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TitleImprinted antibody responses against SARS-CoV-2 Omicron sublineages.
Journal, issue, pagesScience, Vol. 378, Issue 6620, Page 619-627, Year 2022
Publish dateNov 11, 2022
AuthorsYoung-Jun Park / Dora Pinto / Alexandra C Walls / Zhuoming Liu / Anna De Marco / Fabio Benigni / Fabrizia Zatta / Chiara Silacci-Fregni / Jessica Bassi / Kaitlin R Sprouse / Amin Addetia / John E Bowen / Cameron Stewart / Martina Giurdanella / Christian Saliba / Barbara Guarino / Michael A Schmid / Nicholas M Franko / Jennifer K Logue / Ha V Dang / Kevin Hauser / Julia di Iulio / William Rivera / Gretja Schnell / Anushka Rajesh / Jiayi Zhou / Nisar Farhat / Hannah Kaiser / Martin Montiel-Ruiz / Julia Noack / Florian A Lempp / Javier Janer / Rana Abdelnabi / Piet Maes / Paolo Ferrari / Alessandro Ceschi / Olivier Giannini / Guilherme Dias de Melo / Lauriane Kergoat / Hervé Bourhy / Johan Neyts / Leah Soriaga / Lisa A Purcell / Gyorgy Snell / Sean P J Whelan / Antonio Lanzavecchia / Herbert W Virgin / Luca Piccoli / Helen Y Chu / Matteo Samuele Pizzuto / Davide Corti / David Veesler /
PubMed AbstractSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron sublineages carry distinct spike mutations resulting in escape from antibodies induced by previous infection or vaccination. We ...Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron sublineages carry distinct spike mutations resulting in escape from antibodies induced by previous infection or vaccination. We show that hybrid immunity or vaccine boosters elicit plasma-neutralizing antibodies against Omicron BA.1, BA.2, BA.2.12.1, and BA.4/5, and that breakthrough infections, but not vaccination alone, induce neutralizing antibodies in the nasal mucosa. Consistent with immunological imprinting, most antibodies derived from memory B cells or plasma cells of Omicron breakthrough cases cross-react with the Wuhan-Hu-1, BA.1, BA.2, and BA.4/5 receptor-binding domains, whereas Omicron primary infections elicit B cells of narrow specificity up to 6 months after infection. Although most clinical antibodies have reduced neutralization of Omicron, we identified an ultrapotent pan-variant-neutralizing antibody that is a strong candidate for clinical development.
External linksScience / PubMed:36264829
MethodsEM (single particle)
Resolution3.1 - 3.3 Å
Structure data

EMDB-28558, PDB-8erq:
SARS-CoV-2 BA.1 spike ectodomain trimer in complex with the S2X324 neutralizing antibody Fab fragment (local refinement of the RBD and S2X324)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-28559, PDB-8err:
SARS-CoV-2 Omicron BA.1 spike ectodomain trimer in complex with the S2X324 neutralizing antibody Fab fragment
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

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

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / COVID-19 / spike glycoprotein / fusion protein / neutralizing antibodies / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / inhibitor / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex / SARS-CoV-2 Omicron variant

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