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PubMed

Záznam pochází z PubMed

Distinct roles for nucleic acid in in vitro assembly of purified Mason-Pfizer monkey virus CANC proteins

Journal of virology. 2006 Jul ; 80 (14) : 7089-99.

J Virol
ISSN 0022-538X
Zdroj

Jazyk angličtina Země Spojené státy americké Médium print

Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem

Perzistentní odkaz https://www.medvik.cz/link/pmid16809314

Online Plný text

PubMed 16809314
PubMed Central PMC1489063
DOI 10.1128/jvi.02694-05
PII: 80/14/7089
Knihovny.cz E-zdroje

MeSH
bezbuněčný systém MeSH
genom virový fyziologie MeSH
genové produkty gag genetika metabolismus MeSH
HIV-1 izolace a purifikace fyziologie ultrastruktura MeSH
kapsida metabolismus ultrastruktura MeSH
konformace proteinů MeSH
lidé MeSH
Masonův-Pfizerův opičí virus izolace a purifikace fyziologie MeSH
mutace MeSH
oligonukleotidy genetika metabolismus MeSH
RNA ribozomální genetika metabolismus MeSH
RNA virová genetika metabolismus ultrastruktura MeSH
sestavení viru fyziologie MeSH
terciární struktura proteinů genetika MeSH
zvířata MeSH
Check Tag
lidé MeSH
zvířata MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
srovnávací studie MeSH
Názvy látek
genové produkty gag MeSH
oligonukleotidy MeSH
RNA ribozomální MeSH
RNA virová MeSH

In contrast to other retroviruses, Mason-Pfizer monkey virus (M-PMV) assembles immature capsids in the cytoplasm. We have compared the ability of minimal assembly-competent domains from M-PMV and human immunodeficiency virus type 1 (HIV-1) to assemble in vitro into virus-like particles in the presence and absence of nucleic acids. A fusion protein comprised of the capsid and nucleocapsid domains of Gag (CANC) and its N-terminally modified mutant (DeltaProCANC) were used to mimic the assembly of the viral core and immature particles, respectively. In contrast to HIV-1, where CANC assembled efficiently into cylindrical structures, the same domains of M-PMV were assembly incompetent. The addition of RNA or oligonucleotides did not complement this defect. In contrast, the M-PMV DeltaProCANC molecule was able to assemble into spherical particles, while that of HIV-1 formed both spheres and cylinders. For M-PMV, the addition of purified RNA increased the efficiency with which DeltaProCANC formed spherical particles both in terms of the overall amount and the numbers of completed spheres. The amount of RNA incorporated was determined, and for both rRNA and MS2-RNA, quantities similar to that of genomic RNA were encapsidated. Oligonucleotides also stimulated assembly; however, they were incorporated into DeltaProCANC spherical particles in trace amounts that could not serve as a stoichiometric structural component for assembly. Thus, oligonucleotides may, through a transient interaction, induce conformational changes that facilitate assembly, while longer RNAs appear to facilitate the complete assembly of spherical particles.

Department of Biochemistry and Microbiology Institute of Chemical Technology Technicka 3 166 28 Prague Czech Republic

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Distinct roles for nucleic acid in in vitro assembly of purified Mason-Pfizer monkey virus CANC proteins

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