<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wibmer CK</submitter><funding>FIC NIH HHS</funding><funding>NIAID NIH HHS</funding><pagination>10220-10235</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5105658</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>90(22)</volume><pubmed_abstract>All HIV-1-infected individuals develop strain-specific neutralizing antibodies to their infecting virus, which in some cases mature into broadly neutralizing antibodies. Defining the epitopes of strain-specific antibodies that overlap conserved sites of vulnerability might provide mechanistic insights into how broadly neutralizing antibodies arise. We previously described an HIV-1 clade C-infected donor, CAP257, who developed broadly neutralizing plasma antibodies targeting an N276 glycan-dependent epitope in the CD4 binding site. The initial CD4 binding site response potently neutralized the heterologous tier 2 clade B viral strain RHPA, which was used to design resurfaced gp120 antigens for single-B-cell sorting. Here we report the isolation and structural characterization of CAP257-RH1,</pubmed_abstract><journal>Journal of virology</journal><pubmed_title>Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site.</pubmed_title><pmcid>PMC5105658</pmcid><funding_grant_id>D43 TW000231</funding_grant_id><funding_grant_id>U19 AI051794</funding_grant_id><funding_grant_id>U01 AI116086</funding_grant_id><pubmed_authors>Bailer RT</pubmed_authors><pubmed_authors>Schmidt SD</pubmed_authors><pubmed_authors>Gorman J</pubmed_authors><pubmed_authors>Louder MK</pubmed_authors><pubmed_authors>Abdool Karim SS</pubmed_authors><pubmed_authors>Labuschagne P</pubmed_authors><pubmed_authors>Moore PL</pubmed_authors><pubmed_authors>Druz A</pubmed_authors><pubmed_authors>York T</pubmed_authors><pubmed_authors>Mascola JR</pubmed_authors><pubmed_authors>Williamson C</pubmed_authors><pubmed_authors>Morris L</pubmed_authors><pubmed_authors>Anthony CS</pubmed_authors><pubmed_authors>Mkhize NN</pubmed_authors><pubmed_authors>Wibmer CK</pubmed_authors><pubmed_authors>Kwong PD</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site.</name><description>All HIV-1-infected individuals develop strain-specific neutralizing antibodies to their infecting virus, which in some cases mature into broadly neutralizing antibodies. Defining the epitopes of strain-specific antibodies that overlap conserved sites of vulnerability might provide mechanistic insights into how broadly neutralizing antibodies arise. We previously described an HIV-1 clade C-infected donor, CAP257, who developed broadly neutralizing plasma antibodies targeting an N276 glycan-dependent epitope in the CD4 binding site. The initial CD4 binding site response potently neutralized the heterologous tier 2 clade B viral strain RHPA, which was used to design resurfaced gp120 antigens for single-B-cell sorting. Here we report the isolation and structural characterization of CAP257-RH1,</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Nov</publication><modification>2026-05-02T02:34:19.611Z</modification><creation>2019-03-27T02:28:50Z</creation></dates><accession>S-EPMC5105658</accession><cross_references><pubmed>27581986</pubmed><doi>10.1128/JVI.01357-16</doi></cross_references></HashMap>