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HIV Seropositivity: HELP
Articles by Roux-Cil Ferreira
Based on 1 article published since 2010
(Why 1 article?)

Between 2010 and 2020, Roux-Cil Ferreira wrote the following article about HIV Seropositivity.
+ Citations + Abstracts
1 Article Structural Rearrangements Maintain the Glycan Shield of an HIV-1 Envelope Trimer After the Loss of a Glycan. 2018

Ferreira, Roux-Cil / Grant, Oliver C / Moyo, Thandeka / Dorfman, Jeffrey R / Woods, Robert J / Travers, Simon A / Wood, Natasha T. ·South African Medical Research Council Bioinformatics Unit, South African National Bioinformatics Institute, University of the Western Cape, Cape Town, South Africa. · Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, United States. · Division of Immunology, Department of Pathology, University of Cape Town, Cape Town, South Africa. · Division of Immunology, School of Pathology, University of the Witwatersrand, Johannesburg, South Africa. · University of Cape Town, UCT Computational Biology Group, Department of Integrated Biomedical Sciences, Institute of Infectious Disease and Molecular Medicine, Cape Town, South Africa. wood.natasha@gmail.com. ·Sci Rep · Pubmed #30302011.

ABSTRACT: The HIV-1 envelope (Env) glycoprotein is the primary target of the humoral immune response and a critical vaccine candidate. However, Env is densely glycosylated and thereby substantially protected from neutralisation. Importantly, glycan N301 shields V3 loop and CD4 binding site epitopes from neutralising antibodies. Here, we use molecular dynamics techniques to evaluate the structural rearrangements that maintain the protective qualities of the glycan shield after the loss of glycan N301. We examined a naturally occurring subtype C isolate and its N301A mutant; the mutant not only remained protected against neutralising antibodies targeting underlying epitopes, but also exhibited an increased resistance to the VRC01 class of broadly neutralising antibodies. Analysis of this mutant revealed several glycans that were responsible, independently or through synergy, for the neutralisation resistance of the mutant. These data provide detailed insight into the glycan shield's ability to compensate for the loss of a glycan, as well as the cascade of glycan movements on a protomer, starting at the point mutation, that affects the integrity of an antibody epitope located at the edge of the diminishing effect. These results present key, previously overlooked, considerations for HIV-1 Env glycan research and related vaccine studies.