| pubmed-article:16439547 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16439547 | lifeskim:mentions | umls-concept:C0031254 | lld:lifeskim |
| pubmed-article:16439547 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16439547 | lifeskim:mentions | umls-concept:C1137683 | lld:lifeskim |
| pubmed-article:16439547 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:16439547 | lifeskim:mentions | umls-concept:C1522240 | lld:lifeskim |
| pubmed-article:16439547 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16439547 | pubmed:dateCreated | 2006-1-27 | lld:pubmed |
| pubmed-article:16439547 | pubmed:abstractText | The core protein of pestiviruses is released from the polyprotein by viral and cellular proteinases. Here we report on an additional intramembrane proteolytic step that generates the C terminus of the core protein. C-terminal processing of the core protein of classical swine fever virus (CSFV) was blocked by the inhibitor (Z-LL)(2)-ketone, which is specific for signal peptide peptidase (SPP). The same effect was obtained by overexpression of the dominant-negative SPP D(265)A mutant. The presence of (Z-LL)(2)-ketone reduced the viability of CSFV almost 100-fold in a concentration-dependent manner. Reduction of virus viability was also observed in infection experiments using a cell line that inducibly expressed SPP D(265)A. The position of SPP cleavage was determined by C-terminal sequencing of core protein purified from virions. The C terminus of CSFV core protein is alanine(255) and is located in the hydrophobic center of the signal peptide. The intramembrane generation of the C terminus of the CSFV core protein is almost identical to the processing scheme of the core protein of hepatitis C viruses. | lld:pubmed |
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| pubmed-article:16439547 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16439547 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16439547 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16439547 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16439547 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16439547 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:16439547 | pubmed:author | pubmed-author:MartoglioBrun... | lld:pubmed |
| pubmed-article:16439547 | pubmed:author | pubmed-author:ThielHeinz-Jü... | lld:pubmed |
| pubmed-article:16439547 | pubmed:author | pubmed-author:RümenapfTillT | lld:pubmed |
| pubmed-article:16439547 | pubmed:author | pubmed-author:Roman-SosaGle... | lld:pubmed |
| pubmed-article:16439547 | pubmed:author | pubmed-author:HeimannManuel... | lld:pubmed |
| pubmed-article:16439547 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16439547 | pubmed:volume | 80 | lld:pubmed |
| pubmed-article:16439547 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16439547 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16439547 | pubmed:pagination | 1915-21 | lld:pubmed |
| pubmed-article:16439547 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:16439547 | pubmed:meshHeading | pubmed-meshheading:16439547... | lld:pubmed |
| pubmed-article:16439547 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16439547 | pubmed:articleTitle | Core protein of pestiviruses is processed at the C terminus by signal peptide peptidase. | lld:pubmed |
| pubmed-article:16439547 | pubmed:affiliation | Institut für Virologie, FB Veterinärmedizin, Justus Liebig Universität Giessen, Frankfurter Str. 107, D-35392 Giessen, Germany. | lld:pubmed |
| pubmed-article:16439547 | pubmed:publicationType | Journal Article | lld:pubmed |
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