Membrane Interactions of the Mason-Pfizer Monkey Virus Matrix Protein and Its Budding Deficient Mutants

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22810%2F16%3A43901705" target="_blank" >RIV/60461373:22810/16:43901705 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22330/16:43901705

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.jmb.2016.10.010" target="_blank" >http://dx.doi.org/10.1016/j.jmb.2016.10.010</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jmb.2016.10.010" target="_blank" >10.1016/j.jmb.2016.10.010</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Membrane Interactions of the Mason-Pfizer Monkey Virus Matrix Protein and Its Budding Deficient Mutants

Popis výsledku v původním jazyce

Matrix proteins (MAs) play a key role in the transport of retroviral proteins inside infected cells and in the interaction with cellular membranes. In most retroviruses, retroviral MAs are N-terminally myristoylated. This modification serves as a membrane targeting signal and also as an anchor for membrane interaction. The aim of this work was to characterize the interactions anchoring retroviral MA at the plasma membrane of infected cell. To address this issue, we compared the structures and membrane affinity of the Mason-Pfizer monkey virus (M-PMV) wild-type MA with its two budding deficient double mutants, that is, T41I/T78I and Y28F/ Y67F. The structures of the mutants were determined using solution NMR spectroscopy, and their interactions with water-soluble phospholipids were studied.Water-soluble phospholipids are widely usedmodels for studying membrane interactions by solution NMR spectroscopy. However, this approachmight lead to artificial results due to unnatural hydrophobic interactions. Therefore, we used a new approach based on themeasurement of the loss of the 1H NMR signal intensity of the protein sample induced by the addition of the liposomes containing phospholipidswith naturally long fatty acids.HIV-1MAwas used as a positive control because its ability to interact with liposomes has already been described.We found that in contrast to HIV-1, theM-PMVMAinteracted with the liposomes differently and much weaker. In our in vivo experiments, the M-PMV MA did not co-localize with lipid rafts. Therefore, we concluded that M-PMV might adopt a different membrane binding mechanism than HIV-1.

Název v anglickém jazyce

Membrane Interactions of the Mason-Pfizer Monkey Virus Matrix Protein and Its Budding Deficient Mutants

Popis výsledku anglicky

Matrix proteins (MAs) play a key role in the transport of retroviral proteins inside infected cells and in the interaction with cellular membranes. In most retroviruses, retroviral MAs are N-terminally myristoylated. This modification serves as a membrane targeting signal and also as an anchor for membrane interaction. The aim of this work was to characterize the interactions anchoring retroviral MA at the plasma membrane of infected cell. To address this issue, we compared the structures and membrane affinity of the Mason-Pfizer monkey virus (M-PMV) wild-type MA with its two budding deficient double mutants, that is, T41I/T78I and Y28F/ Y67F. The structures of the mutants were determined using solution NMR spectroscopy, and their interactions with water-soluble phospholipids were studied.Water-soluble phospholipids are widely usedmodels for studying membrane interactions by solution NMR spectroscopy. However, this approachmight lead to artificial results due to unnatural hydrophobic interactions. Therefore, we used a new approach based on themeasurement of the loss of the 1H NMR signal intensity of the protein sample induced by the addition of the liposomes containing phospholipidswith naturally long fatty acids.HIV-1MAwas used as a positive control because its ability to interact with liposomes has already been described.We found that in contrast to HIV-1, theM-PMVMAinteracted with the liposomes differently and much weaker. In our in vivo experiments, the M-PMV MA did not co-localize with lipid rafts. Therefore, we concluded that M-PMV might adopt a different membrane binding mechanism than HIV-1.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EI - Biotechnologie a bionika

OECD FORD obor

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Projekt

<a href="/cs/project/GAP302%2F12%2F1895" target="_blank" >GAP302/12/1895: Role retrovirového matrixového proteinu při transportu virové částice a její interakci s cytoplasmatickou membránou.</a><br>

Návaznosti

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

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

Journal of molecular biology

ISSN

0022-2836

e-ISSN

—

Svazek periodika

428

Číslo periodika v rámci svazku

23

Stát vydavatele periodika

BE - Belgické království

Počet stran výsledku

15

Strana od-do

4708-4722

Kód UT WoS článku

000389110300009

EID výsledku v databázi Scopus

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