Title : Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site.

Pub. Date : 2016 Nov 15

PMID : 27581986






6 Functional Relationships(s)
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1 Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site. Polysaccharides CD4 molecule Homo sapiens
2 These glycan-free V5 loops are unusual holes in the glycan shield that may have been necessary for initiating this N276 glycan-dependent CD4 binding site B-cell lineage. Polysaccharides CD4 molecule Homo sapiens
3 These glycan-free V5 loops are unusual holes in the glycan shield that may have been necessary for initiating this N276 glycan-dependent CD4 binding site B-cell lineage. Polysaccharides CD4 molecule Homo sapiens
4 These glycan-free V5 loops are unusual holes in the glycan shield that may have been necessary for initiating this N276 glycan-dependent CD4 binding site B-cell lineage. Polysaccharides CD4 molecule Homo sapiens
5 In this study, we isolate a narrowly neutralizing N276 glycan-dependent antibody and use X-ray crystallography and viral deep sequencing to describe how gp120 lacking glycans in V5 might have elicited these early glycan-dependent CD4 binding site antibodies. Polysaccharides CD4 molecule Homo sapiens
6 These data highlight how glycan holes can play a role in the elicitation of B-cell lineages targeting the CD4 binding site. Polysaccharides CD4 molecule Homo sapiens