Myristoyl switch at the plasma membrane serves as the trigger for Gag cleavage and oligomerization of the matrix protein in the Mason-Pfizer monkey virus

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F23%3A43932689" target="_blank" >RIV/60461373:22330/23:43932689 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22340/23:43932689 RIV/60461373:22810/23:43932689

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Myristoyl switch at the plasma membrane serves as the trigger for Gag cleavage and oligomerization of the matrix protein in the Mason-Pfizer monkey virus

Popis výsledku v původním jazyce

Despite low sequence homology, retroviral structural proteins exhibit remarkable similarity in their secondary structures and interactions. These shared characteristics extend to their assembly processes, albeit with intriguing variations. While most retroviruses, including the well-known HIV-1, utilize the plasma membrane (PM) as a scaffold promoting the assembly of immature particles, which occurs simultaneously with budding and initiation of maturation, certain retroviruses, like the Mason-Pfizer monkey virus (M-PMV), undertake assembly within the cytoplasm. Consequently, M-PMV particles must be transported to the PM in their immature state, necessitating careful orchestration to prevent premature protease activation and specific cleavage events until they reach the PM. This crucial interaction is triggered by a bipartite signal composed of a cluster of basic residues in the matrix (MA) domain of the Gag polyprotein and a myristoyl moiety attached to MA at its N-terminus. In this study, we present evidence that myristoyl exposure from the MA core and its insertion into the PM bilayer occurs in M-PMV. Employing a combination of experimental techniques, we demonstrate that this process induces a structural change at the C-terminus of MA, supporting the efficient cleavage of MA from the downstream region of M-PMV Gag. These findings suggest that, in addition to the known effect of the myristoyl switch of on Gag multimerization and particle assembly in HIV-1, the myristoyl switch may also play a regulatory role in initiating sequential Gag cleavage events within immature M-PMV particles.

Název v anglickém jazyce

Myristoyl switch at the plasma membrane serves as the trigger for Gag cleavage and oligomerization of the matrix protein in the Mason-Pfizer monkey virus

Popis výsledku anglicky

Despite low sequence homology, retroviral structural proteins exhibit remarkable similarity in their secondary structures and interactions. These shared characteristics extend to their assembly processes, albeit with intriguing variations. While most retroviruses, including the well-known HIV-1, utilize the plasma membrane (PM) as a scaffold promoting the assembly of immature particles, which occurs simultaneously with budding and initiation of maturation, certain retroviruses, like the Mason-Pfizer monkey virus (M-PMV), undertake assembly within the cytoplasm. Consequently, M-PMV particles must be transported to the PM in their immature state, necessitating careful orchestration to prevent premature protease activation and specific cleavage events until they reach the PM. This crucial interaction is triggered by a bipartite signal composed of a cluster of basic residues in the matrix (MA) domain of the Gag polyprotein and a myristoyl moiety attached to MA at its N-terminus. In this study, we present evidence that myristoyl exposure from the MA core and its insertion into the PM bilayer occurs in M-PMV. Employing a combination of experimental techniques, we demonstrate that this process induces a structural change at the C-terminus of MA, supporting the efficient cleavage of MA from the downstream region of M-PMV Gag. These findings suggest that, in addition to the known effect of the myristoyl switch of on Gag multimerization and particle assembly in HIV-1, the myristoyl switch may also play a regulatory role in initiating sequential Gag cleavage events within immature M-PMV particles.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10607 - Virology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2023

Kód důvěrnosti údajů

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