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Multivalent Thiosialosides and Their Synergistic Interaction with Pathogenic Sialidases.

Yoan Brissonnet1, Coralie Assailly1, Amélie Saumonneau2

  • 1CEISAM, Chimie Et Interdisciplinarité, Synthèse, Analyse, Modélisation, UMR CNRS 6230, UFR des Sciences et des Techniques, Université de Nantes, 2 rue de la Houssinière, BP 92208, 44322, Nantes Cedex 3, France.

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Multivalent thiosialosides effectively inhibit pathogenic sialidases by targeting specific domains. This multivalency strategy significantly enhances inhibitor potency against bacterial and parasitic enzymes.

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enzymesglycoclustersglycosidasesinhibitionsialidases

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Area of Science:

  • Biochemistry
  • Microbiology
  • Glycobiology

Background:

  • Sialidases (SAs) are crucial virulence factors for pathogens, hydrolyzing cell surface glycoconjugates.
  • Sialidase catalytic domains are often enhanced by carbohydrate-binding modules that interact with sialosides.

Purpose of the Study:

  • To design non-hydrolyzable multivalent thiosialosides as probes and inhibitors for key sialidases.
  • To investigate the roles of the lectin (NanA-L) and catalytic (NanA-C) domains of Streptococcus pneumoniae NanA in binding and inhibition.

Main Methods:

  • Synthesis of di- and polymeric thiosialosides as multivalent inhibitors.
  • Truncation of NanA into its lectin (NanA-L) and catalytic (NanA-C) domains.
  • Affinity and inhibition assays using sialylated surfaces and synthetic thiosialosides.

Main Results:

  • The NanA-L domain was identified as the primary driver of NanA binding to sialylated surfaces and compounds, increasing affinity by over 100-fold.
  • Polymeric thiosialosides demonstrated significantly enhanced inhibitory activity against NanA and NanA-C compared to monovalent counterparts.
  • Inhibitory efficiency of polymer-grafted thiosialosides was up to 3000-fold higher than monovalent thiosialosides.

Conclusions:

  • Multivalency is a powerful strategy for designing potent inhibitors of bacterial and parasitic sialidases.
  • The lectin domain plays a critical role in sialidase binding and can be targeted for enhanced inhibition.
  • These findings pave the way for novel therapeutic strategies against sialidase-producing pathogens.