ArticleJournal of virology2009
Biological effect of Muller's Ratchet: distant capsid site can affect picornavirus protein processing.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Insights into Polyprotein Processing and RNA-Protein Interactions in Foot-and-Mouth Disease Virus Genome Replication.Journal of virology · 2023Article
- Article
- Review
- Adaptive value of foot-and-mouth disease virus capsid substitutions with opposite effects on particle acid stability.Scientific reports · 2021Article
- The Novel Genetic Background of Infectious Bursal Disease Virus Strains Emerging from the Action of Positive Selection.Viruses · 2021Article
- Identification of a short, highly conserved, motif required for picornavirus capsid precursor processing at distal sites.PLoS pathogens · 2019Article
- Muller's Ratchet and Ribosome Degeneration in the Obligate Intracellular ParasitesInternational journal of molecular sciences · 2018Article
- Emergency Services of Viral RNAs: Repair and Remodeling.Microbiology and molecular biology reviews : MMBR · 2018Review
- Porcine Epidemic Diarrhea Virus 3C-Like Protease Regulates Its Interferon Antagonism by Cleaving NEMO.Journal of virology · 2016Article
- How foot-and-mouth disease virus receptor mediates foot-and-mouth disease virus infection.Virology journal · 2015Review
- Adaptive evolution by recombination is not associated with increased mutation rates in Maize streak virus.BMC evolutionary biology · 2012Article
- Foot-and-mouth disease virus 3C protease cleaves NEMO to impair innate immune signaling.Journal of virology · 2012Article
- Viral quasispecies evolution.Microbiology and molecular biology reviews : MMBR · 2012Review
- Quasispecies as a matter of fact: viruses and beyond.Virus research · 2011Review
- Lethal mutagenesis of foot-and-mouth disease virus involves shifts in sequence space.Journal of virology · 2011Article
- Viral genome segmentation can result from a trade-off between genetic content and particle stability.PLoS genetics · 2011Article
- A multi-step process of viral adaptation to a mutagenic nucleoside analogue by modulation of transition types leads to extinction-escape.PLoS pathogens · 2010Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Repeated bottleneck passages of RNA viruses result in accumulation of mutations and fitness decrease. Here, we show that clones of foot-and-mouth disease virus (FMDV) subjected to bottleneck passages, in the form of plaque-to-plaque transfers in BHK-21 cells, increased the thermosensitivity of the viral clones. By constructing infectious FMDV clones, we have identified the amino acid substitution M54I in capsid protein VP1 as one of the lesions associated with thermosensitivity. M54I affects processing of precursor P1, as evidenced by decreased production of VP1 and accumulation of VP1 precursor proteins. The defect is enhanced at high temperatures. Residue M54 of VP1 is exposed on the virion surface, and it is close to the B-C loop where an antigenic site of FMDV is located. M54 is not in direct contact with the VP1-VP3 cleavage site, according to the three-dimensional structure of FMDV particles. Models to account for the effect of M54 in processing of the FMDV polyprotein are proposed. In addition to revealing a distance effect in polyprotein processing, these results underline the importance of pursuing at the biochemical level the biological defects that arise when viruses are subjected to multiple bottleneck events.
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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.