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12 results on '"Schorcht, Anna"'

1. Identification of IOMA-class neutralizing antibodies targeting the CD4-binding site on the HIV-1 envelope glycoprotein

Author

van Schooten, Jelle, Farokhi, Elinaz, Schorcht, Anna, van den Kerkhof, Tom L. G. M., Gao, Hongmei, van der Woude, Patricia, Burger, Judith A., Meesters, Tim G. Rijkhold, Bijl, Tom, Ghalaiyini, Riham, Turner, Hannah L., Dorning, Jessica, van Schaik, Barbera D. C., van Kampen, Antoine H. C., Labranche, Celia C., Stanfield, Robyn L., Sok, Devin, Montefiori, David C., Burton, Dennis R., Seaman, Michael S., Ozorowski, Gabriel, Wilson, Ian A., Sanders, Rogier W., Ward, Andrew B., and van Gils, Marit J.

Published
2022
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2. Enhancing and shaping the immunogenicity of native-like HIV-1 envelope trimers with a two-component protein nanoparticle

Author

Brouwer, Philip J. M., Antanasijevic, Aleksandar, Berndsen, Zachary, Yasmeen, Anila, Fiala, Brooke, Bijl, Tom P. L., Bontjer, Ilja, Bale, Jacob B., Sheffler, William, Allen, Joel D., Schorcht, Anna, Burger, Judith A., Camacho, Miguel, Ellis, Daniel, Cottrell, Christopher A., Behrens, Anna-Janina, Catalano, Marco, del Moral-Sánchez, Iván, Ketas, Thomas J., LaBranche, Celia, van Gils, Marit J., Sliepen, Kwinten, Stewart, Lance J., Crispin, Max, Montefiori, David C., Baker, David, Moore, John P., Klasse, Per Johan, Ward, Andrew B., King, Neil P., and Sanders, Rogier W.

Published
2019
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3. Complementary antibody lineages achieve neutralization breadth in an HIV-1 infected elite neutralizer

Author

van Schooten, Jelle, primary, Schorcht, Anna, additional, Farokhi, Elinaz, additional, Umotoy, Jeffrey C., additional, Gao, Hongmei, additional, van den Kerkhof, Tom L. G. M., additional, Dorning, Jessica, additional, Rijkhold Meesters, Tim G., additional, van der Woude, Patricia, additional, Burger, Judith A., additional, Bijl, Tom, additional, Ghalaiyini, Riham, additional, Torrents de la Peña, Alba, additional, Turner, Hannah L., additional, Labranche, Celia C., additional, Stanfield, Robyn L., additional, Sok, Devin, additional, Schuitemaker, Hanneke, additional, Montefiori, David C., additional, Burton, Dennis R., additional, Ozorowski, Gabriel, additional, Seaman, Michael S., additional, Wilson, Ian A., additional, Sanders, Rogier W., additional, Ward, Andrew B., additional, and van Gils, Marit J., additional

Published
2022
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4. CD4 binding-site antibodies induced by a subtype B HIV-1 envelope trimer

Author

Schorcht, Anna, primary, van den Kerkhof, Tom L.G.M., additional, Torres, Jon, additional, Schermer, Edith, additional, LaBranche, Celia, additional, Bontjer, Ilja, additional, Brinkkemper, Mitch, additional, Gulzar, Naveed, additional, Han, Alvin X., additional, Burger, Judith, additional, Ozorowski, Gabriel, additional, Scott, Jamie, additional, Schuitemaker, Hanneke, additional, Montefiori, David, additional, van Gils, Marit, additional, Ward, Andrew B., additional, and Sanders, Rogier W., additional

Published
2022
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5. The Glycan Hole Area of HIV-1 Envelope Trimers Contributes Prominently to the Induction of Autologous Neutralization

Author

Schorcht, Anna, primary, Cottrell, Christopher A., additional, Pugach, Pavel, additional, Ringe, Rajesh P., additional, Han, Alvin X., additional, Allen, Joel D., additional, van den Kerkhof, Tom L. G. M., additional, Seabright, Gemma E., additional, Schermer, Edith E., additional, Ketas, Thomas J., additional, Burger, Judith A., additional, van Schooten, Jelle, additional, LaBranche, Celia C., additional, Ozorowski, Gabriel, additional, de Val, Natalia, additional, Bader, Daniel L. V., additional, Schuitemaker, Hanneke, additional, Russell, Colin A., additional, Montefiori, David C., additional, van Gils, Marit J., additional, Crispin, Max, additional, Klasse, P. J., additional, Ward, Andrew B., additional, Moore, John P., additional, and Sanders, Rogier W., additional

Published
2022
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6. An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability

Author

van Gils, Marit J., van den Kerkhof, Tom L. G. M., Ozorowski, Gabriel, Cottrell, Christopher A., Sok, Devin, Pauthner, Matthias, Pallesen, Jesper, de Val, Natalia, Yasmeen, Anila, de Taeye, Steven W., Schorcht, Anna, Gumbs, Stephanie, Johanna, Inez, Saye-Francisco, Karen, Liang, Chi-Hui, Landais, Elise, Nie, Xiaoyan, Pritchard, Laura K., Crispin, Max, Kelsoe, Garnett, Wilson, Ian A., Schuitemaker, Hanneke, Klasse, Per Johan, Moore, John P., Burton, Dennis R., Ward, Andrew B., and Sanders, Rogier W.

Published
2016
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7. Neutralizing Antibody Responses Induced by HIV-1 Envelope Glycoprotein SOSIP Trimers Derived from Elite Neutralizers

Author

Schorcht, Anna, primary, van den Kerkhof, Tom L. G. M., additional, Cottrell, Christopher A., additional, Allen, Joel D., additional, Torres, Jonathan L., additional, Behrens, Anna-Janina, additional, Schermer, Edith E., additional, Burger, Judith A., additional, de Taeye, Steven W., additional, Torrents de la Peña, Alba, additional, Bontjer, Ilja, additional, Gumbs, Stephanie, additional, Ozorowski, Gabriel, additional, LaBranche, Celia C., additional, de Val, Natalia, additional, Yasmeen, Anila, additional, Klasse, Per Johan, additional, Montefiori, David C., additional, Moore, John P., additional, Schuitemaker, Hanneke, additional, Crispin, Max, additional, van Gils, Marit J., additional, Ward, Andrew B., additional, and Sanders, Rogier W., additional

Published
2020
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9. The Envelope-Based Fusion Antigen GP120C14K Forming Hexamer-Like Structures Triggers T Cell and Neutralizing Antibody Responses Against HIV-1

Author

Raman, Suresh C., primary, Mejías-Pérez, Ernesto, additional, Gomez, Carmen E., additional, García-Arriaza, Juan, additional, Perdiguero, Beatriz, additional, Vijayan, Aneesh, additional, Pérez-Ruiz, Mar, additional, Cuervo, Ana, additional, Santiago, César, additional, Sorzano, Carlos Oscar S., additional, Sánchez-Corzo, Cristina, additional, Moog, Christiane, additional, Burger, Judith A., additional, Schorcht, Anna, additional, Sanders, Rogier W., additional, Carrascosa, José L., additional, and Esteban, Mariano, additional

Published
2019
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10. Stabilization of the gp120 V3 loop through hydrophobic interactions reduces the immunodominant V3-directed non-neutralizing response to HIV-1 envelope trimers

Author

de Taeye, Steven W., Torrents de la Peña, Alba, Vecchione, Andrea, Scutigliani, Enzo, Sliepen, Kwinten, Burger, Judith A., van der Woude, Patricia, Schorcht, Anna, Schermer, Edith E., van Gils, Marit J., LaBranche, Celia C., Montefiori, David C., Wilson, Ian A., Moore, John P., Ward, Andrew B., Sanders, Rogier W., Graduate School, AII - Infectious diseases, Medical Microbiology and Infection Prevention, AII - Amsterdam institute for Infection and Immunity, and Other departments

Abstract

To provide protective immunity against circulating primary HIV-1 strains, a vaccine most likely has to induce broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) spike. Recombinant Env trimers such as the prototype BG505 SOSIP.664 that closely mimic the native Env spike can induce autologous neutralizing antibodies (NAbs) against relatively resistant (tier 2) primary viruses. Ideally, Env immunogens should present broadly neutralizing antibody epitopes but limit the presentation of immunodominant non-NAb epitopes that might induce off-target and potentially interfering responses. The V3 loop in gp120 is such a non-NAb epitope that can effectively elicit non-NAbs when animals are immunized with SOSIP.664 trimers. V3 immunogenicity can be diminished, but not abolished, by reducing the conformational flexibility of trimers via targeted sequence changes, including an A316W substitution in V3, that create the SOSIP.v4.1 and SOSIP.v5.2 variants. Here, we further modified these trimer designs by introducing leucine residues at V3 positions 306 and 308 to create hydrophobic interactions with the tryptophan residue at position 316 and with other topologically proximal sites in the V1V2 domain. Together, these modifications further stabilized the resulting SOSIP.v5.2 S306L/R308L trimers in the prefusion state in which V3 is sequestered. When we tested these trimers as immunogens in rabbits, the induction of V3 non-NAbs was significantly reduced compared with the SOSIP.v5.2 trimers and even more so compared with the SOSIP.664 prototype, without affecting the autologous NAb response. Hence, these additional trimer sequence modifications may be beneficial for immunization strategies that seek to minimize off-target non-NAb responses

Published
2018

11. Closing and Opening Holes in the Glycan Shield of HIV-1 Envelope Glycoprotein SOSIP Trimers Can Redirect the Neutralizing Antibody Response to the Newly Unmasked Epitopes

Author

Ringe, Rajesh P., primary, Pugach, Pavel, additional, Cottrell, Christopher A., additional, LaBranche, Celia C., additional, Seabright, Gemma E., additional, Ketas, Thomas J., additional, Ozorowski, Gabriel, additional, Kumar, Sonu, additional, Schorcht, Anna, additional, van Gils, Marit J., additional, Crispin, Max, additional, Montefiori, David C., additional, Wilson, Ian A., additional, Ward, Andrew B., additional, Sanders, Rogier W., additional, Klasse, P. J., additional, and Moore, John P., additional

Published
2019
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12. Stabilization of the gp120 V3 loop through hydrophobic interactions reduces the immunodominant V3-directed non-neutralizing response to HIV-1 envelope trimers.

Author

de Taeye SW, de la Peña AT, Vecchione A, Scutigliani E, Sliepen K, Burger JA, van der Woude P, Schorcht A, Schermer EE, van Gils MJ, LaBranche CC, Montefiori DC, Wilson IA, Moore JP, Ward AB, and Sanders RW

Subjects
Antibodies, Neutralizing immunology, Epitopes immunology, HEK293 Cells, HIV Antibodies immunology, HIV Envelope Protein gp120 immunology, Humans, Hydrophobic and Hydrophilic Interactions, Protein Stability, Antibodies, Neutralizing chemistry, Epitopes chemistry, HIV Antibodies chemistry, HIV Envelope Protein gp120 chemistry, Protein Multimerization
Abstract

To provide protective immunity against circulating primary HIV-1 strains, a vaccine most likely has to induce broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) spike. Recombinant Env trimers such as the prototype BG505 SOSIP.664 that closely mimic the native Env spike can induce autologous neutralizing antibodies (NAbs) against relatively resistant (tier 2) primary viruses. Ideally, Env immunogens should present broadly neutralizing antibody epitopes but limit the presentation of immunodominant non-NAb epitopes that might induce off-target and potentially interfering responses. The V3 loop in gp120 is such a non-NAb epitope that can effectively elicit non-NAbs when animals are immunized with SOSIP.664 trimers. V3 immunogenicity can be diminished, but not abolished, by reducing the conformational flexibility of trimers via targeted sequence changes, including an A316W substitution in V3, that create the SOSIP.v4.1 and SOSIP.v5.2 variants. Here, we further modified these trimer designs by introducing leucine residues at V3 positions 306 and 308 to create hydrophobic interactions with the tryptophan residue at position 316 and with other topologically proximal sites in the V1V2 domain. Together, these modifications further stabilized the resulting SOSIP.v5.2 S306L/R308L trimers in the prefusion state in which V3 is sequestered. When we tested these trimers as immunogens in rabbits, the induction of V3 non-NAbs was significantly reduced compared with the SOSIP.v5.2 trimers and even more so compared with the SOSIP.664 prototype, without affecting the autologous NAb response. Hence, these additional trimer sequence modifications may be beneficial for immunization strategies that seek to minimize off-target non-NAb responses., (© 2018 by The American Society for Biochemistry and Molecular Biology, Inc.)

Published
2018
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