Interaction interface of mason-pfizer monkey virus matrix and envelope proteins

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F20%3A43921434" target="_blank" >RIV/60461373:22330/20:43921434 - isvavai.cz</a>

Alternative codes found

RIV/61388963:_____/20:00533120

Result on the web

<a href="https://jvi.asm.org/content/94/20/e01146-20" target="_blank" >https://jvi.asm.org/content/94/20/e01146-20</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1128/JVI.01146-20" target="_blank" >10.1128/JVI.01146-20</a>

Result language

angličtina

Original language name

Interaction interface of mason-pfizer monkey virus matrix and envelope proteins

Original language description

Retroviral envelope glycoprotein (Env) is essential for the specific recognition of the host cell and the initial phase of infection. As reported for human immunodeficiency virus (HIV), the recruitment of Env into a retroviral membrane envelope is mediated through its interaction with a Gag polyprotein precursor of structural proteins. This interaction, occurring between the matrix domain (MA) of Gag and the cytoplasmic tail (CT) of the transmembrane domain of Env, takes place at the host cell plasma membrane. To determine whether the MA of Mason-Pfizer monkey virus (M-PMV) also interacts directly with the CT of Env, we mimicked the in vivo conditions in an in vitro experiment by using a CT in its physiological trimeric conformation mediated by the trimerization motif of the GCN4 yeast transcription factor. The MA protein was used at the concentration shifting the equilibrium to its trimeric form. The direct interaction between MA and CT was confirmed by a pulldown assay. Through the combination of nuclear magnetic resonance (NMR) spectroscopy and protein cross-linking followed by mass spectrometry analysis, the residues involved in mutual interactions were determined. NMR has shown that the C terminus of the CT is bound to the C-terminal part of MA. In addition, protein crosslinking confirmed the close proximity of the N-terminal part of CT and the N terminus of MA, which is enabled in vivo by their location at the membrane. These results are in agreement with the previously determined orientation of MA on the membrane and support the already observed mechanisms of M-PMV virus-like particle transport and budding. © 2020 American Society for Microbiology.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10607 - Virology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2020

Confidentiality

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

Name of the periodical

Journal of Virology

ISSN

0022-538X

e-ISSN

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Volume of the periodical

94

Issue of the periodical within the volume

20

Country of publishing house

US - UNITED STATES

Number of pages

14

Pages from-to

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UT code for WoS article

000576835500007

EID of the result in the Scopus database

2-s2.0-85092332106