Identification and characterization of polymerase inhibitors of L-protein of Rift Valley fever virus

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00578957" target="_blank" >RIV/61388963:_____/23:00578957 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.ccsss.cz/index.php/ccsss/issue/view/41/75" target="_blank" >http://www.ccsss.cz/index.php/ccsss/issue/view/41/75</a>

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Identification and characterization of polymerase inhibitors of L-protein of Rift Valley fever virus

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Identification and characterization of polymerase inhibitors of L-protein of Rift Valley fever virus

Popis výsledku anglicky

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.

Druh

O - Ostatní výsledky

CEP obor

—

OECD FORD obor

10607 - Virology

Projekt

<a href="/cs/project/LX22NPO5103" target="_blank" >LX22NPO5103: Národní institut virologie a bakteriologie</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů