| pubmed-article:6283120 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6283120 | lifeskim:mentions | umls-concept:C0042760 | lld:lifeskim |
| pubmed-article:6283120 | lifeskim:mentions | umls-concept:C0014644 | lld:lifeskim |
| pubmed-article:6283120 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:6283120 | lifeskim:mentions | umls-concept:C1721019 | lld:lifeskim |
| pubmed-article:6283120 | lifeskim:mentions | umls-concept:C1422036 | lld:lifeskim |
| pubmed-article:6283120 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:6283120 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6283120 | pubmed:dateCreated | 1982-8-7 | lld:pubmed |
| pubmed-article:6283120 | pubmed:abstractText | The four major Epstein-Barr virion envelope components were separated by column chromatography and reconstituted into artificial liposomes. These liposomes were tested for their ability to bind selectively to Epstein-Barr virus receptor-positive cells. Only when the two high-molecular-weight glycoproteins, VE1 and VE2, were present together was a stable binding complex formed. The addition of the other virion envelope components did not increase the levels of binding. This binding was inhibited by unlabeled viable virions and by neutralizing antisera, which recognized the two components. Adsorption of viable virus was also eliminated by the antisera. The enzyme susceptibility pattern of the cell-liposome interaction is similar to that of the virus-cell interaction, thus confirming the specificity of the binding site. A model for Epstein-Barr virus binding in which VE1 and VE2 coordinately recognize the same binding site is presented. | lld:pubmed |
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| pubmed-article:6283120 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6283120 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6283120 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6283120 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:6283120 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:6283120 | pubmed:author | pubmed-author:KoideNN | lld:pubmed |
| pubmed-article:6283120 | pubmed:author | pubmed-author:KleinGG | lld:pubmed |
| pubmed-article:6283120 | pubmed:author | pubmed-author:WellsAA | lld:pubmed |
| pubmed-article:6283120 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6283120 | pubmed:volume | 41 | lld:pubmed |
| pubmed-article:6283120 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6283120 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6283120 | pubmed:pagination | 286-97 | lld:pubmed |
| pubmed-article:6283120 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6283120 | pubmed:year | 1982 | lld:pubmed |
| pubmed-article:6283120 | pubmed:articleTitle | Two large virion envelope glycoproteins mediate Epstein-Barr virus binding to receptor-positive cells. | lld:pubmed |
| pubmed-article:6283120 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6283120 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6283120 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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