pubmed-article:7683156 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7683156 | lifeskim:mentions | umls-concept:C0021335 | lld:lifeskim |
pubmed-article:7683156 | lifeskim:mentions | umls-concept:C0033840 | lld:lifeskim |
pubmed-article:7683156 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:7683156 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:7683156 | lifeskim:mentions | umls-concept:C1283195 | lld:lifeskim |
pubmed-article:7683156 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:7683156 | pubmed:dateCreated | 1993-5-27 | lld:pubmed |
pubmed-article:7683156 | pubmed:abstractText | The gIII glycoproteins of both bovine herpesvirus 1 (BHV 1) and pseudorabies virus (PrV) mediate the initial and dominant interactions between virus and permissive host cells. By studying virus binding to wild-type and heparin-deficient CHO cells, we demonstrated that the cellular heparin-like moieties play an essential role in BHV 1 and PrV gIII-mediated virus attachment. Subsequent studies were carried out to map the gIII structures that are responsible for heparin binding. First, based on the observation that BHV 1 and PrV are differentially sensitive to heparin inhibition of gIII-mediated attachment to cells, we conducted a gIII domain shuffling experiment. This involved the construction of a set of recombinant BHV 1 expressing BHV 1 and PrV gIII chimeras and then using the sensitivity to heparin inhibition as a means of mapping the potential heparin-binding regions on the gIII molecules. Next, we synthesized panels of partially overlapping BHV 1 and PrV gIII peptides and examined their reactivity to heparin. The results from these experiments demonstrated five heparin-binding sites between amino acid 129 and 310 of BHV 1 gIII and four heparin-binding sites between amino acid 90 and 275 of PrV gIII. | lld:pubmed |
pubmed-article:7683156 | pubmed:language | eng | lld:pubmed |
pubmed-article:7683156 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7683156 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7683156 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7683156 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7683156 | pubmed:month | May | lld:pubmed |
pubmed-article:7683156 | pubmed:issn | 0042-6822 | lld:pubmed |
pubmed-article:7683156 | pubmed:author | pubmed-author:BabiukL ALA | lld:pubmed |
pubmed-article:7683156 | pubmed:author | pubmed-author:ZambT JTJ | lld:pubmed |
pubmed-article:7683156 | pubmed:author | pubmed-author:LiangXX | lld:pubmed |
pubmed-article:7683156 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7683156 | pubmed:volume | 194 | lld:pubmed |
pubmed-article:7683156 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7683156 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7683156 | pubmed:pagination | 233-43 | lld:pubmed |
pubmed-article:7683156 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:7683156 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:7683156 | pubmed:articleTitle | Mapping of heparin-binding structures on bovine herpesvirus 1 and pseudorabies virus gIII glycoproteins. | lld:pubmed |
pubmed-article:7683156 | pubmed:affiliation | Veterinary Infectious Disease Organization, Saskatoon, Saskatchewan, Canada. | lld:pubmed |
pubmed-article:7683156 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7683156 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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