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Antibodies disrupt bacterial adhesion by ligand mimicry and allosteric interference. | LitMetric

AI Article Synopsis

  • The attachment of microorganisms to host cells via lectins that bind to surface glycans makes lectins potential targets for antimicrobial development.
  • FimH, a key lectin adhesin, changes shape when it binds specific glycans, activating a unique catch-bond mechanism.
  • The study explores how different monoclonal antibodies interact with FimH through various mechanisms, enhancing our understanding of antibody actions and providing insights for creating new antimicrobials.

Article Abstract

A critical step in infections is the attachment of many microorganisms to host cells using lectins that bind surface glycans, making lectins promising antimicrobial targets. Upon binding mannosylated glycans, FimH, the most studied lectin adhesin of type 1 fimbriae in , undergoes an allosteric transition from an inactive to an active conformation that can act as a catch-bond. Monoclonal antibodies that alter FimH glycan binding in various ways are available, but the mechanisms of these antibodies remain unclear. Here, we use cryoEM, mass spectrometry, binding assays, and molecular dynamics simulations to determine the structure-function relationships underlying antibody-FimH binding. Our study reveals four distinct antibody 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 new antimicrobial that target adhesins.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11661100PMC
http://dx.doi.org/10.1101/2024.12.06.627246DOI Listing

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