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Structure paper

TitleAntibodies disrupt bacterial adhesion by ligand mimicry and allosteric interference.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 10590, Year 2025
Publish dateNov 26, 2025
AuthorsKelli L Hvorecny / Gianluca Interlandi / Tim S Veth / Pavel Aprikian / Anna Manchenko / Veronika L Tchesnokova / Miles S Dickinson / Joel D Quispe / Nicholas M Riley / Rachel E Klevit / Pearl Magala / Evgeni V Sokurenko / Justin M Kollman /
PubMed AbstractA critical step in infections is the attachment of microorganisms to host cells using lectins that bind glycans, making lectins promising antimicrobial targets. Upon binding mannosylated glycans, ...A critical step in infections is the attachment of microorganisms to host cells using lectins that bind glycans, making lectins promising antimicrobial targets. Upon binding mannosylated glycans, FimH, an adhesin in E. coli, undergoes an allosteric transition from an inactive to an active conformation that can act as a catch-bond. Distinct monoclonal antibodies that alter FimH glycan binding are available, but the mechanisms of action remain unclear. Here, we use cryo-electron microscopy, mass spectrometry, adhesion assays, and molecular dynamics simulations to determine the structure-function relationships underlying antibody-FimH binding. Our study demonstrates four mechanisms of action: ligand mimicry by an N-linked, high-mannose glycan; stabilization of the ligand pocket in the inactive state; conformational trapping of the active and inactive states; and locking of the ligand pocket through long-range allosteric effects. These structures reveal multiple mechanisms of antibody responses to an allosteric protein and provide blueprints for antimicrobials that target adhesins.
External linksNat Commun / PubMed:41298446 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 5.8 Å
Structure data

48183

9me4

EMDB-48183, PDB-9me4:
Antibody fragments from mAb475 and mAb824 bound to the adhesin protein FimH
Method: EM (single particle) / Resolution: 3.2 Å

48184

9me5

EMDB-48184, PDB-9me5:
Antibody fragments from mAb824 and mAb926 bound to the adhesin protein FimH
Method: EM (single particle) / Resolution: 3.1 Å

48185

9me6

EMDB-48185, PDB-9me6:
Antibody fragments from mAb21, mAb475, and mAb824 bound to the adhesin protein FimH
Method: EM (single particle) / Resolution: 3.2 Å

48186

9me7

EMDB-48186, PDB-9me7:
Antibody fragments from mAb21 and mAb824 bound to the adhesin protein FimH containing alpha-methyl mannose
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-48187: Antibody fragments from mAb21 and mAb475 bound to the fimbrial tip protein, FimH
Method: EM (single particle) / Resolution: 5.8 Å

71842

9ptm

EMDB-71842, PDB-9ptm:
Antibody fragment from mAb824 bound to the adhesin protein FimH.
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-MMA:
methyl alpha-D-mannopyranoside

Source
  • escherichia coli (E. coli)
  • mus musculus (house mouse)
  • escherichia coli k-12 (bacteria)
KeywordsCELL ADHESION/IMMUNE SYSTEM / Fimbrial tip / Lectin domain / Antibody fragments / Antibody-target complex / CELL ADHESION / CELL ADHESION-IMMUNE SYSTEM complex

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