Identification of key amino acid residues required for horseshoe bat angiotensin-I converting enzyme 2 to function as a receptor for severe acute respiratory syndrome coronavirus

J Gen Virol. 2010 Jul;91(Pt 7):1708-12. doi: 10.1099/vir.0.020172-0. Epub 2010 Mar 24.

Abstract

Angiotensin-I converting enzyme 2 (ACE2) is the receptor for severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV). A previous study indicated that ACE2 from a horseshoe bat, the host of a highly related SARS-like coronavirus, could not function as a receptor for SARS-CoV. Here, we demonstrate that a 3 aa change from SHE (aa 40-42) to FYQ was sufficient to convert the bat ACE2 into a fully functional receptor for SARS-CoV. We further demonstrate that an ACE2 molecule from a fruit bat, which contains the FYQ motif, was able to support SARS-CoV infection, indicating a potentially much wider host range for SARS-CoV-related viruses among different bat populations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chiroptera*
  • Molecular Sequence Data
  • Peptidyl-Dipeptidase A / chemistry*
  • Peptidyl-Dipeptidase A / genetics
  • Peptidyl-Dipeptidase A / metabolism*
  • Receptors, Cell Surface
  • Severe acute respiratory syndrome-related coronavirus / physiology*
  • Species Specificity
  • Virus Internalization

Substances

  • Receptors, Cell Surface
  • Peptidyl-Dipeptidase A

Associated data

  • GENBANK/GU253336