{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["D'Addabbo A"],"funding":["National Institutes of Health","IAVI Neutralizing Antibody Center through the Collaboration for AIDS Vaccine Discovery","NIH HHS"],"pagination":["cwae063"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11442005"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["34(11)"],"pubmed_abstract":["Broadly neutralizing antibodies (bNAbs) isolated from HIV-1 infected donors are vaccine paradigms. These bNAbs recognize envelope glycoprotein trimers that carry 75-90 oligomannose and complex-type glycans. Although bNAbs and their precursors must navigate past glycans, they usually also make some glycan contacts. Glycan-modified vaccines may therefore be useful to initiate and guide bNAb development. Here, we describe two ways to modify Env glycans for possible vaccine use: 1) using a cocktail of glycosidases (termed \"NGAF3\" (Neuraminidase, β-Galactosidase, N-Acetylglucosaminidase, endoglycosidase F3 (endo F3)) to deplete complex glycans to try to minimize bNAb-glycan clashes and 2) co-expressing β-1,4-galactosyltransferase 1 (B4G) and β-galactoside α-2,6 sialyltransferase 1 (ST6) during "],"journal":["Glycobiology"],"pubmed_title":["Impact of glycan depletion, glycan debranching and increased glycan charge on HIV-1 neutralization sensitivity and immunogenicity."],"pmcid":["PMC11442005"],"funding_grant_id":["AI93278","AI00790","OPP1153692/INV-008813"],"pubmed_authors":["D'Addabbo A","Binley JM","Thomas A","Osawa K","Allen JD","Crooks ET","Tong T","Xu J","Crispin M"],"additional_accession":[]},"is_claimable":false,"name":"Impact of glycan depletion, glycan debranching and increased glycan charge on HIV-1 neutralization sensitivity and immunogenicity.","description":"Broadly neutralizing antibodies (bNAbs) isolated from HIV-1 infected donors are vaccine paradigms. These bNAbs recognize envelope glycoprotein trimers that carry 75-90 oligomannose and complex-type glycans. Although bNAbs and their precursors must navigate past glycans, they usually also make some glycan contacts. Glycan-modified vaccines may therefore be useful to initiate and guide bNAb development. Here, we describe two ways to modify Env glycans for possible vaccine use: 1) using a cocktail of glycosidases (termed \"NGAF3\" (Neuraminidase, β-Galactosidase, N-Acetylglucosaminidase, endoglycosidase F3 (endo F3)) to deplete complex glycans to try to minimize bNAb-glycan clashes and 2) co-expressing β-1,4-galactosyltransferase 1 (B4G) and β-galactoside α-2,6 sialyltransferase 1 (ST6) during ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2026-04-07T13:24:05.612Z","creation":"2026-04-07T13:21:09.669Z"},"accession":"S-EPMC11442005","cross_references":{"pubmed":["39115361"],"doi":["10.1093/glycob/cwae063"]}}