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.
Zhinan Chen  1 ,  Li Mi ,  Jing Xu ,  Jiyun Yu ,  Xianhui Wang ,  Jianli Jiang ,  Jinliang Xing ,  Peng Shang ,  Airong Qian ,  Yu Li ,  Peter X Shaw ,  Jianwei Wang ,  Shumin Duan ,  Jin Ding ,  Chunmei Fan ,  Yang Zhang ,  Yong Yang ,  Xiaoling Yu ,  Qiang Feng ,  Biehu Li ,  Xiying Yao ,  Zheng Zhang ,  Ling Li ,  Xiaoping Xue ,  Ping Zhu
Affiliations
  • 1. Department of Cell Biology, the Fourth Military Medical University, Xi'an, China.
PMID: 15688292 DOI: 10.1086/427811
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.