TY - JOUR
T1 - Function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome coronavirus
AU - Chen, Zhinan
AU - Mi, Li
AU - Xu, Jing
AU - Yu, Jiyun
AU - Wang, Xianhui
AU - Jiang, Jianli
AU - Xing, Jinliang
AU - Shang, Peng
AU - Qian, Airong
AU - Li, Yu
AU - Shaw, Peter X.
AU - Wang, Jianwei
AU - Duan, Shumin
AU - Ding, Jin
AU - Fan, Chunmei
AU - Zhang, Yang
AU - Yang, Yong
AU - Yu, Xiaoling
AU - Feng, Qiang
AU - Li, Biehu
AU - Yao, Xiying
AU - Zhang, Zheng
AU - Li, Ling
AU - Xue, Xiaoping
AU - Zhu, Ping
PY - 2005/3/1
Y1 - 2005/3/1
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/13944272188
U2 - 10.1086/427811
DO - 10.1086/427811
M3 - 文章
C2 - 15688292
AN - SCOPUS:13944272188
SN - 0022-1899
VL - 191
SP - 755
EP - 760
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
IS - 5
ER -