Evolution and structural dynamics of bacterial glycan binding adhesins

Area of Science:

• Microbiology
• Structural Biology
• Immunology

Background:

• Bacterial pathogens utilize glycan-binding interactions to achieve host and tissue specificity.
• Bacterial lectins exhibit niche specialization and plasticity in their glycan-binding mechanisms, adapting to host glycome dynamics.

Purpose of the Study:

• To review new structural insights into the host adaptation and dynamics of bacterial carbohydrate-binding adhesins and toxins.
• To highlight the potential of structure-aided drug design for combating glycan-mediated host-pathogen interactions.

Main Methods:

• Review of recent functional and structural studies.
• Analysis of structural data for bacterial adhesins and toxins in key human pathogens.
• Examination of structure-aided drug design strategies.

Main Results:

• Bacterial lectins display remarkable plasticity in glycan-binding sites and mechanisms for host adaptation.
• Structural insights reveal specialized adaptations in pathogens like Escherichia coli, Helicobacter pylori, Yersinia pestis, and Vibrio cholerae.
• Structure-aided drug design is emerging as a viable strategy, with novel anti-adhesive compounds and antibodies being developed.

Conclusions:

• Understanding the structural basis of bacterial glycan recognition is crucial for deciphering host-pathogen dynamics.
• The plasticity of bacterial adhesins and toxins offers therapeutic targets for novel anti-infective strategies.
• Structure-aided design of inhibitors and antibodies holds promise for counteracting glycan-mediated infections.