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Conserved cysteines in Mason-Pfizer monkey virus capsid protein are essential for infectious mature particle formation

R. Píchalová, T. Füzik, B. Vokatá, M. Rumlová, M. Llano, A. Dostálková, I. Křížová, T. Ruml, P. Ulbrich,

. 2018 ; 521 (-) : 108-117. [pub] 20180612

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc19028375

Grantová podpora
SC1 GM115240 NIGMS NIH HHS - United States

Retrovirus assembly is driven mostly by Gag polyprotein oligomerization, which is mediated by inter and intra protein-protein interactions among its capsid (CA) domains. Mason-Pfizer monkey virus (M-PMV) CA contains three cysteines (C82, C193 and C213), where the latter two are highly conserved among most retroviruses. To determine the importance of these cysteines, we introduced mutations of these residues in both bacterial and proviral vectors and studied their impact on the M-PMV life cycle. These studies revealed that the presence of both conserved cysteines of M-PMV CA is necessary for both proper assembly and virus infectivity. Our findings suggest a crucial role of these cysteines in the formation of infectious mature particles.

Citace poskytuje Crossref.org

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$a Retrovirus assembly is driven mostly by Gag polyprotein oligomerization, which is mediated by inter and intra protein-protein interactions among its capsid (CA) domains. Mason-Pfizer monkey virus (M-PMV) CA contains three cysteines (C82, C193 and C213), where the latter two are highly conserved among most retroviruses. To determine the importance of these cysteines, we introduced mutations of these residues in both bacterial and proviral vectors and studied their impact on the M-PMV life cycle. These studies revealed that the presence of both conserved cysteines of M-PMV CA is necessary for both proper assembly and virus infectivity. Our findings suggest a crucial role of these cysteines in the formation of infectious mature particles.
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$a Füzik, Tibor $u Department of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Technická 5, 166 28 Prague, Czech Republic. Electronic address: fuzikt@vscht.cz.
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$a Vokatá, Barbora $u Department of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Technická 5, 166 28 Prague, Czech Republic. Electronic address: vokataa@vscht.cz.
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$a Rumlová, Michaela $u Department of Biotechnology, University of Chemistry and Technology Prague, Technická 5, 166 28 Prague, Czech Republic. Electronic address: rumlovai@vscht.cz.
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$a Llano, Manuel $u Department of Biological Sciences, University of Texas at El Paso, 500 West University El Paso, TX 79902, USA. Electronic address: mllano@utep.edu.
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$a Dostálková, Alžběta $u Department of Biotechnology, University of Chemistry and Technology Prague, Technická 5, 166 28 Prague, Czech Republic. Electronic address: dostalkl@vscht.cz. $7 xx0267672
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$a Křížová, Ivana $u Department of Biotechnology, University of Chemistry and Technology Prague, Technická 5, 166 28 Prague, Czech Republic. Electronic address: krizovaa@vscht.cz.
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$a Ruml, Tomáš $u Department of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Technická 5, 166 28 Prague, Czech Republic. Electronic address: rumlt@vscht.cz.
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$a Ulbrich, Pavel $u Department of Biochemistry and Microbiology, University of Chemistry and Technology Prague, Technická 5, 166 28 Prague, Czech Republic. Electronic address: ulbrichp@vscht.cz.
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