H2N2V1, PascalFrancis, Corpus, bibRecord, 000039

Non-compact nucleocapsid protein multimers in influenza-virus-infected cells

Identifieur interne : 000039 ( PascalFrancis/Corpus ); précédent : 000038; suivant : 000040

Non-compact nucleocapsid protein multimers in influenza-virus-infected cells

Auteurs : E. N. Prokudina ; N. P. Semenova ; V. M. Chumakov ; T. A. Grigorieva

Source :

Archives of virology [ 0304-8608 ] ; 2007.

RBID : Pascal:07-0265735

Descripteurs français

Pascal (Inist)
- Influenzavirus, Nucléocapside, Protéine, Cellule infectée.

English descriptors

KwdEn :
- Infected cell, Influenzavirus, Nucleocapsid, Protein.

Abstract

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.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A03		`1`		`@0 Arch. virol.`
A05				`@2 152`
A06				`@2 5`
A08	`01`	`1`	`ENG`	`@1 Non-compact nucleocapsid protein multimers in influenza-virus-infected cells`
A11	`01`	`1`		`@1 PROKUDINA (E. N.)`
A11	`02`	`1`		`@1 SEMENOVA (N. P.)`
A11	`03`	`1`		`@1 CHUMAKOV (V. M.)`
A11	`04`	`1`		`@1 GRIGORIEVA (T. A.)`
A14	`01`			`@1 The D.I. Ivanovsky Institute of Virology @2 Moscow @3 RUS @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut.`
A20				`@1 981-988`
A21				`@1 2007`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 6355 @5 354000149588710130`
A44				`@0 0000 @1 © 2007 INIST-CNRS. All rights reserved.`
A45				`@0 20 ref.`
A47	`01`	`1`		`@0 07-0265735`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Archives of virology`
A66	`01`			`@0 AUT`
C01	`01`		`ENG`	@0 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.
C02	`01`	`X`		`@0 002A05C10`
C03	`01`	`X`	`FRE`	`@0 Influenzavirus @2 NW @5 01`
C03	`01`	`X`	`ENG`	`@0 Influenzavirus @2 NW @5 01`
C03	`01`	`X`	`SPA`	`@0 Influenzavirus @2 NW @5 01`
C03	`02`	`X`	`FRE`	`@0 Nucléocapside @5 05`
C03	`02`	`X`	`ENG`	`@0 Nucleocapsid @5 05`
C03	`02`	`X`	`SPA`	`@0 Nucleocápside @5 05`
C03	`03`	`X`	`FRE`	`@0 Protéine @5 06`
C03	`03`	`X`	`ENG`	`@0 Protein @5 06`
C03	`03`	`X`	`SPA`	`@0 Proteína @5 06`
C03	`04`	`X`	`FRE`	`@0 Cellule infectée @5 07`
C03	`04`	`X`	`ENG`	`@0 Infected cell @5 07`
C03	`04`	`X`	`SPA`	`@0 Célula infectada @5 07`
C07	`01`	`X`	`FRE`	`@0 Orthomyxoviridae @2 NW`
C07	`01`	`X`	`ENG`	`@0 Orthomyxoviridae @2 NW`
C07	`01`	`X`	`SPA`	`@0 Orthomyxoviridae @2 NW`
C07	`02`	`X`	`FRE`	`@0 Virus @2 NW`
C07	`02`	`X`	`ENG`	`@0 Virus @2 NW`
C07	`02`	`X`	`SPA`	`@0 Virus @2 NW`
N21				`@1 176`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 07-0265735 INIST
ET :	Non-compact nucleocapsid protein multimers in influenza-virus-infected cells
AU :	PROKUDINA (E. N.); SEMENOVA (N. P.); CHUMAKOV (V. M.); GRIGORIEVA (T. A.)
AF :	The D.I. Ivanovsky Institute of Virology/Moscow/Russie (1 aut., 2 aut., 3 aut., 4 aut.)
DT :	Publication en série; Niveau analytique
SO :	Archives of virology; ISSN 0304-8608; Autriche; Da. 2007; Vol. 152; No. 5; Pp. 981-988; Bibl. 20 ref.
LA :	Anglais
EA :	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.
CC :	002A05C10
FD :	Influenzavirus; Nucléocapside; Protéine; Cellule infectée
FG :	Orthomyxoviridae; Virus
ED :	Influenzavirus; Nucleocapsid; Protein; Infected cell
EG :	Orthomyxoviridae; Virus
SD :	Influenzavirus; Nucleocápside; Proteína; Célula infectada
LO :	INIST-6355.354000149588710130
ID :	07-0265735

Links to Exploration step

Pascal:07-0265735

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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<ET>Non-compact nucleocapsid protein multimers in influenza-virus-infected cells</ET>
<AU>PROKUDINA (E. N.); SEMENOVA (N. P.); CHUMAKOV (V. M.); GRIGORIEVA (T. A.)</AU>
<AF>The D.I. Ivanovsky Institute of Virology/Moscow/Russie (1 aut., 2 aut., 3 aut., 4 aut.)</AF>
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<EA>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.</EA>
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   |area=    H2N2V1
   |flux=    PascalFrancis
   |étape=   Corpus
   |type=    RBID
   |clé=     Pascal:07-0265735
   |texte=   Non-compact nucleocapsid protein multimers in influenza-virus-infected cells
}}

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Non-compact nucleocapsid protein multimers in influenza-virus-infected cells

Non-compact nucleocapsid protein multimers in influenza-virus-infected cells

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