Composition and divergence of coronavirus spike proteins and host ACE2 receptors predict potential intermediate hosts of SARS‐CoV‐2

From the beginning of 2002 and 2012, severe respiratory syndrome coronavirus (SARS‐CoV) and Middle East respiratory syndrome coronavirus (MERS‐CoV) crossed the species barriers to infect humans, causing thousands of infections and hundreds of deaths, respectively. Currently, a novel coronavirus (SAR...

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Vydáno v:	Journal of medical virology Ročník 92; číslo 6; s. 595 - 601
Hlavní autoři:	Liu, Zhixin, Xiao, Xiao, Wei, Xiuli, Li, Jian, Yang, Jing, Tan, Huabing, Zhu, Jianyong, Zhang, Qiwei, Wu, Jianguo, Liu, Long
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Wiley Subscription Services, Inc 01.06.2020 John Wiley and Sons Inc
Témata:	ACE2 Amino Acid Sequence Amino acids Angiotensin Angiotensin-Converting Enzyme 2 angiotensin‐converting enzyme 2 (ACE2) Animals Aquatic reptiles Betacoronavirus - classification Betacoronavirus - genetics Betacoronavirus - pathogenicity Binding Binding Sites Chelonia mydas China - epidemiology Chiroptera - virology Coronaviridae Coronavirus Disease 2019 (COVID‐19) Coronavirus Infections - epidemiology Coronavirus Infections - transmission Coronavirus Infections - virology Coronaviruses COVID-19 Disease transmission Divergence Epidemics Eutheria - virology Fatalities Humans Models, Molecular Pandemics Pelodiscus sinensis Peptidyl-Dipeptidase A - chemistry Peptidyl-Dipeptidase A - genetics Peptidyl-Dipeptidase A - metabolism Phylogeny Pneumonia, Viral - epidemiology Pneumonia, Viral - transmission Pneumonia, Viral - virology Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Protein Interaction Mapping Proteins Receptors Receptors, Virus - chemistry Receptors, Virus - genetics Receptors, Virus - metabolism receptor‐binding domain (RBD) of coronavirus Respiratory diseases SARS-CoV-2 SARS‐CoV‐2 spike protein (S) Sequence Alignment Sequence Homology, Amino Acid Severe acute respiratory syndrome Severe acute respiratory syndrome coronavirus 2 Snakes - virology Spike Glycoprotein, Coronavirus - chemistry Spike Glycoprotein, Coronavirus - classification Spike Glycoprotein, Coronavirus - genetics Spike Glycoprotein, Coronavirus - metabolism Spike protein Transmission Turtles Turtles - virology Viral diseases Virology China angiotensin-converting enzyme 2 (ACE2) SARS-CoV-2 Coronavirus Disease 2019 (COVID-19) SARS-CoV-2 spike protein (S) receptor-binding domain (RBD) of coronavirus
ISSN:	0146-6615, 1096-9071, 1096-9071
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Popis
Shrnutí:	From the beginning of 2002 and 2012, severe respiratory syndrome coronavirus (SARS‐CoV) and Middle East respiratory syndrome coronavirus (MERS‐CoV) crossed the species barriers to infect humans, causing thousands of infections and hundreds of deaths, respectively. Currently, a novel coronavirus (SARS‐CoV‐2), which has become the cause of the outbreak of Coronavirus Disease 2019 (COVID‐19), was discovered. Until 18 February 2020, there were 72 533 confirmed COVID‐19 cases (including 10 644 severe cases) and 1872 deaths in China. SARS‐CoV‐2 is spreading among the public and causing substantial burden due to its human‐to‐human transmission. However, the intermediate host of SARS‐CoV‐2 is still unclear. Finding the possible intermediate host of SARS‐CoV‐2 is imperative to prevent further spread of the epidemic. In this study, we used systematic comparison and analysis to predict the interaction between the receptor‐binding domain (RBD) of coronavirus spike protein and the host receptor, angiotensin‐converting enzyme 2 (ACE2). The interaction between the key amino acids of S protein RBD and ACE2 indicated that, other than pangolins and snakes, as previously suggested, turtles (Chrysemys picta bellii, Chelonia mydas, and Pelodiscus sinensis) may act as the potential intermediate hosts transmitting SARS‐CoV‐2 to humans. Highlights The critical residues of S protein RBD binding with ACE2 indicated the potential intermediate hosts transmitting SARS‐CoV‐2 to humans.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	0146-6615 1096-9071 1096-9071
DOI:	10.1002/jmv.25726