Molecular Basis of Unusually High Neutralization Resistance in Tier 3 HIV-1 Strain 253-11
Abstract
Understanding the mechanisms used by HIV-1 to evade antibody neutralization may contribute to the design of a high-coverage vaccine. The tier 3 virus 253-11 is poorly neutralized by subtype-matched and subtype C sera, even compared to other tier 3 viruses, and is also recognized poorly by V3/glycan-targeting monoclonal antibodies (MAbs). We found that sequence polymorphisms in the V3 loop and N-linked glycosylation sites contribute only minimally to the high neutralization resistance of 253-11. Interestingly, the 253-11 membrane-proximal external region (MPER) is rarely recognized by sera in the context of the wild-type virus but is commonly recognized in the context of an HIV-2 chimera, suggesting steric or kinetic hindrance of binding to MPER in the native envelope (Env). Mutations in the 253-11 MPER, which were previously reported to increase the lifetime of the prefusion Env conformation, affected the resistance of 253-11 to antibodies targeting various epitopes on HIV-1 Env, presumably destabilizing its otherwise stable, closed trimer structure. To gain insight into the structure of 253-11, we constructed and crystallized a recombinant 253-11 SOSIP trimer. The resulting structure revealed that the heptad repeat helices in gp41 are drawn in close proximity to the trimer axis and that gp120 protomers also showed amore »
- Authors:
-
[8];
- Univ. of Cape Town (South Africa); National Inst. for Communicable Diseases, Johannesburg (South Africa)
- The Hospital for Sick Children Research Institute, Toronto, ON (Canada)
- Univ. of Cape Town (South Africa); International Centre for Genetic Engineering and Biotechnology, Cape Town (South Africa); Univ. of Western Ontario, London, ON (Canada)
- The Hospital for Sick Children Research Institute, Toronto, ON (Canada); Univ. of Toronto, ON (Canada); Univ. of Oxford (England)
- Univ. of Cape Town (South Africa); International Centre for Genetic Engineering and Biotechnology, Cape Town (South Africa); Univ. of Eldoret (Kenya)
- Univ. of Cape Town (South Africa); International Centre for Genetic Engineering and Biotechnology, Cape Town (South Africa)
- The Hospital for Sick Children Research Institute, Toronto, ON (Canada); Univ. of Toronto, ON (Canada)
- Univ. of Cape Town (South Africa); Univ. of the Witwatersrand, Johannesburg (South Africa)
- Emory Univ., Atlanta, GA (United States)
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC); National Inst. of Health
- OSTI Identifier:
- 1463741
- Grant/Contract Number:
- AC02-06CH11357; P41 GM103622; NIH-150414
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Journal of Virology
- Additional Journal Information:
- Journal Volume: 92; Journal Issue: 14; Journal ID: ISSN 0022-538X
- Publisher:
- American Society for Microbiology
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; HIV-1; HIV-1 vaccine; antibody; neutralization
Citation Formats
Moyo, Thandeka, Ereño-Orbea, June, Jacob, Rajesh Abraham, Pavillet, Clara E., Kariuki, Samuel Mundia, Tangie, Emily N., Julien, Jean-Philippe, Dorfman, Jeffrey R., and Silvestri, Guido. Molecular Basis of Unusually High Neutralization Resistance in Tier 3 HIV-1 Strain 253-11. United States: N. p., 2018.
Web. doi:10.1128/JVI.02261-17.
Moyo, Thandeka, Ereño-Orbea, June, Jacob, Rajesh Abraham, Pavillet, Clara E., Kariuki, Samuel Mundia, Tangie, Emily N., Julien, Jean-Philippe, Dorfman, Jeffrey R., & Silvestri, Guido. Molecular Basis of Unusually High Neutralization Resistance in Tier 3 HIV-1 Strain 253-11. United States. https://doi.org/10.1128/JVI.02261-17
Moyo, Thandeka, Ereño-Orbea, June, Jacob, Rajesh Abraham, Pavillet, Clara E., Kariuki, Samuel Mundia, Tangie, Emily N., Julien, Jean-Philippe, Dorfman, Jeffrey R., and Silvestri, Guido. Wed .
"Molecular Basis of Unusually High Neutralization Resistance in Tier 3 HIV-1 Strain 253-11". United States. https://doi.org/10.1128/JVI.02261-17. https://www.osti.gov/servlets/purl/1463741.
@article{osti_1463741,
title = {Molecular Basis of Unusually High Neutralization Resistance in Tier 3 HIV-1 Strain 253-11},
author = {Moyo, Thandeka and Ereño-Orbea, June and Jacob, Rajesh Abraham and Pavillet, Clara E. and Kariuki, Samuel Mundia and Tangie, Emily N. and Julien, Jean-Philippe and Dorfman, Jeffrey R. and Silvestri, Guido},
abstractNote = {Understanding the mechanisms used by HIV-1 to evade antibody neutralization may contribute to the design of a high-coverage vaccine. The tier 3 virus 253-11 is poorly neutralized by subtype-matched and subtype C sera, even compared to other tier 3 viruses, and is also recognized poorly by V3/glycan-targeting monoclonal antibodies (MAbs). We found that sequence polymorphisms in the V3 loop and N-linked glycosylation sites contribute only minimally to the high neutralization resistance of 253-11. Interestingly, the 253-11 membrane-proximal external region (MPER) is rarely recognized by sera in the context of the wild-type virus but is commonly recognized in the context of an HIV-2 chimera, suggesting steric or kinetic hindrance of binding to MPER in the native envelope (Env). Mutations in the 253-11 MPER, which were previously reported to increase the lifetime of the prefusion Env conformation, affected the resistance of 253-11 to antibodies targeting various epitopes on HIV-1 Env, presumably destabilizing its otherwise stable, closed trimer structure. To gain insight into the structure of 253-11, we constructed and crystallized a recombinant 253-11 SOSIP trimer. The resulting structure revealed that the heptad repeat helices in gp41 are drawn in close proximity to the trimer axis and that gp120 protomers also showed a relatively compact disposition around the trimer axis. Furthermore, these observations give substantial insight into the molecular features of an envelope spike from a tier 3 virus and into possible mechanisms that may contribute to its unusually high neutralization resistance.},
doi = {10.1128/JVI.02261-17},
journal = {Journal of Virology},
number = 14,
volume = 92,
place = {United States},
year = {Wed Apr 04 00:00:00 EDT 2018},
month = {Wed Apr 04 00:00:00 EDT 2018}
}
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Works referencing / citing this record:
Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements
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