Author: Alam, S.M.; Aussedat, B.; Vohra, Y.; Ryan Meyerhoff, R.; Cale, E.M.; Walkowicz, W.E.; Radakovich, N.A.; Anasti, K.; Armand, L.; Parks, R.; Sutherland, L.; Scearce, R.; Joyce, M.G.; Pancera, M.; Druz, A.; Georgiev, I.S.; Von Holle, T.; Eaton, A.; Fox, C.; Reed, S.G.; Louder, M.; Bailer, R.T.; Morris, L.; Abdool-Karim, S.S.; Cohen, M.; Liao, H.-X.; Montefiori, D.C.; Park, P.K.; Fernandez-Tejada, A.; Wiehe, K.; Santra, S.; Kepler, T.B.; Saunders, K.O.; Sodroski, J.; Kwong, P.D.; Mascola, J.R.; Bonsignori, M.; Moody, M.A.; Danishefsky, S.; Haynes, B.F.
Description: A goal for an HIV-1 vaccine is to overcome virus variability by inducing broadly neutralizing antibodies (bnAbs). One key target of bnAbs is the glycan-polypeptide at the base of the envelope (Env) third variable loop (V3). We have designed and synthesized a homogeneous minimal immunogen with high-mannose glycans reflective of a native Env V3-glycan bnAb epitope (Man9-V3). V3-glycan bnAbs bound to Man9-V3 glycopeptide and native-like gp140 trimers with similar affinities. Fluorophore-labeled Man9-V3 glycopeptides bound to bnAb memory B cells and were able to be used to isolate a V3-glycan bnAb from an HIV-1-infected individual. In rhesus macaques, immunization with Man9-V3 induced V3-glycan-targeted antibodies. Thus, the Man9-V3 glycopeptide closely mimics an HIV-1 V3-glycan bnAb epitope and can be used to isolate V3-glycan bnAbs.
Subject headings:
Publication year: 2017
Journal or book title: Science Translational Medicine
Volume: 9
Issue: 381
Pages:
Find the full text :Â https://www.science.org/doi/abs/10.1126/scitranslmed.aai7521
Find more like this one (cited by): https://scholar.google.com/scholar?cites=4765419288326545429&as_sdt=1000005&sciodt=0,16&hl=en
Type: Journal Article
Serial number: 1919