Source:http://linkedlifedata.com/resource/pubmed/id/16289409
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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0006104,
umls-concept:C0014047,
umls-concept:C0033684,
umls-concept:C0041242,
umls-concept:C0079686,
umls-concept:C0086418,
umls-concept:C0178499,
umls-concept:C0205147,
umls-concept:C1514562,
umls-concept:C1527178,
umls-concept:C1621837,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
1-2
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pubmed:dateCreated |
2006-2-14
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pubmed:abstractText |
Flavivirus NS2B-NS3 proteases are associated with neurovirulence, becoming an important target for insight into the virus-induced pathogenesis. In this study, a phage-displayed human brain cDNA library was used to detect possible interaction between brain proteins and the Japanese encephalitis virus (JEV) NS2B-NS3 protease. After six rounds of biopanning, eight high-affinity NS2B-NS3 protease-interacting phages were identified. Identified NS2B-NS3 protease-interacting brain proteins contained several repeats of the consensus motifs E(R/K)(R/K)K and G(R/K)(R/K) with the dibasic residues, being similar to the conserved cleavage sites among flavivirus proteases. In addition, three identified brain proteins (phage-24, 34, and 44) were predicted as the domain of trypsin inhibitor and basic region leucine zipper (bZIP) using the SMART genome search. Immunoprecipitation and cleavage of two brain fusion proteins (phage-24 and phage-46) by the NS2B-NS3 protease confirmed the specific interaction between identified brain proteins and the JEV NS2B-NS3 protease. Fluorogenic peptide substrate assays revealed dose-manner inhibitory effects of these two brain fusion proteins on the trans-cleavage activity of NS2B-NS3 protease. Moreover, in vitro signaling pathway assay revealed that the JEV NS2B-NS3 protease significantly inhibited the signaling pathway of activator protein 1(AP1), a member of the bZIP family. Our results provide an insight into the protein interaction network of the JEV NS2B-NS3 protease in human brain.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/NS3 protein, flavivirus,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Nonstructural Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0168-1702
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
116
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
106-13
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16289409-Amino Acid Sequence,
pubmed-meshheading:16289409-Animals,
pubmed-meshheading:16289409-Cercopithecus aethiops,
pubmed-meshheading:16289409-Gene Library,
pubmed-meshheading:16289409-Humans,
pubmed-meshheading:16289409-Immunoprecipitation,
pubmed-meshheading:16289409-Leucine Zippers,
pubmed-meshheading:16289409-Molecular Sequence Data,
pubmed-meshheading:16289409-Nerve Tissue Proteins,
pubmed-meshheading:16289409-Peptide Library,
pubmed-meshheading:16289409-Protein Binding,
pubmed-meshheading:16289409-RNA Helicases,
pubmed-meshheading:16289409-Serine Endopeptidases,
pubmed-meshheading:16289409-Signal Transduction,
pubmed-meshheading:16289409-Transcription Factor AP-1,
pubmed-meshheading:16289409-Trypsin Inhibitors,
pubmed-meshheading:16289409-Vero Cells,
pubmed-meshheading:16289409-Viral Nonstructural Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
Japanese encephalitis virus NS2B-NS3 protease binding to phage-displayed human brain proteins with the domain of trypsin inhibitor and basic region leucine zipper.
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pubmed:affiliation |
Department of Medical Laboratory Science and Biotechnology, China Medical University, Taichung 404, Taiwan, Taiwan, ROC. cwlin@mail.cmu.edu.tw
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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