Structural and genetic convergence of HIV-1 neutralizing antibodies in vaccinated non-human primates
Abstract
A primary goal of HIV-1 vaccine development is the consistent elicitation of protective, neutralizing antibodies. While highly similar neutralizing antibodies (nAbs) have been isolated from multiple HIV-infected individuals, it is unclear whether vaccination can consistently elicit highly similar nAbs in genetically diverse primates. Here, we show in three outbred rhesus macaques that immunization with Env elicits a genotypically and phenotypically conserved nAb response. From these vaccinated macaques, we isolated four antibody lineages that had commonalities in immunoglobulin variable, diversity, and joining gene segment usage. Atomic-level structures of the antigen binding fragments of the two most similar antibodies showed nearly identical paratopes. The Env binding modes of each of the four vaccine-induced nAbs were distinct from previously known monoclonal HIV-1 neutralizing antibodies, but were nearly identical to each other. The similarities of these antibodies show that the immune system in outbred primates can respond to HIV-1 Env vaccination with a similar structural and genotypic solution for recognizing a particular neutralizing epitope. These results support rational vaccine design for HIV-1 that aims to reproducibly elicit, in genetically diverse primates, nAbs with specific paratope structures capable of binding conserved epitopes.
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- Publication Date:
- Research Org.:
- Los Alamos National Laboratory (LANL), Los Alamos, NM (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOD; National Institutes of Health (NIH)
- OSTI Identifier:
- 1797877
- Alternate Identifier(s):
- OSTI ID: 1786266; OSTI ID: 1827597
- Report Number(s):
- LA-UR-21-29267
Journal ID: ISSN 1553-7374; 10.1371/journal.ppat.1009624
- Grant/Contract Number:
- W-31-109-Eng-38; AC02-06CH11357; 89233218CNA000001; W81XWH-07-2-0067; R01- AI120801; UM1-AI100645; 5P30 AI064518; HHSN261200800001E
- Resource Type:
- Published Article
- Journal Name:
- PLoS Pathogens
- Additional Journal Information:
- Journal Name: PLoS Pathogens Journal Volume: 17 Journal Issue: 6; Journal ID: ISSN 1553-7374
- Publisher:
- Public Library of Science (PLoS)
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Biological Science
Citation Formats
Cai, Fangping, Chen, Wei-Hung, Wu, Weimin, Jones, Julia A., Choe, Misook, Gohain, Neelakshi, Shen, Xiaoying, LaBranche, Celia, Eaton, Amanda, Sutherland, Laura, Lee, Esther M., Hernandez, Giovanna E., Wu, Nelson R., Scearce, Richard, Seaman, Michael S., Moody, M. Anthony, Santra, Sampa, Wiehe, Kevin, Tomaras, Georgia D., Wagh, Kshitij, Korber, Bette, Bonsignori, Mattia, Montefiori, David C., Haynes, Barton F., de Val, Natalia, Joyce, M. Gordon, Saunders, Kevin O., and Burton, ed., Dennis R. Structural and genetic convergence of HIV-1 neutralizing antibodies in vaccinated non-human primates. United States: N. p., 2021.
Web. doi:10.1371/journal.ppat.1009624.
Cai, Fangping, Chen, Wei-Hung, Wu, Weimin, Jones, Julia A., Choe, Misook, Gohain, Neelakshi, Shen, Xiaoying, LaBranche, Celia, Eaton, Amanda, Sutherland, Laura, Lee, Esther M., Hernandez, Giovanna E., Wu, Nelson R., Scearce, Richard, Seaman, Michael S., Moody, M. Anthony, Santra, Sampa, Wiehe, Kevin, Tomaras, Georgia D., Wagh, Kshitij, Korber, Bette, Bonsignori, Mattia, Montefiori, David C., Haynes, Barton F., de Val, Natalia, Joyce, M. Gordon, Saunders, Kevin O., & Burton, ed., Dennis R. Structural and genetic convergence of HIV-1 neutralizing antibodies in vaccinated non-human primates. United States. https://doi.org/10.1371/journal.ppat.1009624
Cai, Fangping, Chen, Wei-Hung, Wu, Weimin, Jones, Julia A., Choe, Misook, Gohain, Neelakshi, Shen, Xiaoying, LaBranche, Celia, Eaton, Amanda, Sutherland, Laura, Lee, Esther M., Hernandez, Giovanna E., Wu, Nelson R., Scearce, Richard, Seaman, Michael S., Moody, M. Anthony, Santra, Sampa, Wiehe, Kevin, Tomaras, Georgia D., Wagh, Kshitij, Korber, Bette, Bonsignori, Mattia, Montefiori, David C., Haynes, Barton F., de Val, Natalia, Joyce, M. Gordon, Saunders, Kevin O., and Burton, ed., Dennis R. Fri .
"Structural and genetic convergence of HIV-1 neutralizing antibodies in vaccinated non-human primates". United States. https://doi.org/10.1371/journal.ppat.1009624.
@article{osti_1797877,
title = {Structural and genetic convergence of HIV-1 neutralizing antibodies in vaccinated non-human primates},
author = {Cai, Fangping and Chen, Wei-Hung and Wu, Weimin and Jones, Julia A. and Choe, Misook and Gohain, Neelakshi and Shen, Xiaoying and LaBranche, Celia and Eaton, Amanda and Sutherland, Laura and Lee, Esther M. and Hernandez, Giovanna E. and Wu, Nelson R. and Scearce, Richard and Seaman, Michael S. and Moody, M. Anthony and Santra, Sampa and Wiehe, Kevin and Tomaras, Georgia D. and Wagh, Kshitij and Korber, Bette and Bonsignori, Mattia and Montefiori, David C. and Haynes, Barton F. and de Val, Natalia and Joyce, M. Gordon and Saunders, Kevin O. and Burton, ed., Dennis R.},
abstractNote = {A primary goal of HIV-1 vaccine development is the consistent elicitation of protective, neutralizing antibodies. While highly similar neutralizing antibodies (nAbs) have been isolated from multiple HIV-infected individuals, it is unclear whether vaccination can consistently elicit highly similar nAbs in genetically diverse primates. Here, we show in three outbred rhesus macaques that immunization with Env elicits a genotypically and phenotypically conserved nAb response. From these vaccinated macaques, we isolated four antibody lineages that had commonalities in immunoglobulin variable, diversity, and joining gene segment usage. Atomic-level structures of the antigen binding fragments of the two most similar antibodies showed nearly identical paratopes. The Env binding modes of each of the four vaccine-induced nAbs were distinct from previously known monoclonal HIV-1 neutralizing antibodies, but were nearly identical to each other. The similarities of these antibodies show that the immune system in outbred primates can respond to HIV-1 Env vaccination with a similar structural and genotypic solution for recognizing a particular neutralizing epitope. These results support rational vaccine design for HIV-1 that aims to reproducibly elicit, in genetically diverse primates, nAbs with specific paratope structures capable of binding conserved epitopes.},
doi = {10.1371/journal.ppat.1009624},
journal = {PLoS Pathogens},
number = 6,
volume = 17,
place = {United States},
year = {Fri Jun 04 00:00:00 EDT 2021},
month = {Fri Jun 04 00:00:00 EDT 2021}
}
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