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SARS-CoV-2 spike conformation determines plasma neutralizing activity elicited by a wide panel of human vaccines.
Bowen, John E; Park, Young-Jun; Stewart, Cameron; Brown, Jack T; Sharkey, William K; Walls, Alexandra C; Joshi, Anshu; Sprouse, Kaitlin R; McCallum, Matthew; Tortorici, M Alejandra; Franko, Nicholas M; Logue, Jennifer K; Mazzitelli, Ignacio G; Nguyen, Annalee W; Silva, Rui P; Huang, Yimin; Low, Jun Siong; Jerak, Josipa; Tiles, Sasha W; Ahmed, Kumail; Shariq, Asefa; Dan, Jennifer M; Zhang, Zeli; Weiskopf, Daniela; Sette, Alessandro; Snell, Gyorgy; Posavad, Christine M; Iqbal, Najeeha Talat; Geffner, Jorge; Bandera, Alessandra; Gori, Andrea; Sallusto, Federica; Maynard, Jennifer A; Crotty, Shane; Van Voorhis, Wesley C; Simmerling, Carlos; Grifantini, Renata; Chu, Helen Y; Corti, Davide; Veesler, David.
Affiliation
  • Bowen JE; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Park YJ; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Stewart C; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
  • Brown JT; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Sharkey WK; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Walls AC; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Joshi A; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Sprouse KR; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.
  • McCallum M; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Tortorici MA; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Franko NM; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Logue JK; Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
  • Mazzitelli IG; Division of Allergy and Infectious Diseases, University of Washington, Seattle, WA 98195, USA.
  • Nguyen AW; Division of Allergy and Infectious Diseases, University of Washington, Seattle, WA 98195, USA.
  • Silva RP; Instituto de Investigaciones Biomédicas en Retrovirus y SIDA (INBIRS), Facultad de Medicina, Buenos Aires C1121ABG, Argentina.
  • Huang Y; McKetta Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
  • Low JS; McKetta Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
  • Jerak J; McKetta Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
  • Tiles SW; Institute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.
  • Ahmed K; Institute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.
  • Shariq A; Center for Emerging and Re-emerging Infectious Diseases, Division of Allergy and Infectious Diseases, Department of Medicine, University of Washington School of Medicine, Seattle, WA 98195, USA.
  • Dan JM; Departments of Paediatrics and Child Health and Biological and Biomedical Sciences, Aga Khan University, Karachi 74800, Pakistan.
  • Zhang Z; Departments of Paediatrics and Child Health and Biological and Biomedical Sciences, Aga Khan University, Karachi 74800, Pakistan.
  • Weiskopf D; Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
  • Sette A; Division of Infectious Diseases and Global Public Health, Department of Medicine, University of California, San Diego, La Jolla, CA UC92037, USA.
  • Snell G; Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
  • Posavad CM; Division of Infectious Diseases and Global Public Health, Department of Medicine, University of California, San Diego, La Jolla, CA UC92037, USA.
  • Iqbal NT; Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
  • Geffner J; Division of Infectious Diseases and Global Public Health, Department of Medicine, University of California, San Diego, La Jolla, CA UC92037, USA.
  • Bandera A; Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
  • Gori A; Division of Infectious Diseases and Global Public Health, Department of Medicine, University of California, San Diego, La Jolla, CA UC92037, USA.
  • Sallusto F; Vir Biotechnology, San Francisco, CA 94158, USA.
  • Maynard JA; Vaccine and Infectious Disease Division, Fred Hutchinson Cancer Center, Seattle, WA 98109, USA.
  • Crotty S; Departments of Paediatrics and Child Health and Biological and Biomedical Sciences, Aga Khan University, Karachi 74800, Pakistan.
  • Van Voorhis WC; Instituto de Investigaciones Biomédicas en Retrovirus y SIDA (INBIRS), Facultad de Medicina, Buenos Aires C1121ABG, Argentina.
  • Simmerling C; Infectious Diseases Unit, Fondazione IRCCS Ca' Granda Ospedale Maggiore Policlinico, 20122 Milan, Italy.
  • Grifantini R; Infectious Diseases Unit, Fondazione IRCCS Ca' Granda Ospedale Maggiore Policlinico, 20122 Milan, Italy.
  • Chu HY; Institute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.
  • Corti D; McKetta Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA.
  • Veesler D; Center for Infectious Disease and Vaccine Research, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
Sci Immunol ; 7(78): eadf1421, 2022 12 23.
Article in En | MEDLINE | ID: mdl-36356052
ABSTRACT
Numerous safe and effective coronavirus disease 2019 vaccines have been developed worldwide that use various delivery technologies and engineering strategies. We show here that vaccines containing prefusion-stabilizing S mutations elicit antibody responses in humans with enhanced recognition of S and the S1 subunit relative to postfusion S as compared with vaccines lacking these mutations or natural infection. Prefusion S and S1 antibody binding titers positively and equivalently correlated with neutralizing activity, and depletion of S1-directed antibodies completely abrogated plasma neutralizing activity. We show that neutralizing activity is almost entirely directed to the S1 subunit and that variant cross-neutralization is mediated solely by receptor binding domain-specific antibodies. Our data provide a quantitative framework for guiding future S engineering efforts to develop vaccines with higher resilience to the emergence of variants than current technologies.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Limits: Humans Language: En Journal: Sci Immunol Year: 2022 Document type: Article Affiliation country: United States
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Limits: Humans Language: En Journal: Sci Immunol Year: 2022 Document type: Article Affiliation country: United States