SrasV1, PubMed, Checkpoint, bibRecord, 002B71

Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A.

Identifieur interne : 002B71 ( PubMed/Checkpoint ); précédent : 002B70; suivant : 002B72

Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A.

Auteurs : Cheng Luo [République populaire de Chine] ; Haibin Luo ; Suxin Zheng ; Chunshan Gui ; Liduo Yue ; Changying Yu ; Tao Sun ; Peilan He ; Jing Chen ; Jianhua Shen ; Xiaomin Luo ; Yixue Li ; Hong Liu ; Donglu Bai ; Jingkang Shen ; Yiming Yang ; Fangqiu Li ; Jianping Zuo ; Rolf Hilgenfeld ; Gang Pei ; Kaixian Chen ; Xu Shen ; Hualiang Jiang

Source :

Biochemical and biophysical research communications [ 0006-291X ] ; 2004.

RBID : pubmed:15358143

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Binding Sites, Computational Biology, Cyclophilin A (genetics), Cyclophilin A (metabolism), Humans, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein Binding, Protein Structure, Tertiary, Reproducibility of Results, SARS Virus (genetics), SARS Virus (metabolism), Sequence Alignment, Severe Acute Respiratory Syndrome, Surface Plasmon Resonance.
MESH :
- chemical , genetics : Cyclophilin A, Nucleocapsid Proteins.
- chemical , metabolism : Cyclophilin A, Nucleocapsid Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- Amino Acid Sequence, Binding Sites, Computational Biology, Humans, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Binding, Protein Structure, Tertiary, Reproducibility of Results, Sequence Alignment, Severe Acute Respiratory Syndrome, Surface Plasmon Resonance.

Abstract

Severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid protein (NP) of SARS-CoV (SARS_NP) functions in enveloping the entire genomic RNA and interacts with viron structural proteins, thus playing important roles in the process of virus particle assembly and release. Protein-protein interaction analysis using bioinformatics tools indicated that SARS_NP may bind to human cyclophilin A (hCypA), and surface plasmon resonance (SPR) technology revealed this binding with the equilibrium dissociation constant ranging from 6 to 160nM. The probable binding sites of these two proteins were detected by modeling the three-dimensional structure of the SARS_NP-hCypA complex, from which the important interaction residue pairs between the proteins were deduced. Mutagenesis experiments were carried out for validating the binding model, whose correctness was assessed by the observed effects on the binding affinities between the proteins. The reliability of the binding sites derived by the molecular modeling was confirmed by the fact that the computationally predicted values of the relative free energies of the binding for SARS_NP (or hCypA) mutants to the wild-type hCypA (or SARS_NP) are in good agreement with the data determined by SPR. Such presently observed SARS_NP-hCypA interaction model might provide a new hint for facilitating the understanding of another possible SARS-CoV infection pathway against human cell.

DOI: 10.1016/j.bbrc.2004.07.003
PubMed: 15358143

Affiliations:

République populaire de Chine

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Le document en format XML

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<term>Computational Biology</term>
<term>Cyclophilin A (genetics)</term>
<term>Cyclophilin A (metabolism)</term>
<term>Humans</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Mutagenesis, Site-Directed</term>
<term>Nucleocapsid Proteins (genetics)</term>
<term>Nucleocapsid Proteins (metabolism)</term>
<term>Protein Binding</term>
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<term>SARS Virus (metabolism)</term>
<term>Sequence Alignment</term>
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<term>Cyclophiline A (métabolisme)</term>
<term>Données de séquences moléculaires</term>
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<term>Modèles moléculaires</term>
<term>Mutagenèse dirigée</term>
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<term>Reproducibility of Results</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid protein (NP) of SARS-CoV (SARS_NP) functions in enveloping the entire genomic RNA and interacts with viron structural proteins, thus playing important roles in the process of virus particle assembly and release. Protein-protein interaction analysis using bioinformatics tools indicated that SARS_NP may bind to human cyclophilin A (hCypA), and surface plasmon resonance (SPR) technology revealed this binding with the equilibrium dissociation constant ranging from 6 to 160nM. The probable binding sites of these two proteins were detected by modeling the three-dimensional structure of the SARS_NP-hCypA complex, from which the important interaction residue pairs between the proteins were deduced. Mutagenesis experiments were carried out for validating the binding model, whose correctness was assessed by the observed effects on the binding affinities between the proteins. The reliability of the binding sites derived by the molecular modeling was confirmed by the fact that the computationally predicted values of the relative free energies of the binding for SARS_NP (or hCypA) mutants to the wild-type hCypA (or SARS_NP) are in good agreement with the data determined by SPR. Such presently observed SARS_NP-hCypA interaction model might provide a new hint for facilitating the understanding of another possible SARS-CoV infection pathway against human cell.</div>
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<Month>11</Month>
<Day>03</Day>
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<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>04</Day>
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<Month>Aug</Month>
<Day>27</Day>
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<Abstract><AbstractText>Severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for SARS infection. Nucleocapsid protein (NP) of SARS-CoV (SARS_NP) functions in enveloping the entire genomic RNA and interacts with viron structural proteins, thus playing important roles in the process of virus particle assembly and release. Protein-protein interaction analysis using bioinformatics tools indicated that SARS_NP may bind to human cyclophilin A (hCypA), and surface plasmon resonance (SPR) technology revealed this binding with the equilibrium dissociation constant ranging from 6 to 160nM. The probable binding sites of these two proteins were detected by modeling the three-dimensional structure of the SARS_NP-hCypA complex, from which the important interaction residue pairs between the proteins were deduced. Mutagenesis experiments were carried out for validating the binding model, whose correctness was assessed by the observed effects on the binding affinities between the proteins. The reliability of the binding sites derived by the molecular modeling was confirmed by the fact that the computationally predicted values of the relative free energies of the binding for SARS_NP (or hCypA) mutants to the wild-type hCypA (or SARS_NP) are in good agreement with the data determined by SPR. Such presently observed SARS_NP-hCypA interaction model might provide a new hint for facilitating the understanding of another possible SARS-CoV infection pathway against human cell.</AbstractText>
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<ForeName>Xu</ForeName>
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<Author ValidYN="Y"><LastName>Jiang</LastName>
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Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A.

Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A.

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