Enhancing the receptor affinity of the sialic acid-binding domain of Vibrio cholerae sialidase through multivalency.

ABSTRACT: Many glycoside hydrolases possess carbohydrate-binding modules (CBMs) that help target these enzymes to appropriate substrates and increase their catalytic efficiency. The Vibrio cholerae sialidase contains two CBMs, one of which is designated as a family CBM40 module and has been shown through structural and calorimetry studies to recognize the alpha-anomer of sialic acid with a KD of approximately 30 microM at 37 degrees C. The affinity of this V. cholerae CBM40 module for sialic acid is one of the highest reported for recognition of a monosaccharide by a CBM. As Nature often increases a weak substrate affinity through multivalency, we have explored the potential of developing reagents with an increased affinity for sialic acid receptors through linking CBM40 modules together. The V. cho

SUBMITTER: Connaris H 

PROVIDER: S-EPMC2652270 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature