Effect of dimerizing domains and basic residues on in vitro and in vivo assembly of Mason-Pfizer monkey virus and human immunodeficiency virus
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem
Grantová podpora
R01 CA027834
NCI NIH HHS - United States
R37 CA027834
NCI NIH HHS - United States
CA 27834
NCI NIH HHS - United States
PubMed
20007269
PubMed Central
PMC2812359
DOI
10.1128/jvi.02022-09
PII: JVI.02022-09
Knihovny.cz E-zdroje
- MeSH
- buněčné linie MeSH
- DNA primery genetika MeSH
- DNA virů genetika MeSH
- Escherichia coli genetika ultrastruktura virologie MeSH
- HIV-1 genetika fyziologie MeSH
- lidé MeSH
- Masonův-Pfizerův opičí virus genetika fyziologie ultrastruktura MeSH
- molekulární sekvence - údaje MeSH
- multimerizace proteinu MeSH
- mutageneze MeSH
- nukleokapsida - proteiny chemie genetika fyziologie MeSH
- rekombinantní proteiny chemie genetika metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvence nukleotidů MeSH
- sekvenční homologie aminokyselin MeSH
- sestavení viru genetika fyziologie MeSH
- terciární struktura proteinů MeSH
- transmisní elektronová mikroskopie MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, N.I.H., Extramural MeSH
- Názvy látek
- DNA primery MeSH
- DNA virů MeSH
- nukleokapsida - proteiny MeSH
- rekombinantní proteiny MeSH
Assembly of immature retroviral particles is a complex process involving interactions of several specific domains of the Gag polyprotein localized mainly within capsid protein (CA), spacer peptide (SP), and nucleocapsid protein (NC). In the present work we focus on the contribution of NC to the oligomerization of CA leading to assembly of Mason-Pfizer monkey virus (M-PMV) and HIV-1. Analyzing in vitro assembly of substitution and deletion mutants of DeltaProCANC, we identified a "spacer-like" sequence (NC(15)) at the M-PMV NC N terminus. This NC(15) domain is indispensable for the assembly and cannot be replaced with oligomerization domains of GCN4 or CREB proteins. Although the M-PMV NC(15) occupies a position analogous to that of the HIV-1 spacer peptide, it could not be replaced by the latter one. To induce the assembly, both M-PMV NC(15) and HIV-1 SP1 must be followed by a short peptide that is rich in basic residues. This region either can be specific, i.e., derived from the downstream NC sequence, or can be a nonspecific positively charged peptide. However, it cannot be replaced by heterologous interaction domains either from GCN4 or from CREB. In summary, we report here a novel M-PMV spacer-like domain that is functionally similar to other retroviral spacer peptides and contributes to the assembly of immature-virus-like particles.
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