| Literature DB >> 29906704 |
Růžena Píchalová1, Tibor Füzik2, Barbora Vokatá3, Michaela Rumlová4, Manuel Llano5, Alžběta Dostálková6, Ivana Křížová7, Tomáš Ruml8, Pavel Ulbrich9.
Abstract
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.Entities:
Keywords: Cysteine mutagenesis; M-PMV capsid; M-PMV infectivity; Retrovirus assembly; Virus core stability
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Year: 2018 PMID: 29906704 PMCID: PMC6379149 DOI: 10.1016/j.virol.2018.06.001
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616