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TitleThe antiphage mechanism of a widespread trypsin-MBL defense module.
Journal, issue, pagesNat Chem Biol, Year 2026
Publish dateJun 4, 2026
AuthorsPingping Huang / Jingxian Liu / Lijie Guo / Dongyang Xu / Lingbo Shen / Purui Yan / Chen Tong / Wenying Fei / Mengjun Cheng / Zhaoxing Li / Meiling Lu / Lei Zhang / Nannan Wu / Lian-Wen Qi / Yibei Xiao / Meirong Chen /
PubMed AbstractProtease-mediated activation of immune effectors is an evolutionarily conserved mechanism. This study identifies a widespread trypsin-MBL (metallo-β-lactamase) module as a core effector in diverse ...Protease-mediated activation of immune effectors is an evolutionarily conserved mechanism. This study identifies a widespread trypsin-MBL (metallo-β-lactamase) module as a core effector in diverse antiviral bacterial immune systems, such as Hachiman, AVAST and Argonaute. Focusing on the Hachiman-associated trypsin-MBL system, we show that trypsin•HamAB protease activity is inhibited by ATP, while MBL is an autoinhibited DNase with two insertion loops obstructing its catalytic site. Upon infection, trypsin•HamAB senses foreign DNA and hydrolyzes ATP, activating trypsin-like activity, which specifically cleaves MBL at the insertion loops to release repression. The activated MBL depletes DNA and arrests host cell growth. Cryo-electron microscopy structures of trypsin•HamAB-DNA reveal that DNA binding and ATP hydrolysis trigger HamAB oligomerization and trypsin-like domain release, enabling its activation. Our work elucidates a conserved immune mechanism wherein proteolytic activation of a nuclease enables robust immunity against phage while multilayered controls prevent self-toxicity, expanding the repertoire of immune processes governed by regulatory proteolysis.
External linksNat Chem Biol / PubMed:42243536
MethodsEM (single particle)
Resolution3.22 - 3.5 Å
Structure data

65964

9wh1

EMDB-65964, PDB-9wh1:
Structure of Klebsiella pneumoniae trypsin-HamAB bound with DNA, monomer
Method: EM (single particle) / Resolution: 3.23 Å

65968

9whk

EMDB-65968, PDB-9whk:
Structure of Klebsiella pneumoniae trypsin-HamAB bound with DNA, dimer
Method: EM (single particle) / Resolution: 3.22 Å

65977

9whu

EMDB-65977, PDB-9whu:
Structure of Klebsiella pneumoniae trypsin-HamAB bound with DNA, trimer
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • klebsiella pneumoniae (bacteria)
KeywordsDNA BINDING PROTEIN/DNA / ATPase / Helicase / DNA BINDING PROTEIN-DNA complex

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