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

Identifieur interne : 004827 ( Main/Exploration ); précédent : 004826; suivant : 004828

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

Auteurs : Zhinan Chen [République populaire de Chine] ; 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

Source :

RBID : pubmed:15688292

Descripteurs français

English descriptors

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.

DOI: 10.1086/427811
PubMed: 15688292


Affiliations:


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<term>Antigens, CD (physiology)</term>
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<term>Cyclophilin A (physiology)</term>
<term>Cytopathogenic Effect, Viral (physiology)</term>
<term>Gene Expression</term>
<term>Humans</term>
<term>Nucleocapsid Proteins (physiology)</term>
<term>Protein Binding</term>
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<term>Cyclophiline A (physiologie)</term>
<term>Effet cytopathogène viral (physiologie)</term>
<term>Expression des gènes</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Protéines nucléocapside (physiologie)</term>
<term>Protéines virales structurales (physiologie)</term>
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<term>Basigin</term>
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<div type="abstract" xml:lang="en">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.</div>
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