{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wibmer CK"],"funding":["FIC NIH HHS","NIAID NIH HHS"],"pagination":["10220-10235"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5105658"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["90(22)"],"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,"],"journal":["Journal of virology"],"pubmed_title":["Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site."],"pmcid":["PMC5105658"],"funding_grant_id":["D43 TW000231","U19 AI051794","U01 AI116086"],"pubmed_authors":["Bailer RT","Schmidt SD","Gorman J","Louder MK","Abdool Karim SS","Labuschagne P","Moore PL","Druz A","York T","Mascola JR","Williamson C","Morris L","Anthony CS","Mkhize NN","Wibmer CK","Kwong PD"],"additional_accession":[]},"is_claimable":false,"name":"Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding Site.","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,","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Nov","modification":"2026-05-02T02:34:19.611Z","creation":"2019-03-27T02:28:50Z"},"accession":"S-EPMC5105658","cross_references":{"pubmed":["27581986"],"doi":["10.1128/JVI.01357-16"]}}