ArticleNucleic acids research2024
Structure-functional characterization of Lactococcus AbiA phage defense system.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- A UG5 reverse transcriptase-nitrilase antiviral module confers phage immunity in the plant symbiontMicrobiology spectrum · 2026Article
- Coordinated RNA- and protein-templated synthesis of double-stranded DNA by a dual reverse transcriptase immune system.bioRxiv : the preprint server for biology · 2026Article
- Protein-templated synthesis of dinucleotide repeat DNA by an antiphage reverse transcriptase.Science (New York, N.Y.) · 2026Article
- Bacterial defense systems: Mechanisms, homology to eukaryotic immune systems, and applications.Zoological research · 2026Review
- Revisiting lactococcal abortive infection-like antiphage systems: diversity, structures, and mechanisms.FEMS microbiology reviews · 2026Review
- Anti-phage defense mechanism involving phage-encoded DNA binding protein and bacterial reverse transcriptase DRT4.Nature communications · 2025Article
- Molecular mechanism of the type 2 defense-associated reverse transcriptase.Nucleic acids research · 2025Article
- Antiviral reverse transcriptases reveal the evolutionary origin of telomerase.bioRxiv : the preprint server for biology · 2025Article
- Non-coding RNA mediates the defense-associated reverse transcriptase (DRT) anti-phage oligomerization transition.The EMBO journal · 2025Article
- A bacterial PrimPol-reverse transcriptase hybrid protein has a proofreading exonuclease activity that can be transferred to other reverse transcriptases.bioRxiv : the preprint server for biology · 2025Article
- Article
- Protein-primed DNA homopolymer synthesis by an antiviral reverse transcriptase.bioRxiv : the preprint server for biology · 2025Article
- LoVis4u: a locus visualization tool for comparative genomics and coverage profiles.NAR genomics and bioinformatics · 2025Article
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9 authors.
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Abstract
Bacterial reverse transcriptases (RTs) are a large and diverse enzyme family. AbiA, AbiK and Abi-P2 are abortive infection system (Abi) RTs that mediate defense against bacteriophages. What sets Abi RTs apart from other RT enzymes is their ability to synthesize long DNA products of random sequences in a template- and primer-independent manner. Structures of AbiK and Abi-P2 representatives have recently been determined, but there are no structural data available for AbiA. Here, we report the crystal structure of Lactococcus AbiA polymerase in complex with a single-stranded polymerization product. AbiA comprises three domains: an RT-like domain, a helical domain that is typical for Abi polymerases, and a higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domain that is common for many antiviral proteins. AbiA forms a dimer that distinguishes it from AbiK and Abi-P2, which form trimers/hexamers. We show the DNA polymerase activity of AbiA in an in vitro assay and demonstrate that it requires the presence of the HEPN domain which is enzymatically inactive. We validate our biochemical and structural results in vivo through bacteriophage infection assays. Finally, our in vivo results suggest that AbiA-mediated phage defense may not rely on AbiA-mediated cell death.
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