., additional, Wang, Guiqing, additional, Wang, Qinning, additional, Wang, Xin, additional, Ward, Bruce, additional, Watson, Eleanor, additional, Weil, Ana A., additional, Welkos, Susan L., additional, Wen, Zhensong, additional, Wengenack, Nancy L., additional, Westblade, Lars F., additional, Wexler, Hannah M., additional, Wren, Brendan W., additional, Wu, Min, additional, Wu, Shangwei, additional, Wu, Weihui, additional, Xiao, Li, additional, Zhang, Jing-Ren, additional, Zhao, Zuotao, additional, and Zhong, Guangming, additional

Published
2015
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29. A Modular Synthetic Route Involving N-Aryl-2-nitrosoaniline Intermediates Leads to a New Series of 3-Substituted Halogenated Phenazine Antibacterial Agents

Author

Yang, Hongfen, primary, Kundra, Shivani, additional, Chojnacki, Michaelle, additional, Liu, Ke, additional, Fuse, Marisa A., additional, Abouelhassan, Yasmeen, additional, Kallifidas, Dimitris, additional, Zhang, Peilan, additional, Huang, Guangtao, additional, Jin, Shouguang, additional, Ding, Yousong, additional, Luesch, Hendrik, additional, Rohde, Kyle H., additional, Dunman, Paul M., additional, Lemos, José A., additional, and Huigens, Robert W., additional

Published
2021
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32. Cell-free expression of soluble and membrane proteins in an array device for drug screening

Author

Khnouf, Ruba, Olivero, Daniel, Jin, Shouguang, Coleman, Matthew A., and Fan, Z. Hugh

Subjects
Membrane proteins -- Chemical properties, Gene expression -- Research, Drugs -- Product/Service Evaluations, Drugs -- Methods, Drugs -- Equipment and supplies, Chemistry
Abstract

Enzymes and membrane protein receptors represent almost three-quarters of all current drug targets. As a result, it would be beneficial to have a platform to produce them in a high-throughput format for drug screening. We have developed a miniaturized fluid array device for cell-free protein synthesis, and the device was exploited to produce both soluble and membrane proteins. Two membrane-associated proteins, bacteriorhodopsin and ApoA lipoprotein, were coexpressed in an expression medium in the presence of lipids. Simultaneous expression of ApoA lipoprotein enhanced the solubility of bacteriorhodopsin and would facilitate functional studies. In addition, the device was employed to produce two enzymes, luciferase and [beta]-lactamase, both of which were demonstrated to be compatible with enzyme inhibition assays. [beta]-lactamase, a drug target associated with antibiotic resistance, was further used to show the capability of the device for drug screening. [beta]-Lactamase was synthesized in the 96 units of the device and then assayed by a range of concentrations of four mock drug compounds without harvesting and purification. The inhibitory effects of these compounds on [beta]-lactamase were measured in a parallel format, and the degree in their drug effectiveness agreed well with the data in the literature. This work demonstrated the feasibility of the use of the fluid array device and cell-free protein expression for drug screening, with advantages in less reagent consumption, shorter analysis time, and higher throughput. 10.1021/ac1015479

Published
2010

35. Functional characterization of MigA and WapR: putative Rhamnosyltransferases involved in outer core oligosaccharide biosynthesis of Pseudomonas aeruginosa

Author

Poon, Karen K.H., Westman, Erin L., Vinogradov, Evgeny, Jin, Shouguang, and Lam, Joseph S.

Subjects
Pseudomonas aeruginosa -- Physiological aspects, Biosynthesis -- Research, Oligosaccharides -- Properties, Transferases -- Properties, Transferases -- Influence, Biological sciences
Abstract

Pseudomonas aeruginosa lipopolysaccharide (LPS) contains two glycoforms of core oligosaccharide (OS); one form is capped with O antigen through an [alpha]-1,3-linked L-rhamnose (L-Rha), while the other is uncapped and contains an [alpha]-1,6-linked L-Rha. Two genes in strain PAO1, wapR (PA5000) and migA (PA0705), encode putative glycosyltransferases associated with core biosynthesis. We propose that WapR and MigA are the rhamnosyltransferases responsible for the two linkages of L-Rha to the core. Knockout mutants with mutations in both genes were generated. The wapR mutant produced LPS lacking O antigen, and addition of wapR in trans complemented this defect. The migA mutant produced LPS with a truncated outer core and showed no reactivity to outer core-specific monoclonal antibody (MAb) 5C101. Complementation of this mutant with migA restored reactivity of the LPS to MAb 5C101. Interestingly, LPS from the complemented migA strain was not reactive to MAb 18-19 (specific for the core-plus-one O repeat). This was due to overexpression of MigA in the complemented strain that caused an increase in the proportion of the uncapped core OS, thereby decreasing the amount of the core-plus-one O repeat, indicating that MigA has a regulatory role. The structures of LPS from both mutants were elucidated using nuclear magnetic resonance spectroscopy and mass spectrometry. The capped core of the wapR mutant was found to be truncated and lacked [alpha]-1,3-L-Rha. In contrast, uncapped core OS from the migA mutant lacked [alpha]-l,6-L-Rha. These results provide evidence that WapR is the [alpha]-1,3-rhamnosyltransferase, while MigA is the [alpha]-1,6-rhamnosyltransferase.

Published
2008

36. Regulatory role of PopN and its interacting partners in type III secretion of Pseudomonas aeruginosa

Author

Yang, Hongjing, Shan, Zhiying, Kim, Jaewha, Wu, Weihui, Lian, Wei, Zeng, Lin, Xing, Laijun, and Jin, Shouguang

Subjects
Pseudomonas aeruginosa -- Research, Pseudomonas aeruginosa -- Genetic aspects, Secretion -- Identification and classification, Binding proteins -- Research, Biological sciences
Abstract

The type III secretion system (T3SS) of Pseudomonas aeruginosa plays a significant role in pathogenesis. We have previously identified type III secretion factor (TSF), which is required for effective secretion of the type III effector molecules, in addition to the low calcium signal. TSF includes many low-affinity high-capacity calcium binding proteins, such as serum albumin and casein. A search for the TSF binding targets on the bacterial outer membrane resulted in identification of PopN, a component of the T3SS that is readily detectable on the bacterial cell surface. PopN specifically interacts with Pcr1, and both popN and pcr1 mutants have a constitutive type III secretion phenotype, suggesting that the two proteins form a complex that functions as a T3SS repressor. Further analysis of the popN operon genes resulted in identification of protein-protein interactions between Pcr1 and Pcr4 and between Pcr4 and Pcr3, as well as between PopN and Pcr2 in the presence of PscB. Unlike popN and pcr1 mutants, pcr3 and pcr4 mutants are totally defective in type III secretion, while apcr2 mutant exhibits reduced type III secretion. Interestingly, PopN, Pcr1, Pcr2, and Pcr4 are all secreted in a type III secretion machinery-dependent manner, while Pcr3 is not. These findings imply that these components have important regulatory roles in controlling type III secretion.

Published
2007

37. Ricin detection by biological signal amplification in a well-in-a-well device

Author

Mei, Qian, Fredrickson, Carl K., Lian, Wei, Jin, Shouguang, and Fan, Z. Hugh

Subjects
Ricin -- Research, Genetic transcription -- Research, Biomolecules -- Research, Chemistry
Abstract

This paper presents a ricin detection method based on ricin's inhibitory effects on protein synthesis. Biological synthesis (expression) of a protein includes the steps of gene transcription (DNA [right arrow] RNA) and protein translation (RNA [right arrow] proteins); these reactions can be coupled into a one-step operation and carded out in a cell-free medium. Ricin is known to inhibit protein synthesis by interacting with 28S ribosome RNA; the inhibitory effect is exploited as the sensing mechanism in this work. For each copy of DNA, thousands of copies of proteins can be produced. As a result, the inhibitory effects of ricin are amplified, leading to a significantly enhanced detection signal (the difference between the positive control and samples). An array of protein expression units is developed to accommodate positive/negative controls and multiple samples. The array device contains a solution without any reagent captured on a solid surface, offering flexibility without comprising the activities of biomolecules. The miniaturized well-in-a-well design possesses a mechanism to supply nutrients continuously and remove byproducts, leading to higher protein expression yields and thus larger detection signals (lower detection limit) when ricin is present. We demonstrate the production of green fluorescent protein and luciferase in the device. A calibration curve has been obtained between the luciferase expression yield and the ricin concentration, showing a detection limit of 0.01 nM (0.3 ng/mL) ricin. The nested-well device is also used for measuring the toxicity level of ricin after physical or chemical treatment.

Published
2006

39. Factors triggering type III secretion in Pseudomonas aeruginosa

Author

Kim, Jaewha, Ahn, Kyungseop, Min, Sungran, Jia, Jinghua, Ha, Unhwan, Wu, Donghai, and Jin, Shouguang

Subjects
Pseudomonas aeruginosa -- Research, Calcium-binding proteins -- Research, Protein research, Biological sciences
Abstract

The type III secretion system of Pseudomonas aeruginosa is tightly regulated by various environmental signals, such as low calcium and contact with the host cell. However, the exact signals triggering type III secretion are unknown. The present study describes the finding that secretion of P. aeruginosa type III effector molecules requires protein factors from serum and L broth, designated type III secretion factors (TSFs), in addition to the low-calcium environment. In the absence of TSF or calcium chelator EGTA, basal levels of type III effector molecules are accumulated intracellularly. Addition of TSF and EGTA together effectively triggers the secretion of pre-existing effector molecules in a short time, even before the active expression of type III genes; thus, active type III gene expression does not seem to be a prerequisite for type III secretion. A search for TSF molecules in serum and L broth resulted in the identification of albumin and casein as the functional TSF molecules. Although there is no clear sequence similarity between albumin and casein, both proteins are known to have a low-affinity, high-capacity calcium-binding property. Tests of well-studied calcium-binding proteins seemed to indicate that low-affinity calcium-binding proteins have TSF activity, although the requirement of low-affinity calcium-binding ability for the TSF activity is not clear. P. aeruginosa seems to have evolved a sensing mechanism to detect target cells for type III injection through host-derived proteins in combination with a low-calcium signal. Disruption of the bacterial ability to sense low calcium or TSF might be a valid avenue to the effective control of this bacterial pathogen.

Published
2005

40. PtrB of Pseudomonas aeruginosa suppresses the type III secretion system under the stress of DNA damage

Author

Wu, Weihui and Jin, Shouguang

Subjects
DNA damage -- Research, Pseudomonas aeruginosa -- Genetic aspects, Genetic research, Biological sciences
Abstract

In a search for regulatory genes of the type III secretion system (TTSS) in Pseudomonas aeruginosa, transposon (Tn5) insertional mutants of the prtR gene were found defective in the TTSS. PrtR is an inhibitor of prtN, which encodes a transcriptional activator for pyocin synthesis genes. In P. aeruginosa, pyocin synthesis is activated when PrtR is degraded during the SOS response. Treatment of a wild-type P. aeruginosa strain with mitomycin C, a DNA-damaging agent, resulted in the inhibition of TTSS activation. A prtR/prtN double mutant had the same TTSS defect as the prtR mutant, and complementation by a prtR gene but not by a prtN gene restored the TTSS function. Also, overexpression of the prtN gene in wild-type PAK had no effect on the TTSS; thus, PrtN is not involved in the repression of the TTSS. To identify the PrtR-regulated TTSS repressor, another round of Tn mutagenesis was carried out in the background of a prtR/prtN double mutant. Insertion in a small gene, designated ptrB, restored the normal TTSS activity. Expression of ptrB is specifically repressed by PrtR, and mitomycin C-mediated suppression of the TTSS is also abolished in a ptrB mutant strain. Therefore, PtrB is a new TTSS repressor that coordinates TTSS repression and pyocin synthesis under the stress of DNA damage.

Published
2005

41. Toxin detection by a miniaturized in vitro protein expression array

Author

Mei, Qian, Fredrickson, Carl K., Jin, Shouguang, and Fan, Z. Hugh

Subjects
Toxins -- Measurement, Toxins -- Research, Proteins -- Research, Chemistry
Abstract

A novel concept for toxin detection is presented that is based on the inhibitory effects of certain toxins on protein synthesis. Biological synthesis of proteins is called protein expression, which consists of the steps of DNA transcription and protein translation. In the toxin detection concept, a group of proteins are expressed simultaneously in a device consisting of an array of miniaturized wells. The expression yields of these proteins are inhibited by presence of a toxin. Differential inhibitory effects of each toxin on the expression of proteins in wells result in a response pattern (or signature) of the array device, which can be used as a tool for detection and identification of known and unknown agents. The concept has been demonstrated by in vitro protein expression of three proteins, including green fluorescent protein (GFP), chloramphenicol acetyltransferase (CAT), and luciferase. The production yields of these proteins in a cell-free medium were inhibited differentially by two toxin simulants, tetracycline (TC) and cycloheximide (CH). We confirmed that TC has an inhibitory effect on the production of GFP and CAT in the E. coli expression system whereas CH has a negligible effect. Moreover, the degree of TC's inhibitory effect on GFP is different from that on CAT. We also observed an opposite disparity; TC has a negligible inhibitory effect on the luciferase production in the rabbit reticulocyte expression system, whereas CH has a significant inhibitory effect. In addition, we obtained a response pattern in a 3 x 4 array device; the results suggest the feasibility of toxin detection based on the mechanisms of toxin actions. The device and method are also likely applicable to high-throughput drug screening, evident from the fact that TC is an antibiotic medicine.

Published
2005

42. MucA-mediated coordination of type III secretion and alginate synthesis in Pseudomonas aeruginosa

Author

Wu, Weihui, Badrane, Hassan, Arora, Shiwani, Baker, Henry V., and Jin, Shouguang

Subjects
Pseudomonas aeruginosa -- Research, Pseudomonas aeruginosa -- Genetic aspects, Bacteriology -- Research, Biological sciences
Abstract

The type III secretion system (T3SS) of Pseudomonas aeruginosa is an important virulence factor. The T3SS of P. aeruginosa can be induced by a low calcium signal or upon direct contact with the host cells. The exact pathway of signal sensing and T3SS activation is not clear. By screening a transposon insertion mutant library of the PAK strain, mutation in the mucA gene was found to cause repression of T3SS expression under both type III-inducing and -noninducing conditions. Mutation in the mucA gene is known to cause alginate overproduction, resulting in a mucoid phenotype. Alginate production responds to various environmental stresses and plays a protective role for P. aeruginosa. Comparison of global gene expression of mucA mutant and wild-type PAK under T3SS-inducing conditions confirmed the down regulation of T3SS genes and up regulation of genes involved in alginate biosynthesis. Further analysis indicated that the repression of T3SS in the mucA mutant was AlgU and AlgR dependent, as double mutants mucA/algU and mucA/algR showed normal type III expression. An algR::Gm mutant showed a higher level of type III expression, while overexpression of the algR gene inhibited type III gene expression; thus, it seems that the AlgR-regulated product inhibits the expression of the T3SS genes. It is likely that P. aeruginosa has evolved tight regulatory networks to turn off the energy-expensive T3SS when striving for survival under environmental stresses.

Published
2004

43. The truA gene of Pseudomonas aeruginosa is required for the expression of type III secretory genes

Author

Ahn, Kyung-Seop, Ha, Unhwan, Jia, Jinghua, Wu, Donghai, and Jin, Shouguang

Subjects
RNA -- Research, Apoptosis -- Causes of, Apoptosis -- Research, Pseudomonas aeruginosa -- Genetic aspects, Pseudomonas aeruginosa -- Research, Biological sciences
Abstract

Invasive strains of Pseudomonas aeruginosa can cause rapid host cell apoptosis by injecting the type III effector molecule ExoS. A transposon insertional mutant bank of P. aeruginosa was screened to identify P. aeruginosa genes that contribute to the ability of the bacteria to trigger host cell apoptosis. Several isolated mutants had disruptions in the fimV gene. A fimV mutant was unable to induce the expression of exoS, exoTand exsA genes under type III inducing conditions, thus exhibiting a defect in type III protein secretion. Furthermore, this mutant was defective in twitching motility, although type IV pill were present on the bacterial surface. Complementation by a fimV-containing cosmid clone restored both phenotypes to the wild-type levels. However, expression of the type III genes in the fimV mutant was not restored by the introduction of a fimV gene alone, although it restored the twitching motility. A gene downstream of fimV, encoding a tRNA pseudouridine synthase (truA) homologue, was able to complement the type III gene expression defect of the fimV mutant. Thus fimV and truA form an operon and fimV mutation has a polar effect on truA. Indeed, a truA mutant is defective in type III gene expression while its twitching motility is unaffected, and a truA clone is able to complement the type III secretion defect. Pseudouridination of tRNAs is important for tRNA structure, thereby improving the fidelity of protein synthesis and helping to maintain the proper reading frame; thus the results imply that truA controls tRNAs that are critical for the translation of type III genes or their regulators.

Published
2004

45. Reconstitution of acetosyringone-mediated Agrobacterium tumefaciens virulence gene expression in the heterologous host Escherichia coli

Author

Lohrke, Scott M., Yang, Hongjiang, and Jin, Shouguang

Subjects
Agrobacterium tumefaciens -- Genetic aspects, Gene expression -- Analysis, Virulence (Microbiology) -- Genetic aspects, Genetic engineering -- Research, Biological sciences
Abstract

Research demonstrates that virA and virG virulence genes of Agrobacterium tumefaciens can be successfully reconstituted in Escherichia coli in a inducer-dependent lac promoter-driven approach. Results show that the C-terminal domain of RpoA is necessary for interaction with the transcriptional activator VirG in the above fusion strategy.

Published
2001

47. PvrA is a novel regulator that contributes to Pseudomonas aeruginosa pathogenesis by controlling bacterial utilization of long chain fatty acids

Author

Pan, Xiaolei, primary, Fan, Zheng, primary, Chen, Lei, primary, Liu, Chang, primary, Bai, Fang, primary, Wei, Yu, primary, Tian, Zhenyang, primary, Dong, Yuanyuan, primary, Shi, Jing, primary, Chen, Hao, primary, Jin, Yongxin, primary, Cheng, Zhihui, primary, Jin, Shouguang, primary, Lin, Jianping, primary, and Wu, Weihui, primary

Published
2020
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49. TpiA is a Key Metabolic Enzyme That Affects Virulence and Resistance to Aminoglycoside Antibiotics through CrcZ in Pseudomonas aeruginosa

Author

Xia, Yushan, primary, Wang, Dan, additional, Pan, Xiaolei, additional, Xia, Bin, additional, Weng, Yuding, additional, Long, Yuqing, additional, Ren, Huan, additional, Zhou, Jingyi, additional, Jin, Yongxin, additional, Bai, Fang, additional, Cheng, Zhihui, additional, Jin, Shouguang, additional, and Wu, Weihui, additional

Published
2020
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