Function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome coronavirus

J Infect Dis. 2005 Mar 1;191(5):755-60. doi: 10.1086/427811. Epub 2005 Jan 25.

Abstract

To identify the function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome (SARS) coronavirus (CoV), we analyzed the protein-protein interaction among HAb18G/CD147, cyclophilin A (CyPA), and SARS-CoV structural proteins by coimmunoprecipitation and surface plasmon resonance analysis. Although none of the SARS-CoV proteins was found to be directly bound to HAb18G/CD147, the nucleocapsid (N) protein of SARS-CoV was bound to CyPA, which interacted with HAb18G/CD147. Further research showed that HAb18G/CD147, a transmembrane molecule, was highly expressed on 293 cells and that CyPA was integrated with SARS-CoV. HAb18G/CD147-antagonistic peptide (AP)-9, an AP of HAb18G/CD147, had a high rate of binding to 293 cells and an inhibitory effect on SARS-CoV. These results show that HAb18G/CD147, mediated by CyPA bound to SARS-CoV N protein, plays a functional role in facilitating invasion of host cells by SARS-CoV. Our findings provide some evidence for the cytologic mechanism of invasion by SARS-CoV and provide a molecular basis for screening anti-SARS drugs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, CD / physiology*
  • Basigin
  • Cell Line
  • Cyclophilin A / physiology
  • Cytopathogenic Effect, Viral / physiology
  • Gene Expression
  • Humans
  • Nucleocapsid Proteins / physiology
  • Protein Binding
  • SARS Virus / pathogenicity*
  • Viral Structural Proteins / physiology*

Substances

  • Antigens, CD
  • BSG protein, human
  • Nucleocapsid Proteins
  • Viral Structural Proteins
  • nucleocapsid protein, Coronavirus
  • Basigin
  • Cyclophilin A