Functional Characterization of Flagellin Glycosylation in Campylobacter jejuni 81-176
| Autor: | Patricia Guerry, Cheryl P. Ewing, Ekaterina Andreishcheva |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Glycosylation
Immunoblotting Mutant Mutagenesis (molecular biology technique) Genetics and Molecular Biology macromolecular substances Flagellum Microbiology Campylobacter jejuni Serine chemistry.chemical_compound Bacterial Proteins Microscopy Electron Transmission Molecular Biology biology biology.organism_classification carbohydrates (lipids) Regulon chemistry Biochemistry Flagella Mutagenesis Site-Directed biology.protein Flagellin |
| Zdroj: | Journal of Bacteriology. 191:7086-7093 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | The major flagellin of Campylobacter jejuni strain 81-176, FlaA, has been shown to be glycosylated at 19 serine or threonine sites, and this glycosylation is required for flagellar filament formation. Some enzymatic components of the glycosylation machinery of C. jejuni 81-176 are localized to the poles of the cell in an FlhF-independent manner. Flagellin glycosylation could be detected in flagellar mutants at multiple levels of the regulatory hierarchy, indicating that glycosylation occurs independently of the flagellar regulon. Mutants were constructed in which each of the 19 serine or threonines that are glycosylated in FlaA was converted to an alanine. Eleven of the 19 mutants displayed no observable phenotype, but the remaining 8 mutants had two distinct phenotypes. Five mutants (mutations S417A, S436A, S440A, S457A, and T481A) were fully motile but defective in autoagglutination (AAG). Three other mutants (mutations S425A, S454A, and S460A) were reduced in motility and synthesized truncated flagellar filaments. The data implicate certain glycans in mediating filament-filament interactions resulting in AAG and other glycans appear to be critical for structural subunit-subunit interactions within the filament. |
| Databáze: | OpenAIRE |
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