{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T18:18:07Z","timestamp":1791397087417,"version":"4.3.3"},"reference-count":51,"publisher":"American Society for Microbiology","issue":"20","license":[{"start":{"date-parts":[[2009,10,15]],"date-time":"2009-10-15T00:00:00Z","timestamp":1255564800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2009,10,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            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 NH\n            <jats:sub>2<\/jats:sub>\n            residues of P, respectively) exhibited a rapid, strong, and long-lasting inhibitory potential on luciferase expression (&gt;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.\n          <\/jats:p>","DOI":"10.1128\/jvi.00977-09","type":"journal-article","created":{"date-parts":[[2009,8,18]],"date-time":"2009-08-18T19:27:37Z","timestamp":1250623657000},"page":"10808-10820","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":68,"title":["Peptides That Mimic the Amino-Terminal End of the Rabies Virus Phosphoprotein Have Antiviral Activity"],"prefix":"10.1128","volume":"83","author":[{"given":"Guillaume","family":"Castel","sequence":"first","affiliation":[{"name":"Unite\u0301 Postulante des Strate\u0301gies Antivirales, CNRS URA-3015, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohamed","family":"Chte\u0301oui","sequence":"additional","affiliation":[{"name":"Unite\u0301 Postulante des Strate\u0301gies Antivirales, CNRS URA-3015, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gre\u0301gory","family":"Caignard","sequence":"additional","affiliation":[{"name":"Laboratoire de Ge\u0301nomique virale et Vaccination, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christophe","family":"Pre\u0301haud","sequence":"additional","affiliation":[{"name":"Unite\u0301 de Neuro-Immunologie Virale, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ste\u0301phanie","family":"Me\u0301houas","sequence":"additional","affiliation":[{"name":"Unite\u0301 Postulante des Strate\u0301gies Antivirales, CNRS URA-3015, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France"},{"name":"INSERM U561, Hopital Saint Vincent de Paul, 82 Avenue Denfert Rochereau, 75014 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ele\u0301onore","family":"Re\u0301al","sequence":"additional","affiliation":[{"name":"Unite\u0301 Postulante des Strate\u0301gies Antivirales, CNRS URA-3015, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France"},{"name":"Laboratory of Neurogenetics and Behavior, The Rockefeller University, 1230 York Avenue, New York, New York 10065"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Corinne","family":"Jallet","sequence":"additional","affiliation":[{"name":"Unite\u0301 Postulante des Strate\u0301gies Antivirales, CNRS URA-3015, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yves","family":"Jacob","sequence":"additional","affiliation":[{"name":"Unite\u0301 de Ge\u0301ne\u0301tique, Papillomavirus et Cancer Humain, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rob W. 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