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TitleBroad neutralizing antibody response of a monomeric spike-based SARS-CoV-2 bivalent vaccine against diverse variants.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 35, Page e2503254122, Year 2025
Publish dateSep 2, 2025
AuthorsSiling Wang / Hui Sun / Yizhen Wang / Zikang Wang / Lunzhi Yuan / Huilin Guo / Jiahua Gao / Miaolin Lan / Yangtao Wu / Huixian Shang / Xiuting Chen / Zheng Chen / Jiayi Hu / Zimin Tang / Guiping Wen / Dong Ying / Chang Liu / Yanan Jiang / Jinfu Su / Min Lin / Ting Wu / Shaowei Li / Tianying Zhang / Jun Zhang / Yi Guan / Ningshao Xia / Quan Yuan / Qingbing Zheng / Yali Zhang / Zizheng Zheng /
PubMed Abstractsevereacute respiratory syndrome coronavirus 2 (SARS-CoV-2) bivalent vaccines show potential against variants but lack a full understanding of the immunological mechanisms that drive broadly ...severeacute respiratory syndrome coronavirus 2 (SARS-CoV-2) bivalent vaccines show potential against variants but lack a full understanding of the immunological mechanisms that drive broadly neutralizing antibodies (bnAbs). This study explored the immunogenicity of a bivalent vaccine in rhesus macaques, containing spike (S) proteins from the prototype (S) and chimeric S protein (S). The vaccine induced bnAbs against multiple variants, including challenging subvariants like EG.1, BA.2.86, and JN.1. The monomeric S protein exposed less accessible regions within the receptor-binding domain (RBD) "inner face" and "NTD face" and subdomains 1, eliciting a diverse array of bnAbs against various Omicron subvariants. Notably, antibodies targeting the conserved RBD inner face, such as 4A5, showed potent neutralization across all tested variants. Structural analyses provide insights into the broad protectiveness of these vaccine-elicited nAbs. This study underscores the potential of bivalent vaccines with monomeric spike proteins to confer broad-spectrum immunity, offering a promising direction for future SARS-CoV-2 universal vaccine design.
External linksProc Natl Acad Sci U S A / PubMed:40854137 / PubMed Central
MethodsEM (single particle)
Resolution2.98 - 7.41 Å
Structure data

62589

9kvd

EMDB-62589, PDB-9kvd:
Cryo-EM structure of SARS-CoV-2 prototype spike protein in complex with triple-nAb 3G5, 4H5 and 4C11
Method: EM (single particle) / Resolution: 3.44 Å

EMDB-62590: Cryo-EM structure of SARS-CoV-2 prototype spike protein in complex with nAbs 4H1, 4A5, 4C1 and 2E10
Method: EM (single particle) / Resolution: 7.41 Å

62591

9kve

EMDB-62591, PDB-9kve:
Cryo-EM structure of SARS-CoV-2 prototype spike protein in complex with triple-nAb 4H1, 4A5 and 4C1
Method: EM (single particle) / Resolution: 2.98 Å

62592

9kvf

EMDB-62592, PDB-9kvf:
Cryo-EM structure of SARS-CoV-2 EG.1 spike protein in complex with triple-nAb 4A5, 4C1 and 2E10
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

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

Source
  • severe acute respiratory syndrome coronavirus 2
  • Mus musculus (house mouse)
  • macaca mulatta (Rhesus monkey)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / Neutralizing antibody / Cryo-EM / VIRAL PROTEIN-IMMUNE SYSTEM complex

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