Počet záznamů: 1
Interaction Interface of Mason-Pfizer Monkey Virus Matrix and Envelope Proteins
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SYSNO ASEP 0533120 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Interaction Interface of Mason-Pfizer Monkey Virus Matrix and Envelope Proteins Tvůrce(i) Prchal, J. (CZ)
Sýs, Jakub (UOCHB-X) ORCID
Junková, Petra (UOCHB-X) ORCID
Lipov, J. (CZ)
Ruml, T. (CZ)Číslo článku e01146-20 Zdroj.dok. Journal of Virology - ISSN 0022-538X
Roč. 94, č. 20 (2020)Poč.str. 14 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova Env ; M-PMV ; retrovirus ; cytoplasmic tail ; protein interactions Vědní obor RIV CB - Analytická chemie, separace Obor OECD Analytical chemistry CEP EF16_019/0000729 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Omezený přístup Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000576835500007 EID SCOPUS 85092332106 DOI 10.1128/JVI.01146-20 Anotace 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 cross-linking 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. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2021 Elektronická adresa https://doi.org/10.1128/jvi.01146-20
Počet záznamů: 1