Source:http://linkedlifedata.com/resource/pubmed/id/10580060
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1999-12-15
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pubmed:abstractText |
Substitution of Val(113) in Sendai virus (SeV) M protein generates non-functional polypeptides, characterized by their exclusion from virus particles and by their ability to interfere with virus particle production. These phenotypic traits correlate with a single-band PAGE migration profile, in contrast to wild-type M (M(wt )), which separates into two species, one of which is a phosphorylated form. The single-band migration is likely to result from a conformational change, as evidenced by the lack of maturation of a native epitope and by a particular tryptic digestion profile, and not from the phosphorylation of all M molecules, an assumption consistent with the PAGE migration feature. One of the M mutants (HA-M(30 ), an M protein carrying Thr(112)Met and Val(113) Glu substitutions tagged with an influenza virus haemagglutinin epitope) was characterized further in the context of SeV infection, i.e. under conditions of co-expression with M(wt). HA-M (30) is shown (i) to bind mainly to membrane fractions, (ii) not to co-precipitate M(wt), as HA-M(wt) does, (iii) to interfere with the binding of nucleocapsids to membranes and (iv) to accumulate in perinuclear regions, in contrast to HA-M(wt ), which is also found at the cell periphery. Such mutants constitute potential tools for the identification of critical steps in paramyxovirus assembly and budding.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-1317
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
80 ( Pt 11)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2977-86
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10580060-Amino Acid Sequence,
pubmed-meshheading:10580060-Animals,
pubmed-meshheading:10580060-Defective Viruses,
pubmed-meshheading:10580060-Molecular Sequence Data,
pubmed-meshheading:10580060-Mutation,
pubmed-meshheading:10580060-Nucleocapsid,
pubmed-meshheading:10580060-Protein Conformation,
pubmed-meshheading:10580060-Protein Structure, Secondary,
pubmed-meshheading:10580060-Rabbits,
pubmed-meshheading:10580060-Respirovirus,
pubmed-meshheading:10580060-Structure-Activity Relationship,
pubmed-meshheading:10580060-Viral Matrix Proteins,
pubmed-meshheading:10580060-Virion
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pubmed:year |
1999
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pubmed:articleTitle |
Characterization of Sendai virus M protein mutants that can partially interfere with virus particle production.
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pubmed:affiliation |
Department of Genetics and Microbiology, University of Geneva Medical School, CMU, 9 avenue de Champel, 1211 Geneva 4, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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