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TitleComplete inhibition of β-tryptase by tetramer dissociation and active site allostery due to a single antibody residue.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateApr 9, 2026
AuthorsHenry R Maun / Caleigh M Azumaya / Benjamin T Walters / Rajesh Vij / Ashley Morando / Kelly M Loyet / James T Koerber / Alexis Rohou / Robert A Lazarus /
PubMed AbstractHuman β-tryptase, a tetrameric trypsin-like serine protease, is an important mediator of inflammatory responses in asthma, allergy and other diseases. Here we report an anti-β-tryptase antibody ...Human β-tryptase, a tetrameric trypsin-like serine protease, is an important mediator of inflammatory responses in asthma, allergy and other diseases. Here we report an anti-β-tryptase antibody with a superior mechanism of action compared to others since it not only inhibits tetrameric β-tryptase, but also completely inhibits monomeric β-tryptase activity. The antibody binds to an exosite that causes tetramer dissociation as either an IgG or Fab and, in addition, allosterically alters the substrate binding cleft on monomers, thus preventing substrate binding and proteolysis. We solve the cryoEM structure of the complex, generate biochemical data and engineer point mutations to elucidate the allosteric path of inhibition. This ultimately reveals a single Asp to Gly mutation in CDR-L3 that only slightly impacts binding affinity, but completely eliminates inhibitory activity. Finally, we improve antibody inhibitory potency up to 4.7-fold by structure-based design creating new charge-charge interactions. This antibody may have enhanced efficacy and potential to assess the relevance of β-tryptase, including monomers, in biological and clinical settings.
External linksNat Commun / PubMed:41957026 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

48419

9mnb

EMDB-48419, PDB-9mnb:
Beta1-tryptase monomer bound to inhibitory Fabs E82.AS and E104.v2
Method: EM (single particle) / Resolution: 3.0 Å

Source
  • homo sapiens (human)
  • lama glama (llama)
KeywordsIMMUNE SYSTEM/Hydrolase / Serine Protease / Inhibitory Antibodies / IMMUNE SYSTEM / IMMUNE SYSTEM-Hydrolase complex

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