{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Venditto VJ"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["1086-93"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4135905"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(8)"],"pubmed_abstract":["Broadly neutralizing monoclonal antibodies (bNAbs) 2F5 and 4E10 bind to the membrane proximal external region (MPER) of gp41 and also cross-react with phospholipids. In this study, we investigated if chemical modifications on the MPER adjacent to 2F5 and 4E10 epitopes using mimetics of inflammation-associated posttranslational modifications to induce 2F5- and 4E10-like bNAbs can break tolerance. We synthesized a series of chemically modified peptides spanning the MPER. The serine, threonine, and tyrosine residues in the peptides were modified with sulfate, phosphate, or nitrate moieties and presented in liposomes for rabbit immunizations. All immunizations resulted in high antisera titers directed toward both the modified and unmodified immunogens. Tyrosine modification was observed to sig"],"journal":["Clinical and vaccine immunology : CVI"],"pubmed_title":["Chemically modified peptides based on the membrane-proximal external region of the HIV-1 envelope induce high-titer, epitope-specific nonneutralizing antibodies in rabbits."],"pmcid":["PMC4135905"],"funding_grant_id":["F32 AI095062","R21 AI093135","R01 GM061851","F32AI095062"],"pubmed_authors":["Landucci G","Levy JA","Forthal D","Teque F","Watson DS","Polonis VR","Venditto VJ","Wieczorek L","Szoka FC","Molnar S"],"additional_accession":[]},"is_claimable":false,"name":"Chemically modified peptides based on the membrane-proximal external region of the HIV-1 envelope induce high-titer, epitope-specific nonneutralizing antibodies in rabbits.","description":"Broadly neutralizing monoclonal antibodies (bNAbs) 2F5 and 4E10 bind to the membrane proximal external region (MPER) of gp41 and also cross-react with phospholipids. In this study, we investigated if chemical modifications on the MPER adjacent to 2F5 and 4E10 epitopes using mimetics of inflammation-associated posttranslational modifications to induce 2F5- and 4E10-like bNAbs can break tolerance. We synthesized a series of chemically modified peptides spanning the MPER. The serine, threonine, and tyrosine residues in the peptides were modified with sulfate, phosphate, or nitrate moieties and presented in liposomes for rabbit immunizations. All immunizations resulted in high antisera titers directed toward both the modified and unmodified immunogens. Tyrosine modification was observed to sig","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Aug","modification":"2025-04-22T00:59:27.834Z","creation":"2019-03-27T01:34:14Z"},"accession":"S-EPMC4135905","cross_references":{"pubmed":["24872518"],"doi":["10.1128/CVI.00320-14","10.1128/cvi.00320-14"]}}