ArticleVirus genes2020
The ea22 gene of lambdoid phages: preserved prolysogenic function despite of high sequence diversity.
Article in Virus genes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- Isolation, characterization, and whole-genome analysis of the novel temperate bacteriophage Ph-p5 infecting Glutamicibacter halophytocola.Archives of virology · 2025Article
- Genomic and proteomic analyses of Nus-dependent non-lambdoid phages reveal a novel coliphage group prevalent in gut: mEpFrontiers in microbiology · 2025Article
- The NMR structure of the Orf63 lytic developmental protein from lambda bacteriophage.Scientific reports · 2024Article
- The NMR structure of the Ea22 lysogenic developmental protein from lambda bacteriophage.Scientific reports · 2024Article
- Complex effects of the exo-xis region of the Shiga toxin-converting bacteriophage Φ24Journal of applied genetics · 2024Article
- Molecular Modeling the Proteins from theAntibiotics (Basel, Switzerland) · 2021Review
- Bacteriophages of Shiga Toxin-ProducingPathogens (Basel, Switzerland) · 2021Review
- Ea22 Proteins from Lambda and Shiga Toxin-Producing Bacteriophages Balance Structural Diversity with Functional Similarity.ACS omega · 2020Article
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Authors and funding
9 authors.
Funding
Abstract
The exo-xis region of lambdoid phages contains open reading frames and genes that appear to be evolutionarily important. However, this region has received little attention up to now. In this study, we provided evidence that ea22, the largest gene of this region, favors the lysogenic pathway over the lytic pathway in contrast to other characterized exo-xis region genes including ea8.5, orf61, orf60a, and orf63. Our assays also suggest some functional analogies between Ea22 and the phage integrase protein (Int). While it is unsurprising that Ea22 operates similarly in both λ and Stx phages, we have observed some distinctions that may arise from considerable sequence dissimilarity at the carboxy termini of each protein.
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