ArticleProceedings of the National Academy of Sciences of the United States of America2001
Activation of the Mason-Pfizer monkey virus protease within immature capsids in vitro.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Regulation of Retroviral and SARS-CoV-2 Protease Dimerization and Activity through Reversible Oxidation.Antioxidants (Basel, Switzerland) · 2022Review
- Article
- Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300.bioRxiv : the preprint server for biology · 2021Article
- Construction of a molecular clone of ovine enzootic nasal tumor virus.Virology journal · 2016Article
- Direct evidence for intracellular anterograde co-transport of M-PMV Gag and Env on microtubules.Virology · 2014Article
- HIV-1 assembly, budding, and maturation.Cold Spring Harbor perspectives in medicine · 2012Review
- High-resolution structure of a retroviral protease folded as a monomer.Acta crystallographica. Section D, Biological crystallography · 2011Article
- The initial step in human immunodeficiency virus type 1 GagProPol processing can be regulated by reversible oxidation.PloS one · 2010Article
- The impact of altered polyprotein ratios on the assembly and infectivity of Mason-Pfizer monkey virus.Virology · 2009Article
- Article
- Basic residues in the Mason-Pfizer monkey virus gag matrix domain regulate intracellular trafficking and capsid-membrane interactions.Journal of virology · 2007Article
- An early stage of Mason-Pfizer monkey virus budding is regulated by the hydrophobicity of the Gag matrix domain core.Journal of virology · 2004Article
- Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation.Journal of virology · 2003Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
For all retroviruses, the completion of the viral budding process correlates with the activation of the viral protease by an unknown mechanism, and, as the structural (Gag) polyproteins are cleaved by the viral protease, maturation of the immature virus-like particle into an infectious virion. Unlike most retroviruses, the Mason-Pfizer monkey virus Gag polyproteins assemble into immature capsids within the cytoplasm of the cell before the viral budding event. The results reported here describe a unique experimental system in which Mason-Pfizer monkey virus immature capsids are removed from the cell, and the protease is activated in vitro by the addition of a reducing agent. The cleavage of the protease from the precursor form is a primary event, which proceeds with a half time of 14 min, and is followed by authentic processing of the Gag polyproteins. Activity of the viral protease in vitro depends on pH, with an increase in catalytic rates at acidic and neutral pH. The initiation of protease activity within immature capsids in vitro demonstrates that viral protease activity is sensitive to oxidation-reduction conditions, and that the viral protease can be activated in the absence of viral budding.
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