NDLI: Phase-variable expression of a family of glycoproteins imparts a dynamic surface to a symbiont in its human intestinal ecosystem

Content Provider	PubMed Central
Author	Fletcher, C. Mark Coyne, Michael J. Bentley, David L. Villa, Otto F. Comstock, Laurie E.
Copyright Year	2007
Abstract	The recent report of the synthesis of glycoproteins by the abundant intestinal symbionts Bacteroides showed that these organisms use a novel bacterial enzyme to decorate their surfaces with a sugar residue derived from their environment. As a first step in understanding the importance of these glycoproteins to the bacteria and to the bacterial–host symbiosis, we identified and characterized the abundant glycoproteins of Bacteroides distasonis (proposed reclassification as Parabacteroides distasonis) [Sakamoto M, Benno Y (2006) Int J Syst Evol Microbiol 56:1599–1605]. Using lectin-affinity purification followed by tandem mass spectrometry, we identified a family of at least nine glycoproteins, similar only to the S-layer glycoproteins of Tannerella forsythia. Analysis of one of these purified glycoproteins demonstrated that the glycan is primarily a polymer of xylose, a monosaccharide rarely found in bacterial glycans. Even more unexpected was the finding that seven of nine of the glycoprotein promoters undergo DNA inversion, a process that we show is active in their endogenous human environment. Using cross-species functional assays, we show that a single serine family site-specific recombinase globally mediates the inversions of these glycoprotein promoters. This regulatory mechanism is similar to that of the Bacteroides fragilis capsular polysaccharides and establishes DNA inversion as a general and ancient means of regulation of glycan-containing surface molecules of these important human intestinal symbionts.
Related Links	http://dx.doi.org/10.1073/pnas.0608797104
Starting Page	2413
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	104
Language	English
Publisher	National Academy of Sciences
Publisher Date	2007-02-13
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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