ArticlePLoS pathogens2012
The TPR domain in the host Cyp40-like cyclophilin binds to the viral replication protein and inhibits the assembly of the tombusviral replicase.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- The gibberellic acid derived from the plastidial MEP pathway is involved in the accumulation of Bamboo mosaic virus.The New phytologist · 2022Article
- Race against Time between the Virus and Host: Actin-Assisted Rapid Biogenesis of Replication Organelles is Used by TBSV to Limit the Recruitment of Cellular Restriction Factors.Journal of virology · 2022Article
- Short Peptides Make a Big Difference: The Role of Botany-Derived AMPs in Disease Control and Protection of Human Health.International journal of molecular sciences · 2021Review
- Host protein chaperones, RNA helicases and the ubiquitin network highlight the arms race for resources between tombusviruses and their hosts.Advances in virus research · 2020Article
- The immunophilin repertoire of Plasmodiophora brassicae and functional analysis of PbCYP3 cyclophilin.Molecular genetics and genomics : MGG · 2018Article
- A thioredoxin NbTRXh2 from Nicotiana benthamiana negatively regulates the movement of Bamboo mosaic virus.Molecular plant pathology · 2018Article
- Microbial cyclophilins: specialized functions in virulence and beyond.World journal of microbiology & biotechnology · 2017Review
- Novel mechanism of regulation of tomato bushy stunt virus replication by cellular WW-domain proteins.Journal of virology · 2015Article
- The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome.Eukaryotic cell · 2015Article
- Identification of giant Mimivirus protein functions using RNA interference.Frontiers in microbiology · 2015Article
- The hop-like stress-induced protein 1 cochaperone is a novel cell-intrinsic restriction factor for mitochondrial tombusvirus replication.Journal of virology · 2014Article
- Tombusvirus-yeast interactions identify conserved cell-intrinsic viral restriction factors.Frontiers in plant science · 2014Review
- Cyclophilin A binds to the viral RNA and replication proteins, resulting in inhibition of tombusviral replicase assembly.Journal of virology · 2013Article
- Identification of novel host factors via conserved domain search: Cns1 cochaperone is a novel restriction factor of tombusvirus replication in yeast.Journal of virology · 2013Article
- Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis.The Journal of biological chemistry · 2013Article
- Authentic in vitro replication of two tombusviruses in isolated mitochondrial and endoplasmic reticulum membranes.Journal of virology · 2012Article
- Proteome-wide overexpression of host proteins for identification of factors affecting tombusvirus RNA replication: an inhibitory role of protein kinase C.Journal of virology · 2012Article
- Cyclophilin involvement in the replication of hepatitis C virus and other viruses.Biological chemistry · 2012Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Replication of plus-stranded RNA viruses is greatly affected by numerous host-coded proteins acting either as susceptibility or resistance factors. Previous genome-wide screens and global proteomics approaches with Tomato bushy stunt tombusvirus (TBSV) in a yeast model host revealed the involvement of cyclophilins, which are a large family of host prolyl isomerases, in TBSV replication. In this paper, we identified those members of the large cyclophilin family that interacted with the viral replication proteins and inhibited TBSV replication. Further characterization of the most effective cyclophilin, the Cyp40-like Cpr7p, revealed that it strongly inhibits many steps during TBSV replication in a cell-free replication assay. These steps include viral RNA recruitment inhibited via binding of Cpr7p to the RNA-binding region of the viral replication protein; the assembly of the viral replicase complex and viral RNA synthesis. Since the TPR (tetratricopeptide repeats) domain, but not the catalytic domain of Cpr7p is needed for the inhibitory effect on TBSV replication, it seems that the chaperone activity of Cpr7p provides the negative regulatory function. We also show that three Cyp40-like proteins from plants can inhibit TBSV replication in vitro and Cpr7p is also effective against Nodamura virus, an insect pathogen. Overall, the current work revealed a role for Cyp40-like proteins and their TPR domains as regulators of RNA virus replication.
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