Viral Protein-Mammalian Protein


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Original Article
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SARS-CoV-2 receptor-binding domain (RBD) binds to human ACE2 receptor (hACE2) more strongly than that of bat ACE2 2 from Rhinolophus macrotis (bACE2-Rm). Glycosylation modification in bACE2-Rm doesn't influence the binding of SARS-CoV-2 RBD with bACE2-Rm.ns.
Patch 2 interaction in bACE2-Rm and hACE2 was highly conserved compared to Patch 1 interaction which showed significant differences in both.
In bACE2-Rm, residues Y41 and E42 are significant within the interface of SARS-CoV-2 RBD, whereas the residues in human include Y41 and Q42.
Most of the residues involved in ACE2 homodimer formation were conserved in both human and bats, indicating possible conservation of ACE2 dimer attributes during evolution.
33335073
(Proc Natl Acad Sci U S A)
PMID
33335073
Date of Publishing: 2021 Jan 5
Title Cross-species recognition of SARS-CoV-2 to bat ACE2
Author(s) nameLiu K, Tan S et al.
Journal Proc Natl Acad Sci U S A
Impact factor
9.35
Citation count: 1


Molecular interaction studies and structure simulation of human SARS-related coronavirus (SARS-CoV-2 and SARS-CoV ) and ACE2 from cat/dog/pangolin/Chinese hamster N82 of pangolin ACE2 showed closer contact with RBD than M82 human ACE2, indicating that pangolin ACE2 might show better affinity to SARS-CoV-2.
32201080
(Biochem Biophys Res Commun)
PMID
32201080
Date of Publishing: 2020 May 21
Title Spike protein recognition of mammalian ACE2 predicts the host range and an optimized ACE2 for SARS-CoV-2 infection
Author(s) nameLuan J, Lu Y et al.
Journal Biochem Biophys Res Commun
Impact factor
2.73
Citation count: 80