The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Diversification of molecular pattern recognition in bacterial NLR-like proteins
Open accessPreprint — published as 10.1038/s41467-024-54214-0
Abstract
Antiviral STANDs (Avs) are bacterial anti-phage proteins that are evolutionarily related to immune pattern recognition receptors of the NLR family. Following recognition of a conserved phage protein, Avs proteins exhibit cellular toxicity and abort phage propagation by killing the infected cell. Type 2 Avs proteins (Avs2) were suggested to recognize the large terminase subunit of the phage as a signature of phage infection. Here, we show that while Avs2 from Klebsiella pneumoniae (KpAvs2) can be activated when heterologously co-expressed with the terminase of phage SECphi18, during infection in vivo KpAvs2 recognizes a different phage protein, named KpAvs2-stimulating protein 1 (Ksap1). We show that KpAvs2 directly binds Ksap1 to become activated, and that phages mutated in Ksap1 can escape KpAvs2 defense despite encoding an intact terminase. Our results exemplify the evolutionary diversification of molecular pattern recognition in bacterial Avs2 proteins, and highlight that pattern recognition during infection can differ from results obtained using heterologous co-expression assays.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Research works printed but not linked: 48
- 10.1093/intimm/dxp017 · DOI
- 10.1016/j.jaci.2009.12.980 · DOI · Paper page
- 10.1126/science.aaf6395 · DOI
- 2023, Defining the expanding mechanisms of phage-mediated activation of bacterial immunity, Curr. Opin. Microbiol, 74, 102325, 10.1016/j.mib.2023.102325 · DOI
- 10.1016/j.chom.2009.06.007 · DOI
- 10.1016/j.tplants.2017.07.005 · DOI
- 10.1126/science.abm4096 · DOI
- 10.3389/fimmu.2020.625833 · DOI
- 10.1016/j.jmb.2004.08.023 · DOI
- 10.1126/science.aba0372 · DOI
- Daskalov, A. , Dyrka, W. & Saupe, S. J. NLR Function in Fungi as Revealed by the Study of Self/Non-self Recognition Systems. in Genetics and Biotechnology (eds. Benz, J. P. & Schipper, K. ) 123–141 (Springer International Publishing, Cham, 2020). · DOI
- 2023, Bacterial NLR-related proteins protect against phage, Cell, 186, 2410, 10.1016/j.cell.2023.04.015 · DOI
- 10.1016/j.it.2017.04.005 · DOI
- 2023, The NLR gene family: from discovery to present day, Nat. Rev. Immunol, 23, 635, 10.1038/s41577-023-00849-x · DOI
- 10.1016/j.immuni.2008.02.005 · DOI
- 2022, Phages and their satellites encode hotspots of antiviral systems, Cell Host Microbe, 30, 740, 10.1016/j.chom.2022.02.018 · DOI
- 10.1101/2023.05.28.542683 · DOI
- 10.1146/annurev.genet.42.110807.091545 · DOI
- 2020, Protein Sequence Analysis Using the MPI Bioinformatics Toolkit, Curr. Protoc. Bioinforma, 72, e108, 10.1002/cpbi.108 · DOI · Paper page
- 2005, Protein homology detection by HMM-HMM comparison, Bioinforma. Oxf. Engl, 21, 951
- 10.1101/2021.10.04.463034 · DOI · Paper page
- 2023, The IMG/M data management and analysis system v.7: content updates and new features, Nucleic Acids Res, 51, D723, 10.1093/nar/gkac976 · DOI
- 10.1016/j.chom.2022.03.001 · DOI
- 10.1016/j.cell.2023.02.029 · DOI · Paper page
- 2022, Bacteria deplete deoxynucleotides to defend against bacteriophage infection, Nat. Microbiol, 7, 1200, 10.1038/s41564-022-01158-0 · DOI
- 10.1016/j.chom.2016.08.010 · DOI
- 10.org:10.1016/j.cell.2020.09.065 · DOI
- 2021, Prokaryotic viperins produce diverse antiviral molecules, Nature, 589, 120, 10.1038/s41586-020-2762-2 · DOI
- 2022, RING 3.0: fast generation of probabilistic residue interaction networks from structural ensembles, Nucleic Acids Res, 50, W651, 10.1093/nar/gkac365 · DOI
- 10.1038/s41587-023-01773-0 · DOI · Paper page
- 10.1093/NAR/GKAB1061 · DOI · Paper page
- 10.1016/S0968-0004(01)01852-7 · DOI
- 2009, Enumeration of bacteriophages using the small drop plaque assay system, Methods Mol. Biol. Clifton NJ, 501, 81, 10.1007/978-1-60327-164-6_9 · DOI
- 10.1371/journal.pone.0128036 · DOI · Paper page
- 2014, Identification of mutations in laboratory-evolved microbes from next-generation sequencing data using breseq, Methods Mol. Biol. Clifton NJ, 1151, 165, 10.1007/978-1-4939-0554-6_12 · DOI
- 10.1016/0076-6879(93)18045-E · DOI
- 10.1021/acs.jproteome.8b00891 · DOI
- 10.1021/acs.jproteome.7b00608 · DOI
- 2019, Improved Protein Inference from Multiple Protease Bottom-Up Mass Spectrometry Data, J. Proteome Res, 18, 3429, 10.1021/acs.jproteome.9b00330 · DOI
- 10.1093/nar/gkac1040 · DOI
- 10.1093/NAR/GKAB1038 · DOI · Paper page
- 10.1126/SCIENCE.ABJ8432 · DOI
- 10.1093/nar/gkab1112 · DOI · Paper page
- 10.1006/jmbi.1990.9999 · DOI · Paper page
- 2022, Search and sequence analysis tools services from EMBL-EBI in 2022, Nucleic Acids Res, 50, W276, 10.1093/nar/gkac240 · DOI
- 10.1101/gr.849004 · DOI
- 10.1093/nar/18.20.6097 · DOI
- 10.1021/bi00212a001 · DOI
Metadata
- Authors
- Béchon, N., Tal, N., Stokar-Avihail, A., Melamed, S., Amitai, G., & Sorek, R.
- Affiliations
- Weizmann Institute of Science (IL)
- Corresponding author
- Sorek, Rotem
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2024-01-31
- Volume
- 15
- Issue
- 1
- Pages
- 9860-9860
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC11564622
- OpenAlex
- W4404345944
- Cited by
- 23
- References
- 1
- Citations by year
- 2026: 11 · 2025: 9 · 2024: 3
- FWCI
- 6.30
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Nature Communications (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (464312965, SPP2330)
- Israel Science Foundation (MAPATS 2720/22)
- Azrieli Foundation
- Topics
- Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
- Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- Klebsiella pneumoniae, phage defense, receptor activation
- MeSH terms
- NLR Proteins, Bacterial Proteins, Bacteriophages, Klebsiella pneumoniae, Protein Binding, Viral Proteins, Receptors, Pattern Recognition
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review