ArticleJournal of virology2011
Regulation of foamy virus protease activity by viral RNA: a novel and unique mechanism among retroviruses.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 34 citations in OpenAlex.
- Single-stranded nucleic acid binding enhances the in vitro catalytic activity of Chikungunya virus nsP2 protease.BBA advances · 2026Article
- Interplay between protease and reverse transcriptase dimerization in a model HIV-1 polyprotein.Protein science : a publication of the Protein Society · 2024Article
- Structures of Substrate Complexes of Foamy Viral Protease-Reverse Transcriptase.Journal of virology · 2021Article
- Review
- Foamy Virus Integrase in Development of Viral Vector for Gene Therapy.Journal of microbiology and biotechnology · 2020Review
- Review
- New windows into retroviral RNA structures.Retrovirology · 2018Review
- A purine-rich element in foamy virus pol regulates env splicing and gag/pol expression.Retrovirology · 2017Article
- Review
- Mutagenesis of N-terminal residues of feline foamy virus Gag reveals entirely distinct functions during capsid formation, particle assembly, Gag processing and budding.Retrovirology · 2016Article
- A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In Vitro.Journal of molecular biology · 2015Article
- AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase.Retrovirology · 2015Article
- Inhibition of foamy virus reverse transcriptase by human immunodeficiency virus type 1 RNase H inhibitors.Antimicrobial agents and chemotherapy · 2014Article
- Review
- Presentation overrides specificity: probing the plasticity of alphaviral proteolytic activity through mutational analysis.Journal of virology · 2013Article
- Foamy virus Gag p71-p68 cleavage is required for template switch of the reverse transcriptase.Journal of virology · 2013Article
- U1snRNP-mediated suppression of polyadenylation in conjunction with the RNA structure controls poly (A) site selection in foamy viruses.Retrovirology · 2013Article
- Foamy virus assembly with emphasis on pol encapsidation.Viruses · 2013Review
- Prototype foamy virus protease activity is essential for intraparticle reverse transcription initiation but not absolutely required for uncoating upon host cell entry.Journal of virology · 2013Article
- The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding.Retrovirology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Foamy viruses (FVs) synthesize the Pol precursor protein from a specific transcript. Thus, in contrast to what was found for orthoretroviruses, e.g., human immunodeficiency virus, no Gag-Pol precursor protein is synthesized. Foamy viral Pol consists of a protease (PR) domain, a reverse transcriptase domain, and an integrase domain and is processed into a mature protease-reverse transcriptase (PR-RT) fusion protein and the integrase. Protease activity has to be strictly regulated in order to avoid premature Gag and Pol processing before virus assembly. We have demonstrated recently that FV protease is an inactive monomer with a very weak dimerization tendency and postulated protease activation through dimerization. Here, we identify a specific protease-activating RNA motif (PARM) located in the pol region of viral RNA which stimulates PR activity in vitro and in vivo, revealing a novel and unique mechanism of retroviral protease activation. This mechanism is strikingly different to that of orthoretroviruses, where the protease can be activated even in the absence of viral RNA during the assembly of virus-like particles. Although it has been shown that the integrase domain is important for Pol uptake, activation of the foamy virus protease is integrase independent. We show that at least two foamy virus PR-RT molecules bind to the PARM and only RNAs containing the PARM result in significant activation of the protease. DNA harboring the PARM is not capable of protease activation. Structure determination of the PARM by selective 2' hydroxyl acylation analyzed by primer extension (SHAPE) revealed a distinct RNA folding, important for protease activation and thus virus maturation.
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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.