N-glycans from human milk glycoproteins are selectively released by an infant gut symbiont in vivo. (October 2019)

• Record Type: Journal Article
• Authors: Karav, Sercan; Casaburi, Giorgio; Arslan, Aysenur; Kaplan, Merve; Sucu, Berfin; Frese, Steven
• Is Part Of: Journal of functional foods. Volume 61(2019)
• Publication Date: 2019-10
• Subjects: Probiotic -- Microbiome -- Human milk -- Glycoproteins -- Milk -- Bifidobacterium infantis; Functional foods -- Analysis -- Periodicals; Food -- Biotechnology -- Periodicals; Nutrition -- Periodicals; 613.2
• DOI: 10.1016/j.jff.2019.103485
• Languages: English
• ISSNs: 1756-4646

Abstract

Graphical abstract: Highlights: EndoBI-1, an endo-β-N-acetylglucosaminidase, is an enzyme unique to B. infantis. This enzyme cleaves the chitobiose core of N- glycans bound to glycoproteins. EndoBI-1 is active in vivo and releases N -glycan from human milk glycoproteins. These N- glycans are selectively utilized by B. infantis. Abstract: Complex, indigestible free oligosaccharides as well as conjugated glycans are found in milk that shape the gut microbiome of infants. The activity of an endo-β- N -acetylglucosaminidase from B. longum subsp. infantis ( B. infantis ) is known to release N -glycans from native milk glycoproteins under physiological conditions. We investigated whether this enzyme is active in vivo in breastfed infants fed B. infantis EVC001. Using mass spectrometry, we found 19 N -glycans related to human milk glycoproteins increased in abundance, similar to previous work using bovine milk glycoproteins, and these 19 N -glycans matched unique specificities of this enzyme. Twenty N -glycans were unique to infants fed B. infantis EVC001. Bifidobacteriaceae were correlated with these glycans, confirming the relationship between B. infantis and released N -glycans. This suggests that this enzyme is active in vivo and releases N -glycans from milk glycoproteins, and may play a role in B. infantis EVC001 colonization of the gut microbiome.