pubmed-article:8386261 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8386261 | lifeskim:mentions | umls-concept:C0019351 | lld:lifeskim |
pubmed-article:8386261 | lifeskim:mentions | umls-concept:C0027603 | lld:lifeskim |
pubmed-article:8386261 | lifeskim:mentions | umls-concept:C1423085 | lld:lifeskim |
pubmed-article:8386261 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
pubmed-article:8386261 | lifeskim:mentions | umls-concept:C0024779 | lld:lifeskim |
pubmed-article:8386261 | lifeskim:mentions | umls-concept:C0449719 | lld:lifeskim |
pubmed-article:8386261 | lifeskim:mentions | umls-concept:C0061666 | lld:lifeskim |
pubmed-article:8386261 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:8386261 | pubmed:dateCreated | 1993-5-17 | lld:pubmed |
pubmed-article:8386261 | pubmed:abstractText | Entry of herpes simplex virus (HSV) into cells is believed to be mediated by specific binding of envelope proteins to a cellular receptor. Neomycin specifically blocks this initial step in infection by HSV-1 but not HSV-2. Resistance of HSV-2 to this compound maps to a region of the genome encoding glycoprotein C (gC-2). We have studied the function of gC-2 in the initial interaction of the virus with the host cell, using HSV-2 mutants deleted for gC-2 and gC-2-rescued recombinants. Resistance to neomycin was directly linked to the presence of gC-2 within the viral genome. In addition, deletion of the gC-2 gene caused a marked delay in adsorption to cells relative to the wild-type virus. HSV-1 recombinants containing chimeric gC genes composed of HSV-1 and HSV-2 sequences were used to localize neomycin resistance within the N-terminal 223 amino acids of gC-2. This region of the glycoprotein comprises an important domain responsible for binding of HSV-2 to cell receptors in the presence of neomycin. A gC-2-negative mutant is still infectious, indicating that HSV-2 also has an alternative pathway of adsorption. | lld:pubmed |
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pubmed-article:8386261 | pubmed:language | eng | lld:pubmed |
pubmed-article:8386261 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8386261 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8386261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8386261 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8386261 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8386261 | pubmed:month | May | lld:pubmed |
pubmed-article:8386261 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:8386261 | pubmed:author | pubmed-author:GloriosoJ CJC | lld:pubmed |
pubmed-article:8386261 | pubmed:author | pubmed-author:CrumpackerC... | lld:pubmed |
pubmed-article:8386261 | pubmed:author | pubmed-author:LangelandNN | lld:pubmed |
pubmed-article:8386261 | pubmed:author | pubmed-author:HaarrLL | lld:pubmed |
pubmed-article:8386261 | pubmed:author | pubmed-author:GoinsW FWF | lld:pubmed |
pubmed-article:8386261 | pubmed:author | pubmed-author:DolterK EKE | lld:pubmed |
pubmed-article:8386261 | pubmed:author | pubmed-author:OZENMM | lld:pubmed |
pubmed-article:8386261 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8386261 | pubmed:volume | 67 | lld:pubmed |
pubmed-article:8386261 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8386261 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8386261 | pubmed:pagination | 2434-41 | lld:pubmed |
pubmed-article:8386261 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8386261 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8386261 | pubmed:articleTitle | Resistance of herpes simplex virus type 2 to neomycin maps to the N-terminal portion of glycoprotein C. | lld:pubmed |
pubmed-article:8386261 | pubmed:affiliation | Department of Microbiology and Immunology, Gade Institute, University of Bergen, Norway. | lld:pubmed |
pubmed-article:8386261 | pubmed:publicationType | Journal Article | lld:pubmed |