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Diversification of molecular pattern recognition in bacterial NLR-like proteins

Author

Listed:
  • Nathalie Béchon

    (Weizmann Institute of Science)

  • Nitzan Tal

    (Weizmann Institute of Science)

  • Avigail Stokar-Avihail

    (Weizmann Institute of Science)

  • Alon Savidor

    (Weizmann Institute of Science)

  • Meital Kupervaser

    (Weizmann Institute of Science)

  • Sarah Melamed

    (Weizmann Institute of Science)

  • Gil Amitai

    (Weizmann Institute of Science)

  • Rotem Sorek

    (Weizmann Institute of Science)

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.

Suggested Citation

  • Nathalie Béchon & Nitzan Tal & Avigail Stokar-Avihail & Alon Savidor & Meital Kupervaser & Sarah Melamed & Gil Amitai & Rotem Sorek, 2024. "Diversification of molecular pattern recognition in bacterial NLR-like proteins," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54214-0
    DOI: 10.1038/s41467-024-54214-0
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    References listed on IDEAS

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    2. Josh Abramson & Jonas Adler & Jack Dunger & Richard Evans & Tim Green & Alexander Pritzel & Olaf Ronneberger & Lindsay Willmore & Andrew J. Ballard & Joshua Bambrick & Sebastian W. Bodenstein & David , 2024. "Accurate structure prediction of biomolecular interactions with AlphaFold 3," Nature, Nature, vol. 630(8016), pages 493-500, June.
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    4. Aude Bernheim & Adi Millman & Gal Ofir & Gilad Meitav & Carmel Avraham & Helena Shomar & Masha M. Rosenberg & Nir Tal & Sarah Melamed & Gil Amitai & Rotem Sorek, 2021. "Prokaryotic viperins produce diverse antiviral molecules," Nature, Nature, vol. 589(7840), pages 120-124, January.
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