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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-10-13
pubmed:abstractText
Vaccinia virus encodes at least eight proteins that incorporate label from tritiated palmitic acid when it is added to infected cell cultures. Three of these palmitylproteins are encoded by the A33R, B5R, and F13L open reading frames and migrate by gel electrophoresis with relative molecular masses of 23-28, 42, and 37 kDa, respectively. In this report we provide evidence that the A22R and A36R open reading frames also encode palmitylproteins with apparent molecular masses of 22 and 50-55 kDa, respectively. Furthermore, the hemagglutinin protein (A56R) from the Copenhagen strain is shown to be palmitylated while the hemagglutinin protein from the WR and IHD-J strains is not. A 94-kDa VV palmitylprotein appears to be a multimeric complex composed of the B5R protein and possibly others. All vaccinia-encoded palmitylproteins are present in the membranous fraction of cells and are specific for the trans-Golgi network membrane-enveloped forms of the virus, suggesting that these proteins play a role in the envelopment and egress of virions or the infectivity of released virus.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0042-6822
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-206
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11017799-Acylation, pubmed-meshheading:11017799-Amino Acid Sequence, pubmed-meshheading:11017799-Amino Acid Substitution, pubmed-meshheading:11017799-Animals, pubmed-meshheading:11017799-Base Sequence, pubmed-meshheading:11017799-Cell Line, pubmed-meshheading:11017799-Centrifugation, pubmed-meshheading:11017799-Cloning, Molecular, pubmed-meshheading:11017799-Gene Expression Regulation, Viral, pubmed-meshheading:11017799-Golgi Apparatus, pubmed-meshheading:11017799-Hemagglutinins, Viral, pubmed-meshheading:11017799-Intracellular Membranes, pubmed-meshheading:11017799-Kinetics, pubmed-meshheading:11017799-Macromolecular Substances, pubmed-meshheading:11017799-Molecular Sequence Data, pubmed-meshheading:11017799-Molecular Weight, pubmed-meshheading:11017799-Mutation, pubmed-meshheading:11017799-Myristic Acid, pubmed-meshheading:11017799-Open Reading Frames, pubmed-meshheading:11017799-Palmitic Acid, pubmed-meshheading:11017799-Protein Processing, Post-Translational, pubmed-meshheading:11017799-Solubility, pubmed-meshheading:11017799-Transfection, pubmed-meshheading:11017799-Vaccinia virus, pubmed-meshheading:11017799-Viral Proteins, pubmed-meshheading:11017799-Virion
pubmed:year
2000
pubmed:articleTitle
Identification and analysis of vaccinia virus palmitylproteins.
pubmed:affiliation
Department of Microbiology, Oregon State University, Corvallis, Oregon 97331-3804, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.