Protection of the receptor binding domain (RBD) dimer against SARS-CoV-2 and its variants

J Virol. 2023 Nov 30;97(11):e0127923. doi: 10.1128/jvi.01279-23. Epub 2023 Oct 16.


Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants achieved immune escape and became less virulent and easily transmissible through rapid mutation in the spike protein, thus the efficacy of vaccines on the market or in development continues to be challenged. Updating the vaccine, exploring compromise vaccination strategies, and evaluating the efficacy of candidate vaccines for the emerging variants in a timely manner are important to combat complex and volatile SARS-CoV-2. This study reports that vaccines prepared from the dimeric receptor-binding domain (RBD) recombinant protein, which can be quickly produced using a mature and stable process platform, had both good immunogenicity and protection in vivo and could completely protect rodents from lethal challenge by SARS-CoV-2 and its variants, including the emerging Omicron XBB.1.16, highlighting the value of dimeric recombinant vaccines in the post-COVID-19 era.

Keywords: Omicron XBB.1.16; SARS-CoV-2; cross-protection; homodimer; receptor-binding domain.

MeSH terms

  • Antibodies, Neutralizing
  • Antibodies, Viral
  • COVID-19 Vaccines* / immunology
  • COVID-19* / prevention & control
  • COVID-19* / virology
  • Humans
  • Mutation
  • Polymers
  • SARS-CoV-2* / classification
  • SARS-CoV-2* / physiology
  • Spike Glycoprotein, Coronavirus / chemistry


  • Antibodies, Neutralizing
  • Antibodies, Viral
  • Polymers
  • Spike Glycoprotein, Coronavirus
  • spike protein, SARS-CoV-2
  • COVID-19 Vaccines