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. Author manuscript; available in PMC: 2010 Apr 17.
Published in final edited form as: Cell. 2009 Apr 17;137(2):321–331. doi: 10.1016/j.cell.2009.02.041

Figure 5. Conservation of Protein Glycosylation in the Intestinal Bacteroides.

Figure 5

(A) The lfg region of B. fragilis and the corresponding regions downstream of metG in other intestinal Bacteroides species. Putative glycosyltransferases are hatched. (B) Whole cell lysates of various Bacteroides species separated by SDS-PAGE, blotted and probed with antiserum to the glycan of BF2494. (C) Same as panel B except that the blot was probed with antiserum to BF2494 purified from E. coli, which recognizes the protein component of the molecule. (D) Alignment of segments of BF2494 and its orthologs demonstrating conservation of the glycosylation motif (bolded). The three residues that are glycosylated in B. fragilis (T87, T178 and T231), and its counterparts in the orthologous proteins are underlined. (E) Western blot analysis of whole cell lysates of various Bacteroides species expressing the B. fragilis wild-type BF2494-His protein (WT), or the B. fragilis BF2494-His triple glycosylation site mutant (T87A.T178A.T231A), probed with anti-His-tag.