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Phylum-wide general protein O-glycosylation system of the Bacteroidetes.

Mol Microbiol.. 2013-05;  88(4):772-83
Michael J. Coyne, C. Mark Fletcher, Maria Chatzidaki-Livanis, Gerald Posch, Christina Schaffer, Laurie E. Comstock. Division of Infectious Diseases, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA
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摘要

The human gut symbiont Bacteroides fragilis has a general protein O-glycosylation system in which numerous extracytoplasmic proteins are glycosylated at a three amino acid motif. In B. fragilis, protein glycosylation is a fundamental and essential property as mutants with protein glycosylation defects have impaired growth and are unable to competitively colonize the mammalian intestine. In this study, we analysed the phenotype of B. fragilis mutants with defective protein glycosylation and found that the glycan added to proteins is comprised of a core glycan and an outer glycan. The genetic region encoding proteins for the synthesis of the outer glycan is conserved within a Bacteroides species but... More

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