title: Gram-negative flagella glycosylation.
abstract: Protein glycosylation had been considered as an eccentricity of a few bacteria. However, through advances in analytical methods and genome sequencing, it is now established that bacteria possess both N-linked and O-linked glycosylation pathways. Both glycosylation pathways can modify multiple proteins, flagellins from Archaea and Eubacteria being one of these. Flagella O-glycosylation has been demonstrated in many polar flagellins from Gram-negative bacteria and in only the Gram-positive genera Clostridium and Listeria. Furthermore, O-glycosylation has also been demonstrated in a limited number of lateral flagellins. In this work, we revised the current advances in flagellar glycosylation from Gram-negative bacteria, focusing on the structural diversity of glycans, the O-linked pathway and the biological function of flagella glycosylation.
authors.affiliation: Department of Microbiology, Faculty of Biology, University of Barcelona, Diagonal 643, Barcelona 08071, Spain. smerino@ub.edu.
authors.forename: Susana
authors.initials: S
authors.lastname: Merino
authors.affiliation: Department of Microbiology, Faculty of Biology, University of Barcelona, Diagonal 643, Barcelona 08071, Spain. jtomas@ub.edu.
authors.forename: Juan M
authors.initials: JM
authors.lastname: Tomás
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D005407:Flagella / Q000737:chemistry / Q000378:metabolism*; D005408:Flagellin / Q000737:chemistry / Q000378:metabolism; D006031:Glycosylation; D006090:Gram-Negative Bacteria / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D011134:Polysaccharides; D005408:Flagellin