| pubmed-article:3184275 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3184275 | lifeskim:mentions | umls-concept:C0027610 | lld:lifeskim |
| pubmed-article:3184275 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:3184275 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3184275 | lifeskim:mentions | umls-concept:C1149818 | lld:lifeskim |
| pubmed-article:3184275 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:3184275 | pubmed:dateCreated | 1988-12-20 | lld:pubmed |
| pubmed-article:3184275 | pubmed:abstractText | In addition to members of the Orthomyxoviridae and Paramyxoviridae, several coronaviruses have been shown to possess receptor-destroying activities. Purified bovine coronavirus (BCV) preparations have an esterase activity which inactivates O-acetylsialic acid-containing receptors on erythrocytes. Diisopropyl fluorophosphate (DFP) completely inhibits this receptor-destroying activity of BCV, suggesting that the viral enzyme is a serine esterase. Treatment of purified BCV with [3H]DFP and subsequent sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the proteins revealed that the E3 protein was specifically phosphorylated. This finding suggests that the esterase/receptor-destroying activity of BCV is associated with the E3 protein. Furthermore, treatment of BCV with DFP dramatically reduced its infectivity in a plaque assay. It is assumed that the esterase activity of BCV is required in an early step of virus replication, possibly during virus entry or uncoating. | lld:pubmed |
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| pubmed-article:3184275 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3184275 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3184275 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3184275 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3184275 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:3184275 | pubmed:author | pubmed-author:PalesePP | lld:pubmed |
| pubmed-article:3184275 | pubmed:author | pubmed-author:LeiderJJ | lld:pubmed |
| pubmed-article:3184275 | pubmed:author | pubmed-author:VlasakRR | lld:pubmed |
| pubmed-article:3184275 | pubmed:author | pubmed-author:LuytjesWW | lld:pubmed |
| pubmed-article:3184275 | pubmed:author | pubmed-author:SpaanWW | lld:pubmed |
| pubmed-article:3184275 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3184275 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:3184275 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3184275 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3184275 | pubmed:pagination | 4686-90 | lld:pubmed |
| pubmed-article:3184275 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:3184275 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3184275 | pubmed:articleTitle | The E3 protein of bovine coronavirus is a receptor-destroying enzyme with acetylesterase activity. | lld:pubmed |
| pubmed-article:3184275 | pubmed:affiliation | Department of Microbiology, Mount Sinai School of Medicine, New York, New York 10029-6574. | lld:pubmed |
| pubmed-article:3184275 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3184275 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3184275 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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