| pubmed-article:10864656 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10864656 | lifeskim:mentions | umls-concept:C0030657 | lld:lifeskim |
| pubmed-article:10864656 | lifeskim:mentions | umls-concept:C0206545 | lld:lifeskim |
| pubmed-article:10864656 | lifeskim:mentions | umls-concept:C0019143 | lld:lifeskim |
| pubmed-article:10864656 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
| pubmed-article:10864656 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:10864656 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10864656 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:10864656 | lifeskim:mentions | umls-concept:C1721019 | lld:lifeskim |
| pubmed-article:10864656 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:10864656 | pubmed:dateCreated | 2000-8-22 | lld:pubmed |
| pubmed-article:10864656 | pubmed:abstractText | Human respiratory syncytial virus (RSV) F glycoprotein (RSV-F) can independently interact with immobilized heparin and facilitate both attachment to and infection of cells via an interaction with cellular heparan sulfate. RSV-glycosaminoglycan (GAG) interactions were evaluated using heparin-agarose affinity chromatography. RSV-F from A2- and B1/cp-52 (cp-52)-infected cell lysates, RSV-F derived from a recombinant vaccinia virus, and affinity-purified F protein all bound to and were specifically eluted from heparin columns. In infectivity inhibition studies, soluble GAGs decreased the infectivity of RSV A2 and cp-52, with bovine lung heparin exhibiting the highest specific activity against both A2 (50% effective dose [ED(50)] = 0.28 +/- 0.11 microg/ml) and cp-52 (ED(50) = 0.55 +/- 0. 14 microg/ml). Furthermore, enzymatic digestion of cell surface GAGs by heparin lyase I and heparin lyase III but not chondroitinase ABC resulted in a significant reduction in cp-52 infectivity. Moreover, bovine lung heparin inhibited radiolabeled A2 and cp-52 virus binding up to 90%. Taken together, these data suggest that RSV-F independently interacts with heparin/heparan sulfate and this type of interaction facilitates virus attachment and infectivity. | lld:pubmed |
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| pubmed-article:10864656 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10864656 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10864656 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10864656 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10864656 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10864656 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:10864656 | pubmed:author | pubmed-author:FeldmanS ASA | lld:pubmed |
| pubmed-article:10864656 | pubmed:author | pubmed-author:BeelerJ AJA | lld:pubmed |
| pubmed-article:10864656 | pubmed:author | pubmed-author:AudetSS | lld:pubmed |
| pubmed-article:10864656 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10864656 | pubmed:volume | 74 | lld:pubmed |
| pubmed-article:10864656 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10864656 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10864656 | pubmed:pagination | 6442-7 | lld:pubmed |
| pubmed-article:10864656 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:10864656 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10864656 | pubmed:articleTitle | The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulfate. | lld:pubmed |
| pubmed-article:10864656 | pubmed:affiliation | Laboratory of Pediatric and Respiratory Virus Diseases, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20852-1448, USA. feldmans@cber.fda.gov | lld:pubmed |
| pubmed-article:10864656 | pubmed:publicationType | Journal Article | lld:pubmed |
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