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TitleProkaryotic innate immunity through pattern recognition of conserved viral proteins.
Journal, issue, pagesScience, Vol. 377, Issue 6607, Page eabm4096, Year 2022
Publish dateAug 12, 2022
AuthorsLinyi Alex Gao / Max E Wilkinson / Jonathan Strecker / Kira S Makarova / Rhiannon K Macrae / Eugene V Koonin / Feng Zhang /
PubMed AbstractMany organisms have evolved specialized immune pattern-recognition receptors, including nucleotide-binding oligomerization domain-like receptors (NLRs) of the STAND superfamily that are ubiquitous in ...Many organisms have evolved specialized immune pattern-recognition receptors, including nucleotide-binding oligomerization domain-like receptors (NLRs) of the STAND superfamily that are ubiquitous in plants, animals, and fungi. Although the roles of NLRs in eukaryotic immunity are well established, it is unknown whether prokaryotes use similar defense mechanisms. Here, we show that antiviral STAND (Avs) homologs in bacteria and archaea detect hallmark viral proteins, triggering Avs tetramerization and the activation of diverse N-terminal effector domains, including DNA endonucleases, to abrogate infection. Cryo-electron microscopy reveals that Avs sensor domains recognize conserved folds, active-site residues, and enzyme ligands, allowing a single Avs receptor to detect a wide variety of viruses. These findings extend the paradigm of pattern recognition of pathogen-specific proteins across all three domains of life.
External linksScience / PubMed:35951700 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.48 Å
Structure data

27421

8dgc

EMDB-27421: Avs3 bound to phage PhiV-1 terminase, C2 refinement of Cap4 nuclease domain
PDB-8dgc: Avs3 bound to phage PhiV-1 terminase
Method: EM (single particle) / Resolution: 3.4 Å

27422

8dgf

EMDB-27422: Avs4 bound to phage PhiV-1 portal, C2 refinement of Mrr nuclease domain
PDB-8dgf: Avs4 bound to phage PhiV-1 portal
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-27424: Avs3 bound to PhiV-1 terminase, symmetry-expanded C1 refinement of TPR-terminase domain
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-27425: Avs4 bound to phage PhiV-1 portal, overall C2 reconstruction
Method: EM (single particle) / Resolution: 3.48 Å

EMDB-27426: Avs4 bound to phage PhiV-1 portal, symmetry-expanded C1 refinement of TPR-portal domain
Method: EM (single particle) / Resolution: 3.05 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • salmonella enterica (bacteria)
  • escherichia phage phiv-1 (virus)
  • escherichia coli (E. coli)
KeywordsANTIVIRAL PROTEIN / phage defense / pattern-recognition receptor / nlr / stand / atpase

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