| pubmed-article:2398540 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2398540 | lifeskim:mentions | umls-concept:C0999948 | lld:lifeskim |
| pubmed-article:2398540 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:2398540 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
| pubmed-article:2398540 | lifeskim:mentions | umls-concept:C0449943 | lld:lifeskim |
| pubmed-article:2398540 | lifeskim:mentions | umls-concept:C0018903 | lld:lifeskim |
| pubmed-article:2398540 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:2398540 | pubmed:dateCreated | 1990-10-17 | lld:pubmed |
| pubmed-article:2398540 | pubmed:abstractText | Hemagglutination (HA) by the mammalian reoviruses is mediated by interactions between the viral sigma 1 protein and sialoglycoproteins on the erythrocyte surface. Three serotype 3 (T3) reovirus strains were identified that do not agglutinate either bovine or type O human erythrocytes (HA negative): T3 clone 43 (T3C43), T3 clone 44 (T3C44), and T3 clone 84 (T3C84). These three strains also showed a diminished capacity to bind the major erythrocyte sialoglycoprotein, glycophorin, in an enzyme-linked immunosorbent assay. To determine the molecular basis for these findings, we examined the deduced sigma 1 amino acid sequences of the three HA-negative T3 strains and four HA-positive T3 strains. The limited number of sequence differences in the sigma 1 proteins of these seven strains allowed us to identify single unique amino acid residues in each of the HA-negative strains (aspartate 198 in T3C43, leucine 204 in T3C44, and tryptophan 202 in T3C84) that cluster within a discrete region of the sigma 1 tail. The identification of sigma 1 residues important for HA and glycophorin binding suggests that tail-forming sequences are exposed on the virion surface, where they interact with carbohydrate residues on the surface of cells. | lld:pubmed |
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| pubmed-article:2398540 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2398540 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2398540 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2398540 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2398540 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2398540 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:2398540 | pubmed:author | pubmed-author:FieldsB NBN | lld:pubmed |
| pubmed-article:2398540 | pubmed:author | pubmed-author:DermodyT STS | lld:pubmed |
| pubmed-article:2398540 | pubmed:author | pubmed-author:Bassel-DubyRR | lld:pubmed |
| pubmed-article:2398540 | pubmed:author | pubmed-author:NibertM LML | lld:pubmed |
| pubmed-article:2398540 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2398540 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:2398540 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2398540 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2398540 | pubmed:pagination | 5173-6 | lld:pubmed |
| pubmed-article:2398540 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2398540 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2398540 | pubmed:articleTitle | A sigma 1 region important for hemagglutination by serotype 3 reovirus strains. | lld:pubmed |
| pubmed-article:2398540 | pubmed:affiliation | Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115. | lld:pubmed |
| pubmed-article:2398540 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2398540 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2398540 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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