Emergence of BS.1 and BS.1.1, highly mutated new SARS‐CoV‐2 Omicron variants

Takahashi, Kenichiro; Saito, Masumichi; Sekizuka, Tsuyoshi; Itokawa, Kentaro; Tanio, Michikazu; Yoshida-Furihata, Hazuka; Nojiri, Naomi; Hamada, Yoji; Yokota, Eiichi; Kuroda, Makoto; Saito, Tomoya

doi:10.1002/jmv.28615

Cited by 1 publication

(2 citation statements)

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“…Although the COVID‐19 epidemic has largely ended in China 30 and is expected to end in the United States in May 2023, 31 the World Health Organization still considers COVID‐19 to be a major international health threat due to the emergence of new variants of SARS‐CoV‐2, such as BQ.1, BQ.1.1, XBB, and other Omicron subvariants that have recently emerged and are able to substantially escape neutralizing antibodies 32 . Notably, SARS‐CoV‐2 has undergone convergent evolution, with multiple new variants incorporating R346T and other mutations in the RBD region 33,34 . These mutations impair RBD–ACE2 binding and may allow the virus to enter host cells using alternative receptors.…”

Section: Discussionmentioning

confidence: 99%

“…32 Notably, SARS-CoV-2 has undergone convergent evolution, with multiple new variants incorporating R346T and other mutations in the RBD region. 33,34 These mutations found that AXL, an alternative receptor that binds to the NTD of the S protein, could synergistically work with ACE2 to facilitate virus entry into cells. These results are consistent with prior reports.…”

Section: Discussionmentioning

confidence: 99%

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Verifying AXL and putative proteins as SARS‐CoV‐2 receptors by DnaE intein‐based rapid cell–cell fusion assay

Fang

Zheng

et al. 2023

Journal of Medical Virology

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As the understanding of the mechanisms of SARS-CoV-2 infection continues to grow, researchers have come to realize that ACE2 and TMPRSS2 receptors are not the only way for the virus to invade the host, and that there are many molecules that may serve as potential receptors or cofactors. The functionality of these numerous receptors, proposed by different research groups, demands a fast, simple, and accurate validation method. To address this issue, we here established a DnaE intein-based cell-cell fusion system, a key result of our study, which enables rapid simulation of SARS-CoV-2 host cell infection. This system allowed us to validate that proteins such as AXL function as SARS-CoV-2 spike protein receptors and synergize with ACE2 for cell invasion, and that proteins like NRP1 act as cofactors, facilitating ACE2-mediated syncytium formation. Our results also suggest that mutations in the NTD of the SARS-CoV-2 Delta variant spike protein show a preferential selection for Spike-AXL interaction over Spike-LDLRAD3. In summary, our system serves as a crucial tool for the rapid and comprehensive verification of potential receptors, screening of SARS-CoV-2-neutralizing antibodies, or targeted drugs, bearing substantial implications for translational clinical applications.

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Section: Discussionmentioning

confidence: 99%