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TitleCommon cold embecovirus imprinting primes broadly neutralizing antibody responses to SARS-CoV-2 S2.
Journal, issue, pagesJ Exp Med, Vol. 222, Issue 12, Year 2025
Publish dateDec 1, 2025
AuthorsSiriruk Changrob / Atsuhiro Yasuhara / Suncheol Park / Sandhya Bangaru / Lei Li / Chloe A Troxell / Peter J Halfmann / Steven A Erickson / Nicholas J Catanzaro / Meng Yuan / Panpan Zhou / Min Huang / G Dewey Wilbanks / Joshua J C McGrath / Gagandeep Singh / Sean A Nelson / Yanbin Fu / Nai-Ying Zheng / Sofia M Carayannopoulos / Haley L Dugan / Dustin G Shaw / Christopher T Stamper / Maria Lucia L Madariaga / Florian Krammer / Raiees Andrabi / Dennis R Burton / Andrew B Ward / Ian A Wilson / Yoshihiro Kawaoka / Patrick C Wilson /
PubMed AbstractThe S2 subunit of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike is highly conserved across coronavirus strains and therefore is a potential pan-coronavirus vaccine target. ...The S2 subunit of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike is highly conserved across coronavirus strains and therefore is a potential pan-coronavirus vaccine target. However, antibodies targeting this region are typically non-neutralizing. We report herein that S2-targeting antibodies from patients who recovered from SARS-CoV-2 infection bound only closely related sarbecovirus subgenus strains and, like most known S2 antibodies, none of these were neutralizing. In contrast, first-exposure, severe acutely infected COVID-19 patients predominantly induced back-boosted antibody-secreting cells imprinted against past common cold coronavirus strain OC43 that were cross-reactive to as many as five subgenera of betacoronavirus strains and gave rise to antibodies that were neutralizing and protective. The antibodies targeted two different sites: one defined by competition with stem helix antibodies, and the second to an underdescribed epitope at the apex of S2. These findings suggest that S2-targeted vaccines could strategically exploit controlled OC43 priming followed by SARS-CoV-2 boosting to enhance the breadth and quality of protective antibody responses.
External linksJ Exp Med / PubMed:41066082
MethodsEM (single particle)
Resolution3.59 - 5.7 Å
Structure data

48548

9mr1

EMDB-48548, PDB-9mr1:
SARS-CoV-2 S2 monomer in complex with R125-61 Fab
Method: EM (single particle) / Resolution: 3.59 Å

EMDB-48549: SARS-CoV-2 S2 monomer in complex with NICA01B-1113 Fab
Method: EM (single particle) / Resolution: 5.7 Å

48550

9mr2

EMDB-48550, PDB-9mr2:
SARS-CoV-2 S2 monomer in complex with NICA01A-1401 Fab
Method: EM (single particle) / Resolution: 3.79 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRUS / SARS-CoV-2 / Spike / S2 / COVID / monoclonal antibody / complex / Viral protein / Viral protein-immune system complex

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