HIV-1 gp120 Determinants Proximal to the CD4 Binding Site Shift Protective Glycans That Are Targeted by Monoclonal Antibody 2G12

https://hdl.handle.net/20.500.12080/50770

dc.contributor.author	Clapham, Paul R.
dc.contributor.author	Dueñas Decamp, María José
dc.date.accessioned	2025-10-27T12:09:52Z
dc.date.available	2025-10-27T12:09:52Z
dc.date.created	2010
dc.date.issued	2010
dc.identifier.uri	https://hdl.handle.net/20.500.12080/50770
dc.description.abstract	HIV-1 R5 envelopes vary considerably in their capacities to exploit low CD4 levels on macrophages for infection and in their sensitivities to the CD4 binding site (CD4bs) monoclonal antibody (MAb) b12 and the glycan-specific MAb 2G12. Here, we show that nonglycan determinants flanking the CD4 binding loop, which affect exposure of the CD4bs, also modulate 2G12 neutralization. Our data indicate that such residues act via a mechanism that involves shifts in the orientation of proximal glycans, thus modulating the sensitivity of 2G12 neutralization and affecting the overall presentation and structure of the glycan shield.	es_ES
dc.format	application/pdf	es_ES
dc.language	eng	es_ES
dc.publisher	ASM	es_ES
dc.rights	CC-BY	es_ES
dc.rights.uri	http://creativecommons.org/licenses/by/4.0/deed.es	es_ES
dc.source	Journal of Virology	es_ES
dc.title	HIV-1 gp120 Determinants Proximal to the CD4 Binding Site Shift Protective Glycans That Are Targeted by Monoclonal Antibody 2G12	es_ES
dc.type	Artículo	es_ES
dc.description.curso	2010	es_ES
dc.rights.accessrights	info:eu-repo/semantics/openAccess	es_ES
dc.identifier.dl	2010
dc.identifier.location	N/A	es_ES