Calmodulin involvement in the late phase life cycle of Mason-Pfizer monkey virus

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F25%3A43932633" target="_blank" >RIV/60461373:22330/25:43932633 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22810/25:43932633

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Calmodulin involvement in the late phase life cycle of Mason-Pfizer monkey virus

Popis výsledku v původním jazyce

Some viruses exploit host calcium signaling pathways to regulate key steps in their life cycle. Calmodulin (CaM), a ubiquitous calcium-sensing protein, is known to interact with several viral proteins, modulating processes such as viral replication and assembly. Although the interaction between CaM and HIV-1 matrix (MA) protein has been characterized in detail, the exact role of CaM in the replication of retroviruses remains unclear.In this study, we investigated the interaction between the MA protein of Mason-Pfizer monkey virus (M-PMV) and CaM. Using microscale thermophoresis (MST), we demonstrated that M-PMV MA binds CaM in a calcium-dependent manner. Co-immunoprecipitation assays from HEK293T cells co-expressing the M-PMV structural polyprotein Gag and HA-tagged CaM confirmed the relevance of this interaction in vivo. Furthermore, we found that CaM enhances proteolytic cleavage of myristoylated M-PMV MAPP, an MA construct extended with a downstream region of the phosphoprotein that mimics the M-PMV Gag precursor. This suggests that CaM binding facilitates the myristoyl switch of M-PMV MA. This is supported by liposome binding experiments showing that CaM promotes MA association with liposomes mimicking the cytoplasmic membrane. Formation of CaM–MA complexes was further confirmed by protein crosslinking followed by mass spectrometric analysis. Together, our findings provide new insights into the interaction between CaM and M-PMV MA, highlighting a potential regulatory mechanism during the late phase of the retroviral life cycle.

Název v anglickém jazyce

Calmodulin involvement in the late phase life cycle of Mason-Pfizer monkey virus

Popis výsledku anglicky

Some viruses exploit host calcium signaling pathways to regulate key steps in their life cycle. Calmodulin (CaM), a ubiquitous calcium-sensing protein, is known to interact with several viral proteins, modulating processes such as viral replication and assembly. Although the interaction between CaM and HIV-1 matrix (MA) protein has been characterized in detail, the exact role of CaM in the replication of retroviruses remains unclear.In this study, we investigated the interaction between the MA protein of Mason-Pfizer monkey virus (M-PMV) and CaM. Using microscale thermophoresis (MST), we demonstrated that M-PMV MA binds CaM in a calcium-dependent manner. Co-immunoprecipitation assays from HEK293T cells co-expressing the M-PMV structural polyprotein Gag and HA-tagged CaM confirmed the relevance of this interaction in vivo. Furthermore, we found that CaM enhances proteolytic cleavage of myristoylated M-PMV MAPP, an MA construct extended with a downstream region of the phosphoprotein that mimics the M-PMV Gag precursor. This suggests that CaM binding facilitates the myristoyl switch of M-PMV MA. This is supported by liposome binding experiments showing that CaM promotes MA association with liposomes mimicking the cytoplasmic membrane. Formation of CaM–MA complexes was further confirmed by protein crosslinking followed by mass spectrometric analysis. Together, our findings provide new insights into the interaction between CaM and M-PMV MA, highlighting a potential regulatory mechanism during the late phase of the retroviral life cycle.

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

2025

Kód důvěrnosti údajů

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