# Prokaryotic defense systems: Diversity and evolutionary adaptation

**Authors:** Changjialian Yang, Luyao Gong, Jing Guo, Hua Xiang

PMC · DOI: 10.1002/mlf2.70068 · mLife · 2026-02-21

## TL;DR

This paper reviews how prokaryotes have evolved diverse defense systems against viruses, highlighting their complexity and potential for biotechnology.

## Contribution

The paper provides a comprehensive overview of prokaryotic defense systems and their evolutionary dynamics.

## Key findings

- Prokaryotic defense systems include surface barriers, innate responses, and adaptive defenses.
- The co-evolution of RNA and protein components contributes to defense system diversity.
- Understanding these systems can inform biotechnology and immune system evolution.

## Abstract

Bacteriophages and archaeal viruses are the most abundant biological entities on Earth. Through a long‐standing co‐evolutionary arms race, they have driven the emergence of a diverse repertoire of prokaryotic defense systems. This review summarizes these systems, highlighting their diverse antiviral mechanisms across distinct stages of viral infection, from surface barriers and inducible innate responses to specific adaptive defenses, and the intricate interplay between these defense strategies. By examining host–virus counter defense dynamics, the trade‐off between survival benefit and adaptive cost, the co‐evolution of RNA and protein components, and the comparison with eukaryotic immune systems, we underscore the intrinsic complexity and evolutionary plasticity of prokaryotic antiviral immunity. A deeper understanding of these processes and mechanisms will not only shed light on the origins and evolution of the immune system but also provide valuable opportunities for the development of biotechnological tools.

## Full-text entities

- **Genes:** ADA (adenosine deaminase) [NCBI Gene 100] {aka ADA1}, SMOC1 (SPARC related modular calcium binding 1) [NCBI Gene 64093] {aka OAS}, CGAS (cyclic GMP-AMP synthase) [NCBI Gene 115004] {aka C6orf150, D4, MB21D1, h-cGAS}, ABCC6 (ATP binding cassette subfamily C member 6) [NCBI Gene 368] {aka ABC34, ARA, EST349056, GACI2, MLP1, MOAT-E}, ADAT2 (adenosine deaminase tRNA specific 2) [NCBI Gene 134637] {aka DEADC1, TAD2, dJ20N2, dJ20N2.1}, CASP8 (caspase 8) [NCBI Gene 841] {aka ALPS2B, CAP4, Casp-8, FLICE, MACH, MCH5}, SIRT1 (sirtuin 1) [NCBI Gene 23411] {aka SIR2, SIR2L1, SIR2alpha}, DROSHA (drosha ribonuclease III) [NCBI Gene 29102] {aka ETOHI2, HSA242976, RANSE3L, RN3, RNASE3L, RNASEN}, STING1 (stimulator of interferon response cGAMP interactor 1) [NCBI Gene 340061] {aka ERIS, MITA, MPYS, NET23, SAVI, STING}, ACR (acrosin) [NCBI Gene 49] {aka SPGF87}, ISG15 (ISG15 ubiquitin like modifier) [NCBI Gene 9636] {aka G1P2, IFI15, IMD38, IP17, UCRP, hUCRP}, CARF (calcium responsive transcription factor) [NCBI Gene 79800] {aka ALS2CR8, NYD-SP24}, TLR4 (toll like receptor 4) [NCBI Gene 7099] {aka ARMD10, CD284, TLR-4, TOLL}
- **Diseases:** SYSTEMS (MESH:D015619), toxicity (MESH:D064420), Type II Thoeris (MESH:D006938), Abi (MESH:D007239), R (MESH:C580424), MGEs (MESH:D014086), viral (MESH:D014777), CBASS (MESH:C566796), Type I Thoeris (MESH:D006969), TA (MESH:D065766)
- **Chemicals:** dAMP (MESH:C116255), NAD+ (MESH:D009243), lipids (MESH:D008055), ATP (MESH:D000255), cGAMP (MESH:C584311), NAD(P)+ (MESH:D009249), doxorubicin (MESH:D004317), Abi (-), sulfur (MESH:D013455), ITP (MESH:D007293), cyclic nucleotides (MESH:D009712), nucleotide (MESH:D009711), Daunorubicin (MESH:D003630), 7-deazaguanine (MESH:C066856), thymine (MESH:D013941), glycan (MESH:D011134), oxygen (MESH:D010100)
- **Species:** Streptomyces (genus) [taxon 1883], Streptococcus thermophilus (species) [taxon 1308], Haloarcula hispanica (species) [taxon 51589], Homo sapiens (human, species) [taxon 9606], Vibrio cholerae (species) [taxon 666], Pseudomonas aeruginosa (species) [taxon 287], Escherichia coli (E. coli, species) [taxon 562]

## Full text

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## Figures

4 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12948488/full.md

## References

141 references — full list in the complete paper: https://tomesphere.com/paper/PMC12948488/full.md

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Source: https://tomesphere.com/paper/PMC12948488