| pubmed-article:15795300 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15795300 | lifeskim:mentions | umls-concept:C0010247 | lld:lifeskim |
| pubmed-article:15795300 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:15795300 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15795300 | lifeskim:mentions | umls-concept:C1514490 | lld:lifeskim |
| pubmed-article:15795300 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:15795300 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:15795300 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:15795300 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:15795300 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:15795300 | pubmed:dateCreated | 2005-3-29 | lld:pubmed |
| pubmed-article:15795300 | pubmed:abstractText | The ability of the 3A protein of coxsackievirus B (CVB) to inhibit protein secretion was investigated for this study. Here we show that the ectopic expression of CVB 3A blocked the transport of both the glycoprotein of vesicular stomatitis virus, a membrane-bound secretory marker, and the alpha-1 protease inhibitor, a luminal secretory protein, at a step between the endoplasmic reticulum (ER) and the Golgi complex. CVB 3A contains a conserved proline-rich region in its N terminus. The importance of this proline-rich region was investigated by introducing Pro-to-Ala substitutions. The mutation of Pro19 completely abolished the ability of 3A to inhibit ER-to-Golgi transport. The mutation of Pro14, Pro17, or Pro20 also impaired this ability, but to a lesser extent. The mutation of Pro18 had no effect. We also investigated the possible importance of this proline-rich region for the function of 3A in viral RNA replication. To this end, we introduced the Pro-to-Ala mutations into an infectious cDNA clone of CVB3. The transfection of cells with in vitro-transcribed RNAs of these clones gave rise to mutant viruses that replicated with wild-type characteristics. We concluded that the proline-rich region in CVB 3A is required for its ability to inhibit ER-to-Golgi transport, but not for its function in viral RNA replication. The functional relevance of the proline-rich region is discussed in light of the proposed structural model of 3A. | lld:pubmed |
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| pubmed-article:15795300 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15795300 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15795300 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15795300 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15795300 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15795300 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:15795300 | pubmed:author | pubmed-author:MelchersWille... | lld:pubmed |
| pubmed-article:15795300 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:15795300 | pubmed:author | pubmed-author:WesselsElsE | lld:pubmed |
| pubmed-article:15795300 | pubmed:author | pubmed-author:DuijsingsDani... | lld:pubmed |
| pubmed-article:15795300 | pubmed:author | pubmed-author:NotebaartRich... | lld:pubmed |
| pubmed-article:15795300 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15795300 | pubmed:volume | 79 | lld:pubmed |
| pubmed-article:15795300 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15795300 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15795300 | pubmed:pagination | 5163-73 | lld:pubmed |
| pubmed-article:15795300 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15795300 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15795300 | pubmed:articleTitle | A proline-rich region in the coxsackievirus 3A protein is required for the protein to inhibit endoplasmic reticulum-to-golgi transport. | lld:pubmed |
| pubmed-article:15795300 | pubmed:affiliation | Department of Medical Microbiology, Nijmegen Center for Molecular Life Sciences, University Medical Center Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. | lld:pubmed |
| pubmed-article:15795300 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15795300 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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