Molecular and structural insights into SARS-CoV-2 evolution: from BA.2 to XBB subvariants

mBio. 2024 Oct 16;15(10):e0322023. doi: 10.1128/mbio.03220-23. Epub 2024 Sep 16.

Abstract

Due to the incessant emergence of various SARS-CoV-2 variants with enhanced fitness in the human population, controlling the COVID-19 pandemic has been challenging. Understanding how the virus enhances its fitness during a pandemic could offer valuable insights for more effective control of viral epidemics. In this manuscript, we review the evolution of SARS-CoV-2 from early 2022 to the end of 2023-from Omicron BA.2 to XBB descendants. Focusing on viral evolution during this period, we provide concrete examples that SARS-CoV-2 has increased its fitness by enhancing several functions of the spike (S) protein, including its binding affinity to the ACE2 receptor and its ability to evade humoral immunity. Furthermore, we explore how specific mutations modify these functions of the S protein through structural alterations. This review provides evolutionary, molecular, and structural insights into how SARS-CoV-2 has increased its fitness and repeatedly caused epidemic surges during the pandemic.

Keywords: Omicron; SARS-CoV-2; evolution; molecular phylogenetic; spike; structural biology.

Publication types

  • Review

MeSH terms

  • Angiotensin-Converting Enzyme 2 / chemistry
  • Angiotensin-Converting Enzyme 2 / genetics
  • Angiotensin-Converting Enzyme 2 / metabolism
  • COVID-19* / epidemiology
  • COVID-19* / virology
  • Evolution, Molecular*
  • Humans
  • Immune Evasion
  • Mutation
  • Protein Binding
  • SARS-CoV-2* / chemistry
  • SARS-CoV-2* / genetics
  • SARS-CoV-2* / immunology
  • Spike Glycoprotein, Coronavirus* / chemistry
  • Spike Glycoprotein, Coronavirus* / genetics
  • Spike Glycoprotein, Coronavirus* / metabolism

Substances

  • Spike Glycoprotein, Coronavirus
  • spike protein, SARS-CoV-2
  • Angiotensin-Converting Enzyme 2
  • ACE2 protein, human

Supplementary concepts

  • SARS-CoV-2 variants

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