Bacterial glycosidases acting on red blood cells

Abstract

Glycosidases represent the major catalytic machinery for the breakage of glycosidic bonds. A classification system for glycosyl hydrolases, based on sequence similarity, is available on the dedicated carbohydrate‐active enzymes (CAZy) database and has led to the definition of more than 130 different families (1). Among them, two families of bacterial glycosyl hydrolases, identified by a combination of screening and bioinformatics approaches, perform efficiently and specifically in conversion of red blood cells for the production of universal red blood cells (2,3). Most of the enzymes are found in symbiotic or soil‐borne bacteria. Because members of one family have essentially identical kinetic properties with both branched and linear substrates, they can also act in the enzymatic removal of immunodominant alpha3Gal xenotransplantation epitope (3). We will describe the molecular determinants responsible for the fine substrate specificity of these enzymes and emphasize the potential biomedical applications in remodeling glycan structures.Support or Funding InformationSupported by the CNRS and DGA