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Identification and characterization of polymerase inhibitors of L-protein of Rift Valley fever virus
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SYSNO ASEP 0578957 Document Type A - Abstract R&D Document Type O - Ostatní Title Identification and characterization of polymerase inhibitors of L-protein of Rift Valley fever virus Author(s) Král, Michal (UOCHB-X) ORCID
Kotačka, Tomáš (UOCHB-X)
Radilová, Kateřina (UOCHB-X) ORCID
Gregor, Jiří (UOCHB-X)
Machara, Aleš (UOCHB-X) ORCID
Reiberger, Róbert (UOCHB-X) ORCID
Kožíšek, Milan (UOCHB-X) RID, ORCIDSource Title Czech Chemical Society Symposium Series - ISSN 2336-7202
Roč. 21, č. 5 (2023), s. 183Number of pages 1 s. Publication form Print - P Action Annual meeting of the National Institute of Virology and Bacteriology (NIVB) /2./ Event date 02.10.2023 - 05.10.2023 VEvent location Kutná Hora Country CZ - Czech Republic Event type EUR Language eng - English Country CZ - Czech Republic Keywords Rift Valley fever virus ; L-protein ; polymerase inhibitors OECD category Virology R&D Projects LX22NPO5103 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Institutional support UOCHB-X - RVO:61388963 Annotation Rift Valley fever virus (RVFV) is a mosquito borne, pathogenic phlebovirus of the order Bunyavirales, causing severe disease in both humans and domesticated animals. Outbreaks of the Rift Valley Fever can have devastating impact on the economy of the affected countries, as the virus can cause immense losses of livestock estimated in hundreds of millions USD. Currently, no approved, specific treatment is available for the RVFV infections. Several vaccine types are available, although they are not widely used, and their actual efficiency and safety is questionable. Like other viruses of the Bunyavirales family, replication mechanism of the RVFV is mediated by the L protein. The 250 kDa large protein is responsible for most of the virus replication, it contains the endonuclease domain, the RNA-dependent RNA-polymerase domain and the cap-binding domain. This organization corresponds to the linear composition of the heterotrimeric complex PA-PB1-PB2 of the influenza3. The process of virus replication is initiated by a cap-snatching mechanism, during which the host mRNA is cleaved by the L protein endonuclease domain. The L protein is heavily conserved across the members of the virus family and, although sequentially different it is structurally and functionally closely similar to the RNA polymerase complex of the influenza A virus. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2024 Electronic address http://www.ccsss.cz/index.php/ccsss/issue/view/41/75
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