Evidence map›Paper›PMID 39543107›Full record

ArticleNature communications2024

Diversification of molecular pattern recognition in bacterial NLR-like proteins.

Nathalie Béchon, Nitzan Tal, Avigail Stokar-Avihail, Alon Savidor, Meital Kupervaser, Sarah Melamed, Gil Amitai, Rotem Sorek

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. How bacterial immune systems sense phage infection.Nature reviews. Microbiology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Unlocking genome engineering inMicrobiology spectrum · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. A Gifsy prophage-encoded protein confers broad phage resistance inApplied and environmental microbiology · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Nathalie BéchonDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-0838-7946
Nitzan TalDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.
Avigail Stokar-AvihailDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-2869-5401
Alon Savidorde Botton Institute for Protein Profiling, The Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot, Israel.
Meital Kupervaserde Botton Institute for Protein Profiling, The Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-1068-937X
Sarah MelamedDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.
Gil AmitaiDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-2954-2503
Rotem SorekDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel. rotem.sorek@weizmann.ac.il.ORCID 0000-0002-3872-4982

Funding

Azrieli Foundation postdoctoral fellowshipDeutsche Forschungsgemeinschaft (German Research Foundation) SPP 2330, Grant 464312965Israel Science Foundation (ISF) MAPATS 2720/22
6 · The paper itself

Abstract

Antiviral STANDs (Avs) are bacterial anti-phage proteins evolutionarily related to immune pattern recognition receptors of the NLR family. Type 2 Avs proteins (Avs2) were suggested to recognize the phage large terminase subunit as a signature of phage infection. Here, we show that Avs2 from Klebsiella pneumoniae (KpAvs2) can recognize several different phage proteins as signature for infection. While KpAvs2 recognizes the large terminase subunit of Seuratvirus phages, we find that to protect against Dhillonvirus phages, KpAvs2 recognizes a different phage protein named KpAvs2-stimulating protein 1 (Ksap1). KpAvs2 directly binds Ksap1 to become activated, and phages mutated in Ksap1 escape KpAvs2 defense despite encoding an intact terminase. We further show that KpAvs2 protects against a third group of phages by recognizing another protein, Ksap2. Our results exemplify the evolutionary diversification of molecular pattern recognition in bacterial Avs2, and show that a single pattern recognition receptor evolved to recognize different phage-encoded proteins.

Indexed as

Bacterial ProteinsBacteriophagesKlebsiella pneumoniaeNLR ProteinsReceptors, Pattern RecognitionProtein BindingViral ProteinsBacterial ProteinsNLR ProteinsReceptors, Pattern RecognitionViral Proteins

Identifiers

PMID39543107
PMCPMC11564622

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.