SrasV1, PubMed, Checkpoint, bibRecord, 002702

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

Identifieur interne : 002702 ( PubMed/Checkpoint ); précédent : 002701; suivant : 002703

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 :

The Journal of infectious diseases [ 0022-1899 ] ; 2005.

RBID : pubmed:15688292

Descripteurs français

KwdFr :
- Antigènes CD (physiologie), Cyclophiline A (physiologie), Effet cytopathogène viral (physiologie), Expression des gènes, Humains, Liaison aux protéines, Lignée cellulaire, Protéines nucléocapside (physiologie), Protéines virales structurales (physiologie), Virus du SRAS (pathogénicité).
MESH :
- pathogénicité : Virus du SRAS.
- physiologie : Antigènes CD, Cyclophiline A, Effet cytopathogène viral, Protéines nucléocapside, Protéines virales structurales.
- Expression des gènes, Humains, Liaison aux protéines, Lignée cellulaire.

English descriptors

KwdEn :
- 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).
MESH :
- chemical , physiology : Antigens, CD, Cyclophilin A, Nucleocapsid Proteins, Viral Structural Proteins.
- chemical : Basigin.
- pathogenicity : SARS Virus.
- physiology : Cytopathogenic Effect, Viral.
- Cell Line, Gene Expression, Humans, Protein Binding.

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:

République populaire de Chine

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002909
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pubmed:15688292

Le document en format XML

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<front><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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<Abstract><AbstractText>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.</AbstractText>
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Function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome coronavirus.

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

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