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  • Recent interest in bacterial lectins involved in pathogenesis and host recognition has been accompanied by thermodynamic characterisation that demonstrated much higher affinity than that observed for plant or animal lectins. Cholera and tetanus toxins, as well as lectins from Pseudomonas aeruginosa and Ralstonia solanacearum all display sub-micromolar range affinity towards their carbohydrate ligands. We used combined titration microcalorimetry and x-ray crystallography approaches to decipher the thermodynamical and structural basis for high affinity binding of bacterial lectins to host carbohydrates.
  • Recent interest in bacterial lectins involved in pathogenesis and host recognition has been accompanied by thermodynamic characterisation that demonstrated much higher affinity than that observed for plant or animal lectins. Cholera and tetanus toxins, as well as lectins from Pseudomonas aeruginosa and Ralstonia solanacearum all display sub-micromolar range affinity towards their carbohydrate ligands. We used combined titration microcalorimetry and x-ray crystallography approaches to decipher the thermodynamical and structural basis for high affinity binding of bacterial lectins to host carbohydrates. (en)
Title
  • Thermodynamics of interaction between bacterial lectins and host carbohydrates
  • Thermodynamics of interaction between bacterial lectins and host carbohydrates (en)
skos:prefLabel
  • Thermodynamics of interaction between bacterial lectins and host carbohydrates
  • Thermodynamics of interaction between bacterial lectins and host carbohydrates (en)
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  • RIV/00216224:14310/06:00017389!RIV10-MSM-14310___
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  • P(LC06030), Z(MSM0021622413)
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  • 503795
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  • RIV/00216224:14310/06:00017389
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  • lectin; microcalorimetry; X-ray; pathogen (en)
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  • [C6650B11AD2B]
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  • Brno
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  • Brno
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  • X. Pracovní setkání biochemiků a molekulárních biologů
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  • Imberty, Anne
  • Wimmerová, Michaela
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  • Masarykova univerzita
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  • 80-210-3942-6
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  • 14310
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