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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

View ORCID ProfileJavier A. Jaimes, View ORCID ProfileNicole M. André, View ORCID ProfileJean K. Millet, View ORCID ProfileGary R. Whittaker
doi: https://doi.org/10.1101/2020.02.10.942185
Javier A. Jaimes
1Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca NY 14853 USA
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Nicole M. André
1Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca NY 14853 USA
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Jean K. Millet
2Virologie et Immunologie Moléculaires, INRAE, Université Paris-Saclay, 78352 Jouy-en-Josas, France
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Gary R. Whittaker
1Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca NY 14853 USA
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  • For correspondence: grw7@cornell.edu
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Abstract

The 2019 novel coronavirus (2019-nCoV) is currently causing a widespread outbreak centered on Hubei province, China and is a major public health concern. Taxonomically 2019-nCoV is closely related to SARS-CoV and SARS-related bat coronaviruses, and it appears to share a common receptor with SARS-CoV (ACE-2). Here, we perform structural modeling of the 2019-nCoV spike glycoprotein. Our data provide support for the similar receptor utilization between 2019-nCoV and SARS-CoV, despite a relatively low amino acid similarity in the receptor binding module. Compared to SARS-CoV, we identify an extended structural loop containing basic amino acids at the interface of the receptor binding (S1) and fusion (S2) domains, which we predict to be proteolytically-sensitive. We suggest this loop confers fusion activation and entry properties more in line with MERS-CoV and other coronaviruses, and that the presence of this structural loop in 2019-nCoV may affect virus stability and transmission.

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Posted February 18, 2020.
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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
Javier A. Jaimes, Nicole M. André, Jean K. Millet, Gary R. Whittaker
bioRxiv 2020.02.10.942185; doi: https://doi.org/10.1101/2020.02.10.942185
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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
Javier A. Jaimes, Nicole M. André, Jean K. Millet, Gary R. Whittaker
bioRxiv 2020.02.10.942185; doi: https://doi.org/10.1101/2020.02.10.942185

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