Structure analysis of the receptor binding of 2019-nCoV

2019-nCoV is a newly identified coronavirus with high similarity to SARS-CoV. We performed a structural analysis of the receptor binding domain (RBD) of spike glycoprotein responsible for entry of coronaviruses into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences...

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Vydáno v:Biochemical and biophysical research communications Ročník 525; číslo 1; s. 135 - 140
Hlavní autoři: Chen, Yun, Guo, Yao, Pan, Yihang, Zhao, Zhizhuang Joe
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States Elsevier Inc 23.04.2020
The Authors. Published by Elsevier Inc
Témata:
Coronavirus
fish
glycoproteins
hydrophobicity
kidneys
molecular dynamics
Molecular modeling
phenylalanine
Sequence analysis
Severe acute respiratory syndrome coronavirus 2
Structure analysis
testes
viruses
Coronavirus
Structure analysis
Sequence analysis
Molecular modeling
ISSN:0006-291X, 1090-2104, 1090-2104
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Shrnutí:2019-nCoV is a newly identified coronavirus with high similarity to SARS-CoV. We performed a structural analysis of the receptor binding domain (RBD) of spike glycoprotein responsible for entry of coronaviruses into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. However, 2019-nCoV has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling revealed that 2019-nCoV RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of 2019-nCoV, making them all possible natural hosts for the virus. 2019-nCoV is thought to be transmitted through respiratory droplets. However, since ACE2 is predominantly expressed in intestines, testis, and kidney, fecal-oral and other routes of transmission are also possible. Finally, antibodies and small molecular inhibitors that can block the interaction of ACE2 with RBD should be developed to combat the virus. •Spike glycoprotein of 2019-nCoV may confer a strong ACE2 receptor binding.•Conserved expression of ACE2 suggests a wide range of natural hosts for 2019-nCoV.•Tissue expression of ACE2 suggests multiple routes of 2019-nCoV transmission.
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These authors contribute equally.
ISSN:0006-291X
1090-2104
1090-2104
DOI:10.1016/j.bbrc.2020.02.071