| pubmed-article:19706704 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19706704 | lifeskim:mentions | umls-concept:C0034497 | lld:lifeskim |
| pubmed-article:19706704 | lifeskim:mentions | umls-concept:C0003451 | lld:lifeskim |
| pubmed-article:19706704 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:19706704 | lifeskim:mentions | umls-concept:C0031689 | lld:lifeskim |
| pubmed-article:19706704 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:19706704 | lifeskim:mentions | umls-concept:C1176299 | lld:lifeskim |
| pubmed-article:19706704 | lifeskim:mentions | umls-concept:C0444930 | lld:lifeskim |
| pubmed-article:19706704 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:19706704 | pubmed:dateCreated | 2009-9-24 | lld:pubmed |
| pubmed-article:19706704 | pubmed:abstractText | We wanted to develop a therapeutic approach against rabies disease by targeting the lyssavirus transcription/replication complex. Because this complex (nucleoprotein N-RNA template processed by the L polymerase and its cofactor, the phosphoprotein P) is similar to that of other negative-strand RNA viruses, we aimed to design broad-spectrum antiviral drugs that could be used as a complement to postexposure vaccination and immunotherapy. Recent progress in understanding the structure/function of the rabies virus P, N, and L proteins predicts that the amino-terminal end of P is an excellent target for destabilizing the replication complex because it interacts with both L (for positioning onto the N-RNA template) and N (for keeping N soluble, as needed for viral RNA encapsidation). Thus, peptides mimicking various lengths of the amino-terminal end of P have been evaluated, as follows: (i) for binding properties to the N-P-L partners by the two-hybrid method; (ii) for their capacity to inhibit the transcription/replication of a rabies virus minigenome encoding luciferase in BHK-21-T7 cells; and (iii) for their capacity to inhibit rabies virus infection of BHK-21-T7 cells and of two derivatives of the neuronal SK-N-SH cell line. Peptides P60 and P57 (the first 60 and first 57 NH2 residues of P, respectively) exhibited a rapid, strong, and long-lasting inhibitory potential on luciferase expression (>95% from 24 h to 55 h). P42 was less efficient in its inhibition level (75% for 18 to 30 h) and duration (40% after 48 h). The most promising peptides were synthesized in tandem with the Tat sequence, allowing cell penetration. Their inhibitory effects were observed on BHK-21-T7 cells infected with rabies virus and Lagos bat virus but not with vesicular stomatitis virus. In neuronal cells, a significant inhibition of both nucleocapsid inclusions and rabies virus release was observed. | lld:pubmed |
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| pubmed-article:19706704 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19706704 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19706704 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19706704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19706704 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19706704 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19706704 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19706704 | pubmed:issn | 1098-5514 | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:JacobYvesY | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:TordoNoëlN | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:RuigrokRob... | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:RéalEléonoreE | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:JalletCorinne... | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:PréhaudChrist... | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:MéhouasStépha... | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:CaignardGrégo... | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:CastelGuillau... | lld:pubmed |
| pubmed-article:19706704 | pubmed:author | pubmed-author:ChtéouiMohame... | lld:pubmed |
| pubmed-article:19706704 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19706704 | pubmed:volume | 83 | lld:pubmed |
| pubmed-article:19706704 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19706704 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19706704 | pubmed:pagination | 10808-20 | lld:pubmed |
| pubmed-article:19706704 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
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