Non-compact nucleocapsid protein multimers in influenza-virus-infected cells
Identifieur interne : 001428 ( Main/Exploration ); précédent : 001427; suivant : 001429Non-compact nucleocapsid protein multimers in influenza-virus-infected cells
Auteurs : E. N. Prokudina [Russie] ; N. P. Semenova [Russie] ; V. M. Chumakov [Russie] ; T. A. Grigorieva [Russie]Source :
- Archives of Virology [ 0304-8608 ] ; 2007-05-01.
Descripteurs français
- KwdFr :
- Affinité des anticorps, Animaux, Anticorps antiviraux (immunologie), Anticorps monoclonaux (immunologie), Chiens, Conformation des protéines, Infections à Orthomyxoviridae (virologie), Lignée cellulaire, Protéines nucléocapside (), Protéines nucléocapside (immunologie), Protéines nucléocapside (métabolisme), Sous-type H2N2 du virus de la grippe A (immunologie), Sous-type H3N2 du virus de la grippe A (immunologie), Électrophorèse sur gel de polyacrylamide.
- MESH :
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Protéines nucléocapside, Sous-type H2N2 du virus de la grippe A, Sous-type H3N2 du virus de la grippe A.
- métabolisme : Protéines nucléocapside.
- virologie : Infections à Orthomyxoviridae.
- Affinité des anticorps, Animaux, Chiens, Conformation des protéines, Lignée cellulaire, Protéines nucléocapside, Électrophorèse sur gel de polyacrylamide.
- Pascal (Inist)
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Antibodies, Viral (immunology), Antibody Affinity, Cell Line, Dogs, Electrophoresis, Polyacrylamide Gel, Infected cell, Influenza A Virus, H2N2 Subtype (immunology), Influenza A Virus, H3N2 Subtype (immunology), Influenzavirus, Nucleocapsid, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (immunology), Nucleocapsid Proteins (metabolism), Orthomyxoviridae Infections (virology), Protein, Protein Conformation.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Nucleocapsid Proteins.
- immunology : Influenza A Virus, H2N2 Subtype, Influenza A Virus, H3N2 Subtype.
- chemical , metabolism : Nucleocapsid Proteins.
- virology : Orthomyxoviridae Infections.
- Animals, Antibody Affinity, Cell Line, Dogs, Electrophoresis, Polyacrylamide Gel, Protein Conformation.
Abstract
Summary.: We have previously shown that protease-resistant and highly immunoreactive compact NP oligomers, dissociating at +80 °C and possessing properties of folded proteins, are post-translationally formed in influenza-virus-infected cells. In this study we demonstrate that, in addition to compact NP oligomers, incompletely folded NP multimers are detected intracellularly by SDS/PAGE carried out under weak dissociating conditions. In cells infected with avian, human A(H2N2), and human A(H3N2) viruses, NP multimers are detected in the stacking gel of SDS/PAGE as retarded and loose structures dissociating at +50 °C. NP multimers are more sensitive to proteolysis than NP oligomers, but they are more resistant to proteolysis than NP monomers. In contrast to compact NP oligomers, NP multimers possess a weak immunoreactivity to some monoclonal antibodies. Pulse-chase experiments have shown that NP multimers appear at early stages of NP synthesis and are partially converted post-translationally into faster-migrating compact NP oligomers. In the course of infection, the excess NP multimers not converted into compact NP oligomers accumulate in cells and degrade. Under weak dissociating conditions, intracellular NP multimers are relatively stable in avian, human A(H2N2) and human A(H3N2) viruses and unstable in human A(H1N1) viruses, dissociating into monomers. NP multimers presumably serve to bring nascent unfolded NP molecules into close contact with each other for further oligomerization, to protect NP monomers from proteolysis, and to serve as intermediates in the posttranslational folding of NP.
Url:
DOI: 10.1007/s00705-006-0911-z
Affiliations:
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Le document en format XML
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In this study we demonstrate that, in addition to compact NP oligomers, incompletely folded NP multimers are detected intracellularly by SDS/PAGE carried out under weak dissociating conditions. In cells infected with avian, human A(H2N2), and human A(H3N2) viruses, NP multimers are detected in the stacking gel of SDS/PAGE as retarded and loose structures dissociating at +50 °C. NP multimers are more sensitive to proteolysis than NP oligomers, but they are more resistant to proteolysis than NP monomers. In contrast to compact NP oligomers, NP multimers possess a weak immunoreactivity to some monoclonal antibodies. Pulse-chase experiments have shown that NP multimers appear at early stages of NP synthesis and are partially converted post-translationally into faster-migrating compact NP oligomers. In the course of infection, the excess NP multimers not converted into compact NP oligomers accumulate in cells and degrade. Under weak dissociating conditions, intracellular NP multimers are relatively stable in avian, human A(H2N2) and human A(H3N2) viruses and unstable in human A(H1N1) viruses, dissociating into monomers. NP multimers presumably serve to bring nascent unfolded NP molecules into close contact with each other for further oligomerization, to protect NP monomers from proteolysis, and to serve as intermediates in the posttranslational folding of NP.</div></front></TEI><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><country name="Russie"><region name="District fédéral central"><name sortKey="Prokudina, E N" sort="Prokudina, E N" uniqKey="Prokudina E" first="E. N." last="Prokudina">E. N. Prokudina</name></region><name sortKey="Chumakov, V M" sort="Chumakov, V M" uniqKey="Chumakov V" first="V. M." last="Chumakov">V. M. Chumakov</name><name sortKey="Grigorieva, T A" sort="Grigorieva, T A" uniqKey="Grigorieva T" first="T. A." last="Grigorieva">T. A. Grigorieva</name><name sortKey="Semenova, N P" sort="Semenova, N P" uniqKey="Semenova N" first="N. P." last="Semenova">N. P. Semenova</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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