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Publication Abstract from PubMed

The DcCoV UAE-HKU23 coronavirus is a newly-found betacoronavirus (betaCoV) that can infect human cells. The viral spike protein plays pivotal roles in mediating receptor-recognition and membrane-fusion, and is therefore a key factor involved in viral pathogenesis and inter-species transmission. Here we reported the structural and functional characterization of the spike N-terminal domain (NTD) from DcCoV UAE-HKU23 (HKU23-NTD). Via mucin-binding assays, we showed that HKU23-NTD is able to bind sugars. We further solved the structure of HKU23-NTD, performed structure-guided mutagenesis and successfully located the potential sugar-binding pockets in the structure. Furthermore, via comparison of available betaCoV NTD structures, we demonstrated that betaCoV NTDs contain a conserved beta-sandwich core, but exhibit variant folds in the peripheral elements located in the top-ceiling region and on the lateral side. While showing different compositions and structures, these peripheral elements are topologically equivalent beta-sandwich-core insertions, highlighting a divergent evolution process for betaCoVs to form different lineages.

Crystal structure of the S1 subunit N-terminal domain from DcCoV UAE-HKU23 spike protein.,Cheng Y, He B, Yang J, Ye F, Lin S, Yang F, Chen Z, Chen Z, Cao Y, Lu G Virology. 2019 Jun 27;535:74-82. doi: 10.1016/j.virol.2019.06.015. PMID:31279241^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.