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Identification of a conserved neutralizing epitope present on spike proteins from highly pathogenic coronaviruses
Yimin Huang; Annalee W Nguyen; Ching-Lin Hsieh; Rui Silva; Oladimeji S Olaluwoye; Rebecca Wilen; Tamer S Kaoud; Laura R Azouz; Ahlam N Qerqez; Kevin C Le; Amanda L Bohanon; Andrea M DiVenere; Yutong Liu; Dzifa Amengor; Sophie R Shoemaker; Shawn M Costello; Susan Marqusee; Kevin Dalby; Jason S McLellan; Jennifer A Maynard.
Afiliación
  • Yimin Huang; Dept of Molecular Biosciences, University of Texas at Austin
  • Annalee W Nguyen; Dept of Chemical Engineering, University of Texas at Austin
  • Ching-Lin Hsieh; Dept. of Molecular Biosciences, University of Texas at Austin
  • Rui Silva; Dept. of Molecular Biosciences, University of Texas at Austin
  • Oladimeji S Olaluwoye; Dept of Chemistry and Biochemistry, University of Texas at Dallas
  • Rebecca Wilen; Dept of Chemical Engineering, University of Texas at Austin
  • Tamer S Kaoud; Division of Chemical Biology and Medicinal Chemistry, University of Texas at Austin
  • Laura R Azouz; Dept of Chemical Engineering, University of Texas at Austin
  • Ahlam N Qerqez; Dept of Chemical Engineering, University of Texas at Austin
  • Kevin C Le; Dept of Chemical Engineering, University of Texas at Austin
  • Amanda L Bohanon; Dept. of Molecular Biosciences, University of Texas at Austin
  • Andrea M DiVenere; Dept of Chemical Engineering, University of Texas at Austin
  • Yutong Liu; Dept of Chemical Engineering, University of Texas at Austin
  • Dzifa Amengor; Dept. of Molecular Biosciences, University of Texas at Austin
  • Sophie R Shoemaker; University of California at Berkeley
  • Shawn M Costello; UC Berkeley
  • Susan Marqusee; University of California, Berkeley
  • Kevin Dalby; Division of Chemical Biology and Medicinal Chemistry, University of Texas at Austin
  • Jason S McLellan; Dept. of Molecular Biosciences, University of Texas at Austin
  • Jennifer A Maynard; Dept of Chemical Engineering, University of Texas at Austin
Preprint en En | PREPRINT-BIORXIV | ID: ppbiorxiv-428824
ABSTRACT
Three pathogenic human coronaviruses have emerged within the last 20 years, with SARS-CoV-2 causing a global pandemic. Although therapeutic antibodies targeting the SARS-CoV-2 spike currently focus on the poorly conserved receptor-binding domain, targeting essential neutralizing epitopes on the more conserved S2 domain may provide broader protection. We report an antibody binding an epitope conserved in the pre-fusion core of MERS-CoV, SARS-CoV and SARS-CoV-2 spike S2 domains. Antibody 3A3 binds a conformational epitope with ~2.5 nM affinity and neutralizes spike from SARS-CoV, SARS-CoV-2 and variants of concern in in vitro pseudovirus assays. Hydrogen-deuterium exchange mass spectrometry identified residues 980-1006 in the flexible hinge region at the S2 apex as the 3A3 epitope, suggesting 3A3 prevents the S2 conformational rearrangements required for conversion to the spike post-fusion state and virus-host cell fusion. This work defines a conserved vulnerable site on the SARS-CoV-2 S2 domain and guides the design of pan-protective spike immunogens.
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Texto completo: 1 Colección: 09-preprints Base de datos: PREPRINT-BIORXIV Idioma: En Año: 2021 Tipo del documento: Preprint
Texto completo
Añadir a Mi BVS
Imprimir
XML
Buscar en Google
Texto completo: 1 Colección: 09-preprints Base de datos: PREPRINT-BIORXIV Idioma: En Año: 2021 Tipo del documento: Preprint