| pubmed-article:9420211 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9420211 | lifeskim:mentions | umls-concept:C0014644 | lld:lifeskim |
| pubmed-article:9420211 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
| pubmed-article:9420211 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:9420211 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:9420211 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9420211 | pubmed:dateCreated | 1998-1-28 | lld:pubmed |
| pubmed-article:9420211 | pubmed:abstractText | The Epstein-Barr virus gH-gL complex includes a third glycoprotein, gp42, which is the product of the BZLF2 open reading frame (ORF). gp42 has been implicated as critical to infection of the B lymphocyte by virtue of its interaction with HLA class II on the B-cell surface. A neutralizing antibody that reacts with gp42 inhibits virus-cell fusion and blocks binding of gp42 to HLA class II; antibody to HLA class II can inhibit infection, and B cells that lack HLA class II can only be infected if HLA class II expression is restored. To confirm whether gp42 is an essential component of the virion, we derived a recombinant virus with a selectable marker inserted into the BZLF2 ORF to interrupt expression of the protein. A complex of gH and gL was expressed by the recombinant virus in the absence of gp42. Recombinant virus egressed from the cell normally and could bind to receptor-positive cells. It had, however, lost the ability to infect or transform B lymphocytes. Treatment with polyethylene glycol restored the infectivity of recombinant virus, confirming that gp42 is essential for penetration of the B-cell membrane. | lld:pubmed |
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| pubmed-article:9420211 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9420211 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9420211 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9420211 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9420211 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9420211 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:9420211 | pubmed:author | pubmed-author:WangXX | lld:pubmed |
| pubmed-article:9420211 | pubmed:author | pubmed-author:Hutt-Fletcher... | lld:pubmed |
| pubmed-article:9420211 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9420211 | pubmed:volume | 72 | lld:pubmed |
| pubmed-article:9420211 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9420211 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9420211 | pubmed:pagination | 158-63 | lld:pubmed |
| pubmed-article:9420211 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9420211 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9420211 | pubmed:articleTitle | Epstein-Barr virus lacking glycoprotein gp42 can bind to B cells but is not able to infect. | lld:pubmed |
| pubmed-article:9420211 | pubmed:affiliation | School of Biological Sciences, University of Missouri-Kansas City, 64110, USA. | lld:pubmed |
| pubmed-article:9420211 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9420211 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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