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TitleSARS-CoV-2 spike conformation determines plasma neutralizing activity elicited by a wide panel of human vaccines.
Journal, issue, pagesSci Immunol, Vol. 7, Issue 78, Page eadf1421, Year 2022
Publish dateDec 23, 2022
AuthorsJohn E Bowen / Young-Jun Park / Cameron Stewart / Jack T Brown / William K Sharkey / Alexandra C Walls / Anshu Joshi / Kaitlin R Sprouse / Matthew McCallum / M Alejandra Tortorici / Nicholas M Franko / Jennifer K Logue / Ignacio G Mazzitelli / Annalee W Nguyen / Rui P Silva / Yimin Huang / Jun Siong Low / Josipa Jerak / Sasha W Tiles / Kumail Ahmed / Asefa Shariq / Jennifer M Dan / Zeli Zhang / Daniela Weiskopf / Alessandro Sette / Gyorgy Snell / Christine M Posavad / Najeeha Talat Iqbal / Jorge Geffner / Alessandra Bandera / Andrea Gori / Federica Sallusto / Jennifer A Maynard / Shane Crotty / Wesley C Van Voorhis / Carlos Simmerling / Renata Grifantini / Helen Y Chu / Davide Corti / David Veesler /
PubMed AbstractNumerous 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 ...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 S subunit relative to postfusion S as compared with vaccines lacking these mutations or natural infection. Prefusion S and S antibody binding titers positively and equivalently correlated with neutralizing activity, and depletion of S-directed antibodies completely abrogated plasma neutralizing activity. We show that neutralizing activity is almost entirely directed to the S 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.
External linksSci Immunol / PubMed:36356052 / PubMed Central
MethodsEM (single particle)
Resolution3.67 Å
Structure data

27779

8dya

EMDB-27779, PDB-8dya:
Structure of the SARS-CoV-2 spike glycoprotein S2 subunit
Method: EM (single particle) / Resolution: 3.67 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / SARS-CoV-2 / COVID-19 / spike glycoprotein / fusion protein / neutralizing antibodies / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID

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