How and when are bacterial flagellins glycosylated? (360G-Wellcome-089550_Z_09_Z)

Post-translational modification of proteins was not thought to occur in bacteria. Recently there have been a number of reports about bacterial protein glycosylation. Interestingly most bacterial glycoproteins are involved in pathogenesis or they are surface exposed/polymeric protein structures such as flagella or pili. Glycosylation appears to be a fundamental aspect of flagellar assembly however it may also serve specific roles in infection and pathogenesis. Nothing is known about when the gly can is transferred onto flagellin during the filament assembly process. We aim to establish whether this occurs before interaction with chaperones or recognises chaperone-subsunit complexes during passage to the export apparatus. We believe this process occurs via the members of the Maf protein family. Therefore we wish to investigate the interaction of this family of proteins with the flagellin or flagellin specific chaperones and determine whether glycosylation is required for entry into the f lagella export pathway or to ensure polymerization of a functional flagellum. Other questions to be investigated include identification of he glycosylation sites and to establish the minimum amount of glycosylation required for filament assembly.