Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2

J Gen Virol. 2008 Nov;89(Pt 11):2741-2745. doi: 10.1099/vir.0.2008/003962-0.

Abstract

Although in different groups, the coronaviruses severe acute respiratory syndrome-coronavirus (SARS-CoV) and NL63 use the same receptor, angiotensin converting enzyme (ACE)-2, for entry into the host cell. Despite this common receptor, the consequence of entry is very different; severe respiratory distress in the case of SARS-CoV but frequently only a mild respiratory infection for NL63. Using a wholly recombinant system, we have investigated the ability of each virus receptor-binding protein, spike or S protein, to bind to ACE-2 in solution and on the cell surface. In both assays, we find that the NL63 S protein has a weaker interaction with ACE-2 than the SARS-CoV S protein, particularly in solution binding, but the residues required for contact are similar. We also confirm that the ACE-2-binding site of NL63 S lies between residues 190 and 739. A lower-affinity interaction with ACE-2 might partly explain the different pathological consequences of infection by SARS-CoV and NL63.

MeSH terms

  • Coronavirus / physiology*
  • Coronavirus Infections / physiopathology*
  • Flow Cytometry
  • Humans
  • Kinetics
  • Membrane Glycoproteins / metabolism*
  • Peptidyl-Dipeptidase A / metabolism*
  • Protein Binding
  • SARS Virus / physiology*
  • Severe Acute Respiratory Syndrome / physiopathology*
  • Severity of Illness Index
  • Solutions
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins / metabolism*

Substances

  • MHV surface projection glycoprotein
  • Membrane Glycoproteins
  • Solutions
  • Spike Glycoprotein, Coronavirus
  • Viral Envelope Proteins
  • spike glycoprotein, SARS-CoV
  • Peptidyl-Dipeptidase A
  • angiotensin converting enzyme 2