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The 2019 novel coronavirus (2019-nCoV) is currently causing a widespreadoutbreak centered on Hubei province, China and is a major public healthconcern. Taxonomically 2019-nCoV is closely related to SARS-CoV andSARS-related bat coronaviruses, and it appears to share a common receptor withSARS-CoV (ACE-2). Here, we perform structural modeling of the 2019-nCoV spikeglycoprotein. Our data provide support for the similar receptor utilizationbetween 2019-nCoV and SARS-CoV, despite a relatively low amino acid similarityin the receptor binding module. Compared to SARS-CoV, we identify an extendedstructural loop containing basic amino acids at the interface of the receptorbinding (S1) and fusion (S2) domains, which we predict to beproteolytically-sensitive. We suggest this loop confers fusion activation andentry properties more in line with MERS-CoV and other coronaviruses, and thatthe presence of this structural loop in 2019-nCoV may affect virus stabilityand transmission.

Structural modeling of 2019-novel coronavirus (nCoV) spike protein  reveals a proteolytically-sensitive activation loop as a distinguishing  feature compared to SARS-CoV and related SARS-like coronaviruses