Oligosaccharide Binding Proteins from Bifidobacterium longum subsp. infantis Reveal a Preference for Host Glycans
2011

Bifidobacterium longum subsp. infantis and Its Preference for Host Glycans

publication 10 minutes Evidence: moderate

Author Information

Author(s): Garrido Daniel, Kim Jae Han, German J. Bruce, Raybould Helen E., Mills David A.

Primary Institution: University of California Davis

Hypothesis

How do the oligosaccharide binding proteins (F1SBPs) in Bifidobacterium longum subsp. infantis interact with host glycans?

Conclusion

The study provides evidence that B. infantis has adapted to the infant gut environment by developing specific binding proteins for host-derived oligosaccharides.

Supporting Evidence

  • B. infantis has a unique set of F1SBPs that bind to various mammalian oligosaccharides.
  • Half of the F1SBPs in B. infantis were found to bind mammalian oligosaccharides.
  • Growth on human milk oligosaccharides induced the expression of specific binding proteins.
  • Some F1SBPs were shown to adhere to intestinal epithelial cells in vitro.

Takeaway

Bifidobacterium infantis can grab onto sugars from human milk and other sources to help it grow in babies' tummies.

Methodology

The study used the Mammalian Glycan Array to analyze the binding affinities of F1SBPs from B. infantis and correlated these with protein expression induced by different prebiotics.

Limitations

The study primarily focuses on in vitro findings, which may not fully represent in vivo conditions.

Digital Object Identifier (DOI)

10.1371/journal.pone.0017315

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