2012
DOI: 10.1186/1742-4690-9-s2-p346
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Structural definition of a novel CD4-induced epitope that is targeted by a single-headed immunoglobulin to effect broad and potent HIV neutralization

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“…Epitopes on exposed peptide regions rapidly mutate, because of the error-prone nature of the viral reverse transcriptase, thereby pressuring the immune system to constantly produce new antibodies. In contrast, many of the structurally conserved portions of the envelope spike are masked by extensive glycosylation or are otherwise sterically occluded (7)(8)(9)(10). Other conserved potential antibody targets are only transiently exposed during the receptor-induced conformational changes associated with the fusion process.…”
mentioning
confidence: 99%
“…Epitopes on exposed peptide regions rapidly mutate, because of the error-prone nature of the viral reverse transcriptase, thereby pressuring the immune system to constantly produce new antibodies. In contrast, many of the structurally conserved portions of the envelope spike are masked by extensive glycosylation or are otherwise sterically occluded (7)(8)(9)(10). Other conserved potential antibody targets are only transiently exposed during the receptor-induced conformational changes associated with the fusion process.…”
mentioning
confidence: 99%