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

Journal of Medical Virology

Volumn 92, Issue 6, 2020, Pages 595-601

  Liu, Zhixin ^a,b   Xiao, Xiao ^a   Wei, Xiuli ^a   Li, Jian ^a   Yang, Jing ^a   Tan, Huabing ^a   Zhu, Jianyong ^a   Zhang, Qiwei ^c,d   Wu, Jianguo ^b,c   Liu, Long ^a  

^a HUBEI UNIVERSITY OF MEDICINE   (China)

^b WUHAN UNIVERSITY   (China)

^c JINAN UNIVERSITY   (China)

^d SOUTHERN MEDICAL UNIVERSITY   (China)

Author keywords

angiotensin converting enzyme 2 (ACE2); Coronavirus Disease 2019 (COVID 19); receptor binding domain (RBD) of coronavirus; SARS CoV 2; SARS CoV 2 spike protein (S)

Indexed keywords

ANGIOTENSIN CONVERTING ENZYME 2; CORONAVIRUS SPIKE GLYCOPROTEIN; VITRONECTIN; DIPEPTIDYL CARBOXYPEPTIDASE; PROTEIN BINDING; SPIKE PROTEIN, SARS-COV-2; VIRUS RECEPTOR;

ARTICLE; CHELONIA; CHRYSEMYS PICTA BELLII; COMPARATIVE STUDY; CORONAVIRUS DISEASE 2019; HUMAN; NONHUMAN; PELODISCUS SINENSIS; PHOLIDOTA (ANIMAL); PREDICTION; PROTEIN ANALYSIS; PROTEIN PROTEIN INTERACTION; SARS-RELATED CORONAVIRUS; SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS 2; SNAKE; TURTLE; VIRUS TRANSMISSION; ALPHA HELIX; AMINO ACID SEQUENCE; ANIMAL; BAT; BETA SHEET; BETACORONAVIRUS; BINDING SITE; CHEMISTRY; CHINA; CLASSIFICATION; CORONAVIRUS INFECTION; GENETICS; METABOLISM; MOLECULAR MODEL; PANDEMIC; PATHOGENICITY; PHYLOGENY; PLACENTAL MAMMAL; PROTEIN DOMAIN; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; VIROLOGY; VIRUS PNEUMONIA;

AMINO ACID SEQUENCE; ANIMALS; BETACORONAVIRUS; BINDING SITES; CHINA; CHIROPTERA; CORONAVIRUS INFECTIONS; EUTHERIA; HUMANS; MODELS, MOLECULAR; PANDEMICS; PEPTIDYL-DIPEPTIDASE A; PHYLOGENY; PNEUMONIA, VIRAL; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN INTERACTION MAPPING; RECEPTORS, VIRUS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SNAKES; SPIKE GLYCOPROTEIN, CORONAVIRUS; TURTLES;

EID: 85081543024     PISSN: 01466615     EISSN: 10969071     Source Type: Journal    
DOI: 10.1002/jmv.25726     Document Type: Article

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