Journal
JOURNAL OF BACTERIOLOGY
Volume 186, Issue 9, Pages 2523-2531Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.186.9.2523-2531.2004
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Funding
- NIAID NIH HHS [R01 AI 47852, R01 AI047852] Funding Source: Medline
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Type a flagellins from two strains of Pseudomonas aeruginosa, strains PAK and JJ692, were found to be glycosylated with unique glycan structures. In both cases, two sites of O-linked glycosylation were identified on each monomer, and these sites were localized to the central, surface-exposed domain of the monomer in the assembled filament. The PAK flagellin was modified with a heterogeneous glycan comprising up to 11 monosaccharide units that were O linked through a rhamnose residue to the protein backbone. The flagellin of JJ692 was less complex and had a single rhamnose substitution at each site. The role of the glycosylation island gene cluster in the production of each of these glycosyl moieties was investigated. These studies revealed that the orfA and orfN genes were required for attachment of the heterologous glycan and the proximal rhamnose residue, respectively.
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