ArticleJournal of virology2006
Distinct roles for nucleic acid in in vitro assembly of purified Mason-Pfizer monkey virus CANC proteins.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- Structural Determinants of Virion Assembly and Release in the C Terminus of the Mason-Pfizer Monkey Virus Capsid Protein.Journal of virology · 2021Article
- Effect of Small Polyanions on In Vitro Assembly of Selected Members of Alpha-, Beta- and Gammaretroviruses.Viruses · 2021Article
- Article
- PF74 and Its Novel Derivatives Stabilize Hexameric Lattice of HIV-1 Mature-Like Particles.Molecules (Basel, Switzerland) · 2020Article
- A simple, high-throughput stabilization assay to test HIV-1 uncoating inhibitors.Scientific reports · 2019Article
- Mason-Pfizer Monkey Virus Envelope Glycoprotein Cycling and Its Vesicular Co-Transport with Immature Particles.Viruses · 2018Article
- Conserved cysteines in Mason-Pfizer monkey virus capsid protein are essential for infectious mature particle formation.Virology · 2018Article
- Mutations in the Basic Region of the Mason-Pfizer Monkey Virus Nucleocapsid Protein Affect Reverse Transcription, Genomic RNA Packaging, and the Virus Assembly Site.Journal of virology · 2018Article
- Nucleic Acid Binding by Mason-Pfizer Monkey Virus CA Promotes Virus Assembly and Genome Packaging.Journal of virology · 2016Article
- Role of Mason-Pfizer monkey virus CA-NC spacer peptide-like domain in assembly of immature particles.Journal of virology · 2014Article
- Stabilization of the β-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity.Retrovirology · 2014Article
- Structure of the immature retroviral capsid at 8 Å resolution by cryo-electron microscopy.Nature · 2012Article
- In vitro assembly of virus-like particles of a gammaretrovirus, the murine leukemia virus XMRV.Journal of virology · 2012Article
- Protease cleavage leads to formation of mature trimer interface in HIV-1 capsid.PLoS pathogens · 2012Article
- Purification of proteins containing zinc finger domains using immobilized metal ion affinity chromatography.Protein expression and purification · 2011Article
- Conserved and variable features of Gag structure and arrangement in immature retrovirus particles.Journal of virology · 2010Article
- Effect of dimerizing domains and basic residues on in vitro and in vivo assembly of Mason-Pfizer monkey virus and human immunodeficiency virus.Journal of virology · 2010Article
- Heterologous expression of full-length capsid protein of porcine circovirus 2 in Escherichia coli and its potential use for detection of antibodies.Journal of virological methods · 2009Article
- A molecular switch required for retrovirus assembly participates in the hexagonal immature lattice.The EMBO journal · 2008Article
- Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.