ArticleCell reports2025
Systematic identification and characterization of eukaryotic and viral 2A peptide-bond-skipping sequences.
Article in Cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Ribosome dynamics at the conserved PGP motif governs 2A peptide-bond-skipping efficiency.Nucleic acids research · 2026Article
- Generation of a New Immunodeficient Rat Model of Retinal Degeneration With LSL TdTomato Reporter and TdTomato-Pcp2 Expression.Translational vision science & technology · 2026Article
- High Throughput Characterization of Eukaryotic 2A-Like Peptides Identifies Novel Leucine-Associated Reduction in Protein Abundance.bioRxiv : the preprint server for biology · 2026Article
- Molecular architecture and diversity of StopGo/2A translational recoding.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Does a Polycistronic 2A Design Enable Functional FcRn Production for Antibody Pharmacokinetic Studies?Pharmaceutics · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
2A peptides are 18- to 22-amino-acid sequences that cause an unusual co-translational peptide-bond-skipping event. Initially discovered in viruses, they allow multiple proteins to be produced from a single open reading frame. Despite their utility, their evolutionary prevalence and sequence diversity remain unclear. Our computational analyses predict ∼2,200 2A peptides, significantly expanding the known class of 2A peptides (class A) and identifying a previously unrecognized class (class B). Predicted 2A peptides are widespread in RNA viruses and eukaryotes. Functional tests in human cells confirm skipping activity in most cases, suggesting that thousands of active 2A peptides exist. Mutational analysis reveals key residues near the skipped bond and within the upstream region; for instance, class B 2A peptides contain a conserved N-terminal tryptophan, whose register and identity are critical for activity. Together, our findings reveal that 2A peptides are more diverse and widespread than previously appreciated.
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Registered trials
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