Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3.
Identifieur interne : 003051 ( Main/Exploration ); précédent : 003050; suivant : 003052Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3.
Auteurs : Benjamin W. Neuman [États-Unis] ; Jeremiah S. Joseph ; Kumar S. Saikatendu ; Pedro Serrano ; Amarnath Chatterjee ; Margaret A. Johnson ; Lujian Liao ; Joseph P. Klaus ; John R. Yates ; Kurt Wüthrich ; Raymond C. Stevens ; Michael J. Buchmeier ; Peter KuhnSource :
- Journal of virology [ 1098-5514 ] ; 2008.
Descripteurs français
- KwdFr :
- Acides nucléiques (métabolisme), Animaux, Cellules Vero, Cobalt (métabolisme), Liaison aux protéines, Phylogénie, Protein kinases (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (isolement et purification), Protéines virales non structurales (métabolisme), Protéomique, Sensibilité et spécificité, Virion (génétique), Virion (métabolisme).
- MESH :
- génétique : Protéines recombinantes, Protéines virales non structurales, Virion.
- isolement et purification : Protéines virales non structurales.
- métabolisme : Acides nucléiques, Cobalt, Protein kinases, Protéines recombinantes, Protéines virales non structurales, Virion.
- Animaux, Cellules Vero, Liaison aux protéines, Phylogénie, Protéines virales non structurales, Protéomique, Sensibilité et spécificité.
English descriptors
- KwdEn :
- Animals, Chlorocebus aethiops, Cobalt (metabolism), Nucleic Acids (metabolism), Phylogeny, Protein Binding, Protein Kinases (metabolism), Proteomics, Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sensitivity and Specificity, Vero Cells, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (isolation & purification), Viral Nonstructural Proteins (metabolism), Virion (genetics), Virion (metabolism).
- MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemical , genetics : Recombinant Proteins, Viral Nonstructural Proteins.
- chemical , isolation & purification : Viral Nonstructural Proteins.
- chemical , metabolism : Cobalt, Nucleic Acids, Protein Kinases, Recombinant Proteins, Viral Nonstructural Proteins.
- genetics : Virion.
- metabolism : Virion.
- Animals, Chlorocebus aethiops, Phylogeny, Protein Binding, Proteomics, Sensitivity and Specificity, Vero Cells.
Abstract
Severe acute respiratory syndrome (SARS) coronavirus infection and growth are dependent on initiating signaling and enzyme actions upon viral entry into the host cell. Proteins packaged during virus assembly may subsequently form the first line of attack and host manipulation upon infection. A complete characterization of virion components is therefore important to understanding the dynamics of early stages of infection. Mass spectrometry and kinase profiling techniques identified nearly 200 incorporated host and viral proteins. We used published interaction data to identify hubs of connectivity with potential significance for virion formation. Surprisingly, the hub with the most potential connections was not the viral M protein but the nonstructural protein 3 (nsp3), which is one of the novel virion components identified by mass spectrometry. Based on new experimental data and a bioinformatics analysis across the Coronaviridae, we propose a higher-resolution functional domain architecture for nsp3 that determines the interaction capacity of this protein. Using recombinant protein domains expressed in Escherichia coli, we identified two additional RNA-binding domains of nsp3. One of these domains is located within the previously described SARS-unique domain, and there is a nucleic acid chaperone-like domain located immediately downstream of the papain-like proteinase domain. We also identified a novel cysteine-coordinated metal ion-binding domain. Analyses of interdomain interactions and provisional functional annotation of the remaining, so-far-uncharacterized domains are presented. Overall, the ensemble of data surveyed here paint a more complete picture of nsp3 as a conserved component of the viral protein processing machinery, which is intimately associated with viral RNA in its role as a virion component.
DOI: 10.1128/JVI.02631-07
PubMed: 18367524
Affiliations:
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Proteins packaged during virus assembly may subsequently form the first line of attack and host manipulation upon infection. A complete characterization of virion components is therefore important to understanding the dynamics of early stages of infection. Mass spectrometry and kinase profiling techniques identified nearly 200 incorporated host and viral proteins. We used published interaction data to identify hubs of connectivity with potential significance for virion formation. Surprisingly, the hub with the most potential connections was not the viral M protein but the nonstructural protein 3 (nsp3), which is one of the novel virion components identified by mass spectrometry. Based on new experimental data and a bioinformatics analysis across the Coronaviridae, we propose a higher-resolution functional domain architecture for nsp3 that determines the interaction capacity of this protein. Using recombinant protein domains expressed in Escherichia coli, we identified two additional RNA-binding domains of nsp3. One of these domains is located within the previously described SARS-unique domain, and there is a nucleic acid chaperone-like domain located immediately downstream of the papain-like proteinase domain. We also identified a novel cysteine-coordinated metal ion-binding domain. Analyses of interdomain interactions and provisional functional annotation of the remaining, so-far-uncharacterized domains are presented. Overall, the ensemble of data surveyed here paint a more complete picture of nsp3 as a conserved component of the viral protein processing machinery, which is intimately associated with viral RNA in its role as a virion component.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Buchmeier, Michael J" sort="Buchmeier, Michael J" uniqKey="Buchmeier M" first="Michael J" last="Buchmeier">Michael J. Buchmeier</name><name sortKey="Chatterjee, Amarnath" sort="Chatterjee, Amarnath" uniqKey="Chatterjee A" first="Amarnath" last="Chatterjee">Amarnath Chatterjee</name><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A" last="Johnson">Margaret A. Johnson</name><name sortKey="Joseph, Jeremiah S" sort="Joseph, Jeremiah S" uniqKey="Joseph J" first="Jeremiah S" last="Joseph">Jeremiah S. Joseph</name><name sortKey="Klaus, Joseph P" sort="Klaus, Joseph P" uniqKey="Klaus J" first="Joseph P" last="Klaus">Joseph P. Klaus</name><name sortKey="Kuhn, Peter" sort="Kuhn, Peter" uniqKey="Kuhn P" first="Peter" last="Kuhn">Peter Kuhn</name><name sortKey="Liao, Lujian" sort="Liao, Lujian" uniqKey="Liao L" first="Lujian" last="Liao">Lujian Liao</name><name sortKey="Saikatendu, Kumar S" sort="Saikatendu, Kumar S" uniqKey="Saikatendu K" first="Kumar S" last="Saikatendu">Kumar S. Saikatendu</name><name sortKey="Serrano, Pedro" sort="Serrano, Pedro" uniqKey="Serrano P" first="Pedro" last="Serrano">Pedro Serrano</name><name sortKey="Stevens, Raymond C" sort="Stevens, Raymond C" uniqKey="Stevens R" first="Raymond C" last="Stevens">Raymond C. Stevens</name><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name><name sortKey="Yates, John R" sort="Yates, John R" uniqKey="Yates J" first="John R" last="Yates">John R. Yates</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Neuman, Benjamin W" sort="Neuman, Benjamin W" uniqKey="Neuman B" first="Benjamin W" last="Neuman">Benjamin W. Neuman</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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