Linked Life Data

9267002

Source:http://linkedlifedata.com/resource/pubmed/id/9267002

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-9-8
pubmed:databankReference
pubmed:abstractText
Genes encoding glycoprotein gH and gL homologues were localized in the genome of the gamma-herpesvirus bovine herpesvirus-4 (BHV-4). Both genes were sequenced and glutathione S-transferase fusion proteins were produced and used to immunize rabbits against the translation products of the two genes. The anti-gH serum recognized a protein with an apparent molecular mass (MM) of 110 kDa both in infected cells and in virions. This protein was sensitive to endo-beta-N-acetylglucosaminase-H (endoH) and endoglycosidase F-N-glycosidase F (endoF-PNGaseF) digestion. A protein with the same relative mobility was immunoprecipitated from infected cells radiolabelled with [3H]glucosamine which confirmed that this product (gp110), now designated BHV-4 gH, was glycosylated. Western blotting with the anti-gL serum detected in infected cells a product with an apparent MM ranging from 31-35 kDa and diffusely migrating protein species ranging from 45-65 kDa. Tunicamycin, monensin, endoH or endoF-PNGaseF treatments showed that both the 31-35 kDa and the 45-65 kDa proteins were glycosylated, gp31-35 being a precursor of the 45-65 kDa glycoprotein species. In radioimmunoprecipitation assays, the anti-gL serum immunoprecipitated from infected cells two glycosylated proteins with apparent MMs of 31-35 kDa (gp31-35) and 45-55 kDa (gp45-55). However a third glycoprotein, gp110, was also immunoprecipitated together with gp31-35 and gp45-55. gp110 and gp45-55 were subsequently confirmed to be virion glycoproteins corresponding to mature forms of BHV-4 gH and gL respectively. In addition, the present study clearly demonstrated complex formation between BHV-4 gH and gL both in virions and in infected cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
78 ( Pt 8)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2015-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9267002-Animals, pubmed-meshheading:9267002-Blotting, Western, pubmed-meshheading:9267002-Cattle, pubmed-meshheading:9267002-Cell Line, pubmed-meshheading:9267002-Cloning, Molecular, pubmed-meshheading:9267002-DNA, pubmed-meshheading:9267002-Gammaherpesvirinae, pubmed-meshheading:9267002-Gene Expression, pubmed-meshheading:9267002-Glutathione Transferase, pubmed-meshheading:9267002-Glycoside Hydrolases, pubmed-meshheading:9267002-Glycosylation, pubmed-meshheading:9267002-Kidney, pubmed-meshheading:9267002-Molecular Sequence Data, pubmed-meshheading:9267002-Molecular Weight, pubmed-meshheading:9267002-Monensin, pubmed-meshheading:9267002-Oligosaccharides, pubmed-meshheading:9267002-Rabbits, pubmed-meshheading:9267002-Recombinant Fusion Proteins, pubmed-meshheading:9267002-Tunicamycin, pubmed-meshheading:9267002-Viral Envelope Proteins, pubmed-meshheading:9267002-Virion
pubmed:year
1997
pubmed:articleTitle
Analysis of the biochemical properties of, and complex formation between, glycoproteins H and L of the gamma2 herpesvirus bovine herpesvirus-4.
pubmed:affiliation
Laboratory of Virology-Immunology, Faculty of Veterinary Medicine, University of Liège, Belgium. p.lomonte@vir.gla.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't