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Mimicry of an HIV broadly neutralizing antibody epitope with a synthetic glycopeptide.
Alam, S Munir; Aussedat, Baptiste; Vohra, Yusuf; Meyerhoff, R Ryan; Cale, Evan M; Walkowicz, William E; Radakovich, Nathan A; Anasti, Kara; Armand, Lawrence; Parks, Robert; Sutherland, Laura; Scearce, Richard; Joyce, M Gordon; Pancera, Marie; Druz, Aliaksandr; Georgiev, Ivelin S; Von Holle, Tarra; Eaton, Amanda; Fox, Christopher; Reed, Steven G; Louder, Mark; Bailer, Robert T; Morris, Lynn; Abdool-Karim, Salim S; Cohen, Myron; Liao, Hua-Xin; Montefiori, David C; Park, Peter K; Fernández-Tejada, Alberto; Wiehe, Kevin; Santra, Sampa; Kepler, Thomas B; Saunders, Kevin O; Sodroski, Joseph; Kwong, Peter D; Mascola, John R; Bonsignori, Mattia; Moody, M Anthony; Danishefsky, Samuel; Haynes, Barton F.
Afiliação
  • Alam SM; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Aussedat B; Department of Medicine, Duke University School of Medicine, Durham, NC 27710, USA.
  • Vohra Y; Department of Pathology, Duke University School of Medicine, Durham, NC 27710, USA.
  • Meyerhoff RR; Department of Chemical Biology, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
  • Cale EM; Department of Chemical Biology, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
  • Walkowicz WE; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Radakovich NA; Department of Immunology, Duke University School of Medicine, Durham, NC 27710, USA.
  • Anasti K; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Armand L; Department of Chemical Biology, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
  • Parks R; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Sutherland L; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Scearce R; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Joyce MG; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Pancera M; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Druz A; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Georgiev IS; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Von Holle T; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Eaton A; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Fox C; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Reed SG; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Louder M; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Bailer RT; Infectious Disease Research Institute, Seattle, WA 98102, USA.
  • Morris L; Infectious Disease Research Institute, Seattle, WA 98102, USA.
  • Abdool-Karim SS; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Cohen M; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
  • Liao HX; National Institute for Communicable Diseases, Johannesburg 2131, South Africa.
  • Montefiori DC; Center for the AIDS Programme of Research in South Africa, University of KwaZulu-Natal, Durban 4013, South Africa.
  • Park PK; National Institute for Communicable Diseases, Johannesburg 2131, South Africa.
  • Fernández-Tejada A; Center for the AIDS Programme of Research in South Africa, University of KwaZulu-Natal, Durban 4013, South Africa.
  • Wiehe K; Department of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
  • Santra S; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Kepler TB; Department of Medicine, Duke University School of Medicine, Durham, NC 27710, USA.
  • Saunders KO; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Sodroski J; Department of Medicine, Duke University School of Medicine, Durham, NC 27710, USA.
  • Kwong PD; Department of Surgery, Duke University School of Medicine, Durham, NC 27710, USA.
  • Mascola JR; Department of Chemical Biology, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
  • Bonsignori M; Department of Chemical Biology, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
  • Moody MA; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA.
  • Danishefsky S; Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.
  • Haynes BF; Department of Microbiology, Boston University School of Medicine, Boston, MA 02118, USA.
Sci Transl Med ; 9(381)2017 03 15.
Article em En | MEDLINE | ID: mdl-28298421
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Glicopeptídeos / HIV-1 / Mimetismo Molecular / Anticorpos Neutralizantes / Epitopos Idioma: En Ano de publicação: 2017 Tipo de documento: Article
Texto completo
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XML
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Glicopeptídeos / HIV-1 / Mimetismo Molecular / Anticorpos Neutralizantes / Epitopos Idioma: En Ano de publicação: 2017 Tipo de documento: Article