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

Result code in 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>

Alternative codes found

RIV/60461373:22330/16:43901705

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EI - Biotechnology and bionics

OECD FORD branch

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Project

<a href="/en/project/GAP302%2F12%2F1895" target="_blank" >GAP302/12/1895: Role of retroviral matrix protein in virus particle targeting and interaction with plasma membrane.</a><br>

Continuities

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

Publication year

2016

Confidentiality

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

Name of the periodical

Journal of molecular biology

ISSN

0022-2836

e-ISSN

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Volume of the periodical

428

Issue of the periodical within the volume

23

Country of publishing house

BE - BELGIUM

Number of pages

15

Pages from-to

4708-4722

UT code for WoS article

000389110300009

EID of the result in the Scopus database

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