SrasV1, PubMed, Curation, bibRecord, 001A87

Variable oligomerization modes in coronavirus non-structural protein 9.

Identifieur interne : 001A87 ( PubMed/Curation ); précédent : 001A86; suivant : 001A88

Variable oligomerization modes in coronavirus non-structural protein 9.

Auteurs : Rajesh Ponnusamy [Allemagne] ; Ralf Moll ; Thomas Weimar ; Jeroen R. Mesters ; Rolf Hilgenfeld

Source :

Journal of molecular biology [ 1089-8638 ] ; 2008.

RBID : pubmed:18694760

Descripteurs français

KwdFr :
- ADN (métabolisme), Acides nucléiques (métabolisme), Coronavirus (), Cristallographie aux rayons X, Cystéine (métabolisme), Dimérisation, Glutaraldéhyde (pharmacologie), Modèles moléculaires, Oxydoréduction (), Polymères, Protéines de liaison à l'ARN (), Protéines mutantes (), Protéines virales (), Protéines virales non structurales (), Protéines virales non structurales (métabolisme), Réactifs réticulants (pharmacologie), Résonance plasmonique de surface, Solutions, Structure quaternaire des protéines, Structure secondaire des protéines, Substitution d'acide aminé (), Test de retard de migration électrophorétique.
MESH :

English descriptors

KwdEn :
- Amino Acid Substitution (drug effects), Coronavirus (chemistry), Cross-Linking Reagents (pharmacology), Crystallography, X-Ray, Cysteine (metabolism), DNA (metabolism), Dimerization, Electrophoretic Mobility Shift Assay, Glutaral (pharmacology), Models, Molecular, Mutant Proteins (chemistry), Nucleic Acids (metabolism), Oxidation-Reduction (drug effects), Polymers, Protein Structure, Quaternary, Protein Structure, Secondary, RNA-Binding Proteins (chemistry), Solutions, Surface Plasmon Resonance, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism), Viral Proteins (chemistry).
MESH :
- chemical , chemistry : Mutant Proteins, RNA-Binding Proteins, Viral Nonstructural Proteins, Viral Proteins.
- chemical , metabolism : Cysteine, DNA, Nucleic Acids, Viral Nonstructural Proteins.
- chemical , pharmacology : Cross-Linking Reagents, Glutaral.
- chemistry : Coronavirus.
- drug effects : Amino Acid Substitution, Oxidation-Reduction.
- Crystallography, X-Ray, Dimerization, Electrophoretic Mobility Shift Assay, Models, Molecular, Polymers, Protein Structure, Quaternary, Protein Structure, Secondary, Solutions, Surface Plasmon Resonance.

Abstract

Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.

DOI: 10.1016/j.jmb.2008.07.071
PubMed: 18694760

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.</div>
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<Abstract><AbstractText>Non-structural protein 9 (Nsp9) of coronaviruses is believed to bind single-stranded RNA in the viral replication complex. The crystal structure of Nsp9 of human coronavirus (HCoV) 229E reveals a novel disulfide-linked homodimer, which is very different from the previously reported Nsp9 dimer of SARS coronavirus. In contrast, the structure of the Cys69Ala mutant of HCoV-229E Nsp9 shows the same dimer organization as the SARS-CoV protein. In the crystal, the wild-type HCoV-229E protein forms a trimer of dimers, whereas the mutant and SARS-CoV Nsp9 are organized in rod-like polymers. Chemical cross-linking suggests similar modes of aggregation in solution. In zone-interference gel electrophoresis assays and surface plasmon resonance experiments, the HCoV-229E wild-type protein is found to bind oligonucleotides with relatively high affinity, whereas binding by the Cys69Ala and Cys69Ser mutants is observed only for the longest oligonucleotides. The corresponding mutations in SARS-CoV Nsp9 do not hamper nucleic acid binding. From the crystal structures, a model for single-stranded RNA binding by Nsp9 is deduced. We propose that both forms of the Nsp9 dimer are biologically relevant; the occurrence of the disulfide-bonded form may be correlated with oxidative stress induced in the host cell by the viral infection.</AbstractText>
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Variable oligomerization modes in coronavirus non-structural protein 9.

Variable oligomerization modes in coronavirus non-structural protein 9.

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