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Review
. 2023 Aug;31(4):1779-1788.
doi: 10.1007/s10787-023-01253-6. Epub 2023 May 19.

Omicron variant evolution on vaccines and monoclonal antibodies

Affiliations
Review

Omicron variant evolution on vaccines and monoclonal antibodies

Michela Sabbatucci et al. Inflammopharmacology. 2023 Aug.

Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV)-2 responsible for the global COVID-19 pandemic has caused almost 760 million confirmed cases and 7 million deaths worldwide, as of end-February 2023. Since the beginning of the first COVID-19 case, several virus variants have emerged: Alpha (B1.1.7), Beta (B135.1), Gamma (P.1), Delta (B.1.617.2) and then Omicron (B.1.1.529) and its sublineages. All variants have diversified in transmissibility, virulence, and pathogenicity. All the newly emerging SARS-CoV-2 variants appear to contain some similar mutations associated with greater "evasiveness" of the virus to immune defences. From early 2022 onward, several Omicron subvariants named BA.1, BA.2, BA.3, BA.4, and BA.5, with comparable mutation forms, have followed. After the wave of contagions caused by Omicron BA.5, a new Indian variant named Centaurus BA.2.75 and its new subvariant BA.2.75.2, a second-generation evolution of the Omicron variant BA.2, have recently been identified. From early evidence, it appears that this new variant has higher affinity for the cell entry receptor ACE-2, making it potentially able to spread very fast. According to the latest studies, the BA.2.75.2 variant may be able to evade more antibodies in the bloodstream generated by vaccination or previous infection, and it may be more resistant to antiviral and monoclonal antibody drug treatments. In this manuscript, the authors highlight and describe the latest evidences and critical issues have emerged on the new SARS-CoV-2 variants.

Keywords: Antiviral drugs; B.1.1.529; COVID-19; Coronavirus; Epidemiology; Monoclonal antibodies; Mutations; Omicron; Pandemic; Public health; SARS-CoV-2; Spike protein; VOC; VOI; Vaccines; Variants.

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Conflict of interest statement

All the authors declare no conflict of interest.

Figures

Fig. 1
Fig. 1
Illustration of the three-dimensional structure of the spike protein from SARS-CoV-2 Omicron subvariant BA.2.75. Nine additional mutations are highlighted in the spike protein subvariant BA.2.75 compared with the BA.2 variant, namely G339H, G446S, G257S, I210V, F157L, R493Q, N460K, W152R and K147E. RBD: receptor-binding domain; FP: N-terminal hydrophobic fusion peptide; S2 subunit of spike protein

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Supplementary concepts