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Review
. 2022 Mar;94(3):847-857.
doi: 10.1002/jmv.27376. Epub 2021 Oct 13.

The global epidemic of SARS-CoV-2 variants and their mutational immune escape

Dandan Tian  1 , YanHong Sun  1 , JianMing Zhou  1 , Qing Ye  1
Affiliations
Review

The global epidemic of SARS-CoV-2 variants and their mutational immune escape

Dandan Tian et al. J Med Virol. 2022 Mar.

Abstract

During the COVID-19 pandemic, genetic variants of SARS-CoV-2 have been emerging and spreading around the world. Several SARS-CoV-2 endemic variants were found in United Kingdom, South Africa, Japan, and India between 2020 and April 2021. Studies have shown that many SARS-CoV-2 variants are more infectious than early wild strain and produce immune escape. These SARS-CoV-2 variants have brought new challenges to the prevention and control of COVID-19. This review summarizes and analyzes the biological characteristics of different amino acid mutations and the epidemic characteristics and immune escape of different SARS-CoV-2 variants. We hope to provide scientific reference for the monitoring, prevention, and control measures of new SARS-CoV-2 variants and the development strategy of the second-generation vaccine.

Keywords: COVID-19; SARS-CoV-2 variants; immune escape; mutations.

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Conflict of interest statement

All authors declare that there are no conflict of interests.

Figures

Figure 1
Figure 1
The biological characteristics of key amino acid mutations of Spike in B.1.1.7 and B.1.617.2 variant. Mutations (HV69‐70del, N501Y, D614G, P681H/R, L452R, T478K) could increase the binding affinity and binding tightness of SARS‐CoV‐2 spike to hACE2 receptor, or increase cell‐cell membrane fusion, result in increasing the infectivity of B.1.1.7 and B.1.617.2 variant. 144del and L452R mutations generated resistance to the neutralization activity of mAbs, convalescent plasma, and post‐vaccination serum against B.1.1.7 and B.1.617.2 variant, respectively. del, deletion; FP, fusion peptide; HR1, heptad repeat 1; HR2, heptad repeat 2; IC, intracellular domain; NTD, N‐terminal domain; RBD, receptor‐binding domain; RBM, receptor binding motif; SD1, subdomain 1; SD2, subdomain 2; TD, transmembrane domain
Figure 2
Figure 2
The biological characteristics of key amino acid mutations of Spike in B.1.351 and P.1 variant. Mutations including N501Y, D614G could increase the binding affinity and binding tightness of SARS‐CoV‐2 spike to hACE2 receptor, and result in increasing the infectivity of B.1.1.7 and B.1.617.2 variant. 241‐243del, L18F, K417N/T, E484K mutations generated resistance to the neutralization activity of mAbs, convalescent plasma, and postvaccination serum against B.1.351 and P.1 variant. del, deletion; FP, fusion peptide; HR1, heptad repeat 1; HR2, heptad repeat 2; IC, intracellular domain; NTD, N‐terminal domain; RBD, receptor‐binding domain; RBM, receptor binding motif; SD1, subdomain 1; SD2, subdomain 2; TD, transmembrane domain
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