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O'Riordan, N,O'Callaghan, J,Butto, LF,Kilcoyne, M,Joshi, L,Hickey, RM
2018
August
Journal Of Dairy Science
Bovine glycomacropeptide promotes the growth of Bifidobacterium longum ssp infantis and modulates its gene expression
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glycomacropeptide Bifidobacterium bovine milk transcription KAPPA-CASEIN GLYCOMACROPEPTIDE HUMAN-MILK OLIGOSACCHARIDES SUBSP INFANTIS CHEMICAL-STRUCTURE ESCHERICHIA-COLI COLOSTRUM PROTEIN CASEINOMACROPEPTIDE CONSUMPTION LACTOFERRIN
101
6730
6741
Bovine milk glycomacropeptide (GMP) is derived from kappa-casein, with exclusively o-linked glycosylation. Glycomacropeptide promoted the growth of Bifidobacterium longum ssp. infantis in a concentration-dependent manner, and this activity was lost following periodate treatment of the GMP (GMP-P), which disables biological recognition of the conjugated oligosaccharides. Transcriptional analysis of B. longum ssp. infantis following exposure to GMP revealed a substantial response to GMP relative to bacteria treated with GMP-P, with a greater number of differentially expressed transcripts and larger fold changes versus the control. Therefore, stimulation of B. longum ssp. infantis growth by GMP is intrinsically linked to the peptide's O-linked glycosylation. The pool of differentially expressed transcripts included 2 glycoside hydrolase (family 25) genes, which were substantially upregulated following exposure to GMP, but not GMP-P. These GH25 genes were present in duplicated genomic islands that also contained genes encoding fibronectin type III binding domain proteins and numerous phage-related proteins, all of which were also upregulated. Homologs of this genomic arrangement were present in other Bifidobacterium species, which suggest it may be a conserved domain for the utilization of glycosylated peptides. This study provides insights into the molecular basis for the prebiotic effect of bovine milk GMP on B. longum ssp. infantis.
10.3168/jds.2018-14499
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