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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-6-6
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pubmed:databankReference | |
pubmed:abstractText |
The nucleotide sequences of the glycoprotein B (gB) genes of Marek's disease virus (MDV) serotypes 2 and 3 were determined (gB-2 and gB-3, respectively). The genomic locations of these genes coincide with that of the gB gene of serotype 1 MDV (gB-1). Alignment with gB-1 (Ross et al., 1989, J. Gen. Virol. 70, 1789-1804) revealed predicted amino acid identities of 83 and 82% for gB-2 and gB-3, respectively. Excluding the predicted N-terminal signal sequences, 8 of 9 potential N-linked glycosylation sites and all 10 cysteine residues in gB-1 are conserved in both gB-2 and gB-3. In addition, the putative proteolytic cleavage sites for processing of precursors (gp100s) to gp60s and gp49s are conserved among the three gB homologs. Fowlpox virus (FPV) recombinants expressing either the gB-2 or the gB-3 gene were constructed. We detected expression of authentic gB-2 and gB-3 complexes in cells infected with these FPV recombinants. Digestion of immunoprecipitated gB-1 and gB-3 with endoglycosidases revealed that both gp60s are modified by the additions of O-glycans and complex carbohydrates after cleavage of gp100s, while gp100s and gp49s contain only high-mannose carbohydrates. We confirm that the size differences between gB-1 and gB-3 complexes are due to different carbohydrate modifications.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein B, Marek's disease...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
200
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
484-93
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8178437-Amino Acid Sequence,
pubmed-meshheading:8178437-Antigens, Viral,
pubmed-meshheading:8178437-Base Sequence,
pubmed-meshheading:8178437-Carbohydrate Metabolism,
pubmed-meshheading:8178437-Fowlpox virus,
pubmed-meshheading:8178437-Gene Expression,
pubmed-meshheading:8178437-Genes, Viral,
pubmed-meshheading:8178437-Glycoside Hydrolases,
pubmed-meshheading:8178437-Herpesvirus 2, Gallid,
pubmed-meshheading:8178437-Molecular Sequence Data,
pubmed-meshheading:8178437-Polysaccharides,
pubmed-meshheading:8178437-Recombinant Proteins,
pubmed-meshheading:8178437-Sequence Analysis, DNA,
pubmed-meshheading:8178437-Sequence Homology, Amino Acid,
pubmed-meshheading:8178437-Sequence Homology, Nucleic Acid,
pubmed-meshheading:8178437-Serotyping,
pubmed-meshheading:8178437-Viral Envelope Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
The glycoprotein B genes of Marek's disease virus serotypes 2 and 3: identification and expression by recombinant fowlpox viruses.
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pubmed:affiliation |
USDA-Agricultural Research Service, Avian Disease and Oncology Laboratory, East Lansing, Michigan 48823.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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