|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
2006-1-27
|
|
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.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-11533209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-12077416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-12145199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-14747544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-15163730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-15479818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-15681445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-15998642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-1870198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-2370675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-2449095,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-2545029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-8087844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-8189517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-8230432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-8388499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-8431436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-8862403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-9150918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-9486650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16439547-9499122
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0022-538X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
80
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1915-21
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:16439547-Amino Acid Sequence,
pubmed-meshheading:16439547-Animals,
pubmed-meshheading:16439547-Aspartic Acid Endopeptidases,
pubmed-meshheading:16439547-Cell Line,
pubmed-meshheading:16439547-Classical swine fever virus,
pubmed-meshheading:16439547-Dipeptides,
pubmed-meshheading:16439547-Enzyme Inhibitors,
pubmed-meshheading:16439547-Molecular Sequence Data,
pubmed-meshheading:16439547-Protein Processing, Post-Translational,
pubmed-meshheading:16439547-Protein Structure, Tertiary,
pubmed-meshheading:16439547-Sequence Analysis, Protein,
pubmed-meshheading:16439547-Swine,
pubmed-meshheading:16439547-Viral Core Proteins
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Core protein of pestiviruses is processed at the C terminus by signal peptide peptidase.
|
|
pubmed:affiliation |
Institut für Virologie, FB Veterinärmedizin, Justus Liebig Universität Giessen, Frankfurter Str. 107, D-35392 Giessen, Germany.
|
|
pubmed:publicationType |
Journal Article
|
