title: Lipoproteins in bacteria: structures and biosynthetic pathways.
abstract: Bacterial lipoproteins are characterized by the presence of a conserved N-terminal lipid-modified cysteine residue that allows the hydrophilic protein to anchor onto bacterial cell membranes. These proteins play important roles in a wide variety of bacterial physiological processes, including virulence, and induce innate immune reactions by functioning as ligands of the mammalian Toll-like receptor 2. We review recent advances in our understanding of bacterial lipoprotein structure, biosynthesis and structure-function relationships between bacterial lipoproteins and Toll-like receptor 2. Notably, 40 years after the first report of the triacyl structure of Braun's lipoprotein in Escherichia coli, recent intensive MS-based analyses have led to the discovery of three new lipidated structures of lipoproteins in monoderm bacteria: the lyso, N-acetyl and peptidyl forms. Moreover, the bacterial lipoprotein structure is considered to be constant in each bacterium; however, lipoprotein structures in Staphylococcus aureus vary between the diacyl and triacyl forms depending on the environmental conditions. Thus, the lipidation state of bacterial lipoproteins, particularly in monoderm bacteria, is more complex than previously assumed.
authors.affiliation: Biomolecular Characterization Team, RIKEN Advanced Science Institute, Wako, Saitama, Japan. knife@riken.jp
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Nakayama
authors.forename: Kenji
authors.initials: K
authors.lastname: Kurokawa
authors.forename: Bok Luel
authors.initials: BL
authors.lastname: Lee
mesh_terms: D001419:Bacteria / Q000235:genetics / Q000378:metabolism*; D006094:Gram-Positive Bacteria / Q000235:genetics / Q000378:metabolism; D008074:Lipoproteins / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D051193:Toll-Like Receptors / Q000235:genetics / Q000378:metabolism
chemical_list: D008074:Lipoproteins; D051193:Toll-Like Receptors