| pubmed-article:2016768 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2016768 | lifeskim:mentions | umls-concept:C0011315 | lld:lifeskim |
| pubmed-article:2016768 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2016768 | lifeskim:mentions | umls-concept:C1860991 | lld:lifeskim |
| pubmed-article:2016768 | lifeskim:mentions | umls-concept:C1514570 | lld:lifeskim |
| pubmed-article:2016768 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:2016768 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:2016768 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:2016768 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:2016768 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2016768 | pubmed:dateCreated | 1991-5-20 | lld:pubmed |
| pubmed-article:2016768 | pubmed:abstractText | The cleavages at the junctions of the flavivirus nonstructural (NS) proteins NS2A/NS2B, NS2B/NS3, NS3/NS4A, and NS4B/NS5 share an amino acid sequence motif and are presumably catalyzed by a virus-encoded protease. We constructed recombinant vaccinia viruses expressing various portions of the NS region of the dengue virus type 4 polyprotein. By analyzing immune precipitates of 35S-labeled lysates of recombinant virus-infected cells, we could monitor the NS2A/NS2B, NS2B/NS3, and NS3/NS4A cleavages. A polyprotein composed of NS2A, NS2B, and the N-terminal 184 amino acids of NS3 was cleaved at the NS2A/NS2B and NS2B/NS3 junctions, whereas a similar polyprotein containing only the first 77 amino acids of NS3 was not cleaved. This finding is consistent with the proposal that the N-terminal 180 amino acids of NS3 constitute a protease domain. Polyproteins containing NS2A and NS3 with large in-frame deletions of NS2B were not cleaved at the NS2A/NS2B or NS2B/NS3 junctions. Coinfection with a recombinant expressing NS2B complemented these NS2B deletions for NS2B/NS3 cleavage and probably also for NS2A/NS2B cleavage. Thus, NS2B is also required for the NS2A/NS2B and NS2B/NS3 cleavages and can act in trans. Other experiments showed that NS2B was needed, apparently in cis, for NS3/NS4A cleavage and for a series of internal cleavages in NS3. Indirect evidence that NS3 can also act in trans was obtained. Models are discussed for a two-component protease activity requiring both NS2B and NS3. | lld:pubmed |
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| pubmed-article:2016768 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2016768 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2016768 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2016768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2016768 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2016768 | pubmed:month | May | lld:pubmed |
| pubmed-article:2016768 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:2016768 | pubmed:author | pubmed-author:LaiC JCJ | lld:pubmed |
| pubmed-article:2016768 | pubmed:author | pubmed-author:ZhangY MYM | lld:pubmed |
| pubmed-article:2016768 | pubmed:author | pubmed-author:FalgoutBB | lld:pubmed |
| pubmed-article:2016768 | pubmed:author | pubmed-author:PethelMM | lld:pubmed |
| pubmed-article:2016768 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2016768 | pubmed:volume | 65 | lld:pubmed |
| pubmed-article:2016768 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2016768 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2016768 | pubmed:pagination | 2467-75 | lld:pubmed |
| pubmed-article:2016768 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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