Chinks in the armor of the HIV-1 Envelope glycan shield: implications for immune escape from anti-glycan broadly neutralizing antibodies

 

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dc.contributor.author Moyo, Thandeka
dc.contributor.author Ferreira, Roux-cil
dc.contributor.author Davids, Reyaaz
dc.contributor.author Sonday, Zarinah
dc.contributor.author Moore, Penny L
dc.contributor.author Travers, Simon A
dc.contributor.author Wood, Natasha T
dc.contributor.author Dorfman, Jeffrey Robert
dc.date.accessioned 2017-09-14T12:43:07Z
dc.date.available 2017-07-15
dc.date.available 2017-09-14T12:43:07Z
dc.date.issued 2017-01-15
dc.identifier.citation Moyo, T., Ferreira, R. C., Davids, R., Sonday, Z., Moore, P. L., Travers, S. A., ... & Dorfman, J. R. (2017). Chinks in the armor of the HIV-1 Envelope glycan shield: Implications for immune escape from anti-glycan broadly neutralizing antibodies. Virology, 501, 12-24. en_ZA
dc.identifier.uri http://hdl.handle.net/11427/25211
dc.description.abstract Glycans on HIV-1 Envelope serve multiple functions including blocking epitopes from antibodies. We show that removal of glycan 301, a major target of anti-V3/glycan antibodies, has substantially different effects in two viruses. While glycan 301 on Du156.12 blocks epitopes commonly recognized by sera from chronically HIV-1-infected individuals, it does not do so on CAP45.G3, suggesting that removing the 301 glycan has a smaller effect on the integrity of the glycan shield in CAP45.G3. Changes in sensitivity to broadly neutralizing monoclonal antibodies suggest that the interaction between glycan 301 and the CD4 binding site differ substantially between these 2 viruses. Molecular modeling suggests that removal of glycan 301 likely exposes a greater surface area of the V3 and C4 regions in Du156.12. Our data indicate that the contribution of the 301 glycan to resistance to common neutralizing antibodies varies between viruses, allowing for easier selection for its loss in some viruses. en_ZA
dc.language eng en_ZA
dc.publisher Elsevier en_ZA
dc.source Virology en_ZA
dc.source.uri https://www.journals.elsevier.com/virology
dc.subject.other HIV-1
dc.subject.other neutralising antibody
dc.title Chinks in the armor of the HIV-1 Envelope glycan shield: implications for immune escape from anti-glycan broadly neutralizing antibodies en_ZA
dc.type Journal Article en_ZA
uct.type.publication Research en_ZA
uct.type.resource Article en_ZA
dc.publisher.institution University of Cape Town
dc.publisher.faculty Faculty of Health Sciences en_ZA
dc.publisher.department Division of Immunology en_ZA
uct.type.filetype Text
uct.type.filetype Image
dc.identifier.apacitation Moyo, T., Ferreira, R., Davids, R., Sonday, Z., Moore, P. L., Travers, S. A., ... Dorfman, J. R. (2017). Chinks in the armor of the HIV-1 Envelope glycan shield: implications for immune escape from anti-glycan broadly neutralizing antibodies. <i>Virology</i>, http://hdl.handle.net/11427/25211 en_ZA
dc.identifier.chicagocitation Moyo, Thandeka, Roux-cil Ferreira, Reyaaz Davids, Zarinah Sonday, Penny L Moore, Simon A Travers, Natasha T Wood, and Jeffrey Robert Dorfman "Chinks in the armor of the HIV-1 Envelope glycan shield: implications for immune escape from anti-glycan broadly neutralizing antibodies." <i>Virology</i> (2017) http://hdl.handle.net/11427/25211 en_ZA
dc.identifier.vancouvercitation Moyo T, Ferreira R, Davids R, Sonday Z, Moore PL, Travers SA, et al. Chinks in the armor of the HIV-1 Envelope glycan shield: implications for immune escape from anti-glycan broadly neutralizing antibodies. Virology. 2017; http://hdl.handle.net/11427/25211. en_ZA
dc.identifier.ris TY - Journal Article AU - Moyo, Thandeka AU - Ferreira, Roux-cil AU - Davids, Reyaaz AU - Sonday, Zarinah AU - Moore, Penny L AU - Travers, Simon A AU - Wood, Natasha T AU - Dorfman, Jeffrey Robert AB - Glycans on HIV-1 Envelope serve multiple functions including blocking epitopes from antibodies. We show that removal of glycan 301, a major target of anti-V3/glycan antibodies, has substantially different effects in two viruses. While glycan 301 on Du156.12 blocks epitopes commonly recognized by sera from chronically HIV-1-infected individuals, it does not do so on CAP45.G3, suggesting that removing the 301 glycan has a smaller effect on the integrity of the glycan shield in CAP45.G3. Changes in sensitivity to broadly neutralizing monoclonal antibodies suggest that the interaction between glycan 301 and the CD4 binding site differ substantially between these 2 viruses. Molecular modeling suggests that removal of glycan 301 likely exposes a greater surface area of the V3 and C4 regions in Du156.12. Our data indicate that the contribution of the 301 glycan to resistance to common neutralizing antibodies varies between viruses, allowing for easier selection for its loss in some viruses. DA - 2017-01-15 DB - OpenUCT DP - University of Cape Town J1 - Virology LK - https://open.uct.ac.za PB - University of Cape Town PY - 2017 T1 - Chinks in the armor of the HIV-1 Envelope glycan shield: implications for immune escape from anti-glycan broadly neutralizing antibodies TI - Chinks in the armor of the HIV-1 Envelope glycan shield: implications for immune escape from anti-glycan broadly neutralizing antibodies UR - http://hdl.handle.net/11427/25211 ER - en_ZA


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