The Importance of the G-patch Motif of Mason-Pfizer Monkey Virus in the Recruitment and Activity of Cellular DHX15

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22810%2F25%3A43932656" target="_blank" >RIV/60461373:22810/25:43932656 - isvavai.cz</a>

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RIV/60461373:22330/25:43932656

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

The Importance of the G-patch Motif of Mason-Pfizer Monkey Virus in the Recruitment and Activity of Cellular DHX15

Popis výsledku v původním jazyce

The G‑patch motif is a glycine‑rich region composed of 45 amino acid residues that occurs exclusively in G‑patch proteins of eukaryotic cells. G‑patch proteins participate in fundamental cellular processes, particularly those associated with RNA metabolism. Specifically, the G‑patch mediates protein‑RNA or protein‑protein interactions, specifies the target, or enhances the enzymatic activity. Interestingly, despite no cells different from eukaryotic cells contain G‑patch proteins, betaretroviruses evolutionarily preserved this motif. Last year, we discovered a direct relationship between the G ‑patch localized within Gag‑Pro and Gag ‑Pro‑Pol polyproteins of the betaretrovirus Mason‑Pfizer monkey virus (M‑PMV) and the presence of the RNA helicase DHX15 in M‑PMV virions. DHX15 was revealed to be involved in two essential processes in the M‑PMV replication cycle: gRNA packaging and reverse transcription. Our study documented that DHX15 is recruited by the G‑patch via a mode similar to that published for the interaction of DHX15 with the cellular G ‑patch protein NF‑κB Repressing Factor (NKRF). The secondary structure of the M‑PMV G‑patch corresponds to that of the cellular G‑patch and includes two structural elements: a brace helix (BH) and a brace loop (BL). To investigatethe interchangeability and importance of the M‑PMV G ‑patch motif, we substituted M‑PMV BH for NKRF BH and examined its impact on the incorporation of DHX15 into the virions, M‑PMV gRNA packaging and helicase activity. Surprisingly, the substitution negatively affected the recruitment of DHX15 more than we expected. Our results indicate that the betaretroviral G‑patch interacts and activates DHX15 more effectively than its native cellular interaction partner.Supported by the project National Institute of virology and bacteriology (Programme EXCELES, ID Project No. LX22NPO5103) – Funded by the European Union – Next Generation EU.

Název v anglickém jazyce

The Importance of the G-patch Motif of Mason-Pfizer Monkey Virus in the Recruitment and Activity of Cellular DHX15

Popis výsledku anglicky

The G‑patch motif is a glycine‑rich region composed of 45 amino acid residues that occurs exclusively in G‑patch proteins of eukaryotic cells. G‑patch proteins participate in fundamental cellular processes, particularly those associated with RNA metabolism. Specifically, the G‑patch mediates protein‑RNA or protein‑protein interactions, specifies the target, or enhances the enzymatic activity. Interestingly, despite no cells different from eukaryotic cells contain G‑patch proteins, betaretroviruses evolutionarily preserved this motif. Last year, we discovered a direct relationship between the G ‑patch localized within Gag‑Pro and Gag ‑Pro‑Pol polyproteins of the betaretrovirus Mason‑Pfizer monkey virus (M‑PMV) and the presence of the RNA helicase DHX15 in M‑PMV virions. DHX15 was revealed to be involved in two essential processes in the M‑PMV replication cycle: gRNA packaging and reverse transcription. Our study documented that DHX15 is recruited by the G‑patch via a mode similar to that published for the interaction of DHX15 with the cellular G ‑patch protein NF‑κB Repressing Factor (NKRF). The secondary structure of the M‑PMV G‑patch corresponds to that of the cellular G‑patch and includes two structural elements: a brace helix (BH) and a brace loop (BL). To investigatethe interchangeability and importance of the M‑PMV G ‑patch motif, we substituted M‑PMV BH for NKRF BH and examined its impact on the incorporation of DHX15 into the virions, M‑PMV gRNA packaging and helicase activity. Surprisingly, the substitution negatively affected the recruitment of DHX15 more than we expected. Our results indicate that the betaretroviral G‑patch interacts and activates DHX15 more effectively than its native cellular interaction partner.Supported by the project National Institute of virology and bacteriology (Programme EXCELES, ID Project No. LX22NPO5103) – Funded by the European Union – Next Generation EU.

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)

Rok uplatnění

2025

Kód důvěrnosti údajů

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