pubmed-article:9267002 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9267002 | lifeskim:mentions | umls-concept:C0206558 | lld:lifeskim |
pubmed-article:9267002 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
pubmed-article:9267002 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
pubmed-article:9267002 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:9267002 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:9267002 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:9267002 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:9267002 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:9267002 | pubmed:dateCreated | 1997-9-8 | lld:pubmed |
pubmed-article:9267002 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | 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. | lld:pubmed |
pubmed-article:9267002 | pubmed:language | eng | lld:pubmed |
pubmed-article:9267002 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9267002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9267002 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9267002 | pubmed:month | Aug | lld:pubmed |
pubmed-article:9267002 | pubmed:issn | 0022-1317 | lld:pubmed |
pubmed-article:9267002 | pubmed:author | pubmed-author:PastoretP PPP | lld:pubmed |
pubmed-article:9267002 | pubmed:author | pubmed-author:ThiryEE | lld:pubmed |
pubmed-article:9267002 | pubmed:author | pubmed-author:BublotMM | lld:pubmed |
pubmed-article:9267002 | pubmed:author | pubmed-author:LomontePP | lld:pubmed |
pubmed-article:9267002 | pubmed:author | pubmed-author:LyakuJ RJR | lld:pubmed |
pubmed-article:9267002 | pubmed:author | pubmed-author:FiléePP | lld:pubmed |
pubmed-article:9267002 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9267002 | pubmed:volume | 78 ( Pt 8) | lld:pubmed |
pubmed-article:9267002 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9267002 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9267002 | pubmed:pagination | 2015-23 | lld:pubmed |
pubmed-article:9267002 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:9267002 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9267002 | pubmed:articleTitle | Analysis of the biochemical properties of, and complex formation between, glycoproteins H and L of the gamma2 herpesvirus bovine herpesvirus-4. | lld:pubmed |
pubmed-article:9267002 | pubmed:affiliation | Laboratory of Virology-Immunology, Faculty of Veterinary Medicine, University of Liège, Belgium. p.lomonte@vir.gla.ac.uk | lld:pubmed |
pubmed-article:9267002 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9267002 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
family:PF05259.6 | family:pubmed | pubmed-article:9267002 | lld:pfam |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9267002 | lld:pubmed |