Interaction of cellular helicase DHX15 and the Mason-Pfizer monkey virus genome

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22810%2F25%3A43932632" target="_blank" >RIV/60461373:22810/25:43932632 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22330/25:43932632

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Interaction of cellular helicase DHX15 and the Mason-Pfizer monkey virus genome

Popis výsledku v původním jazyce

RNA helicase DHX15 is involved in numerous steps of the cellular metabolism. Its activation by protein cofactors containing a glycine-rich sequence known as the G-patch domain (GPD) is crucial for its proper function. GPD has been identified in Mason-Pfizer monkey virus (M-PMV), in which it positively influences reverse transcriptase activity and viral infectivity. Similarities in the sequence and secondary structure of M-PMV GPD and cellular GPD proteins known to interact with DHX15 (e.g., NF-kappa-B-repressing factor) suggest shared mode of action. This is confirmed by the finding of DHX15 in purified M-PMV particles, but only those containing intact GPD, not in those with deleted version.Using Photoactivatable Ribonucleoside-Enhanced Crosslinking and Immunoprecipitation, a potential binding site of DHX15 was identified at the 3’ end of M-PMV genome. This region consists of the constitutive transport element, an RNA element essential for the export of unspliced viral RNA from nucleus, and its upstream sequence. Binding of DHX15 to this region was confirmed using microscale thermophoresis. Mutations in this region led to a decrease in the amount of DHX15 in purified M-PMV virions and also to a decrease in the virion’s gRNA content.A more profound comprehension of the interaction between DHX15 and M-PMV genome could provide a novel perspective on the metabolism of viral RNA during the retroviral infection.

Název v anglickém jazyce

Interaction of cellular helicase DHX15 and the Mason-Pfizer monkey virus genome

Popis výsledku anglicky

RNA helicase DHX15 is involved in numerous steps of the cellular metabolism. Its activation by protein cofactors containing a glycine-rich sequence known as the G-patch domain (GPD) is crucial for its proper function. GPD has been identified in Mason-Pfizer monkey virus (M-PMV), in which it positively influences reverse transcriptase activity and viral infectivity. Similarities in the sequence and secondary structure of M-PMV GPD and cellular GPD proteins known to interact with DHX15 (e.g., NF-kappa-B-repressing factor) suggest shared mode of action. This is confirmed by the finding of DHX15 in purified M-PMV particles, but only those containing intact GPD, not in those with deleted version.Using Photoactivatable Ribonucleoside-Enhanced Crosslinking and Immunoprecipitation, a potential binding site of DHX15 was identified at the 3’ end of M-PMV genome. This region consists of the constitutive transport element, an RNA element essential for the export of unspliced viral RNA from nucleus, and its upstream sequence. Binding of DHX15 to this region was confirmed using microscale thermophoresis. Mutations in this region led to a decrease in the amount of DHX15 in purified M-PMV virions and also to a decrease in the virion’s gRNA content.A more profound comprehension of the interaction between DHX15 and M-PMV genome could provide a novel perspective on the metabolism of viral RNA during the retroviral infection.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10607 - Virology

Projekt

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

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2025

Kód důvěrnosti údajů

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