Oligosaccharide binding proteins from Bifidobacterium longum subsp. infantis reveal a preference for host glycans.

ABSTRACT: Bifidobacterium longum subsp. infantis (B. infantis) is a common member of the infant intestinal microbiota, and it has been characterized by its foraging capacity for human milk oligosaccharides (HMO). Its genome sequence revealed an overabundance of the Family 1 of solute binding proteins (F1SBPs), part of ABC transporters and associated with the import of oligosaccharides. In this study we have used the Mammalian Glycan Array to determine the specific affinities of these proteins. This was correlated with binding protein expression induced by different prebiotics including HMO. Half of the F1SBPs in B. infantis were determined to bind mammalian oligosaccharides. Their affinities included different blood group structures and mucin oligosaccharides. Related to HMO, other proteins were spe

SUBMITTER: Garrido D 

PROVIDER: S-EPMC3057974 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature