title: Genetic and functional analysis of the phosphorylcholine moiety of commensal Neisseria lipopolysaccharide.
abstract: Phosphorylcholine (ChoP) is a common surface feature of many mucosal organisms, including Neisseria spp., in which it is present exclusively on pili of pathogenic Neisseria and on the lipopolysaccharide (LPS) of commensal Neisseria (Cn). Its presence in Cn has been confirmed by nuclear magnetic resonance. It appears that choline is the main source for the production of ChoP by Cn. We have sequenced a locus, containing four genes (licA-D) with 47-73% identity to the lic1 locus of Haemophilus influenzae (Hi) and 21-40% identity to lic genes in Streptococcus pneumoniae, involved in the production and incorporation of ChoP. The arrangement of the Cn genes and the presence of CAAT repeats, responsible for phase variation of ChoP expression, resemble Hi and differ from S. pneumoniae. Cn DNA flanking the lic locus contains genes ilvE and NMA2149 with >85% identity to the pathogenic Neisseria genes. However, there are no lic genes in the corresponding location or elsewhere in pathogenic Neisseria. This suggests either the loss of the locus from pathogenic Neisseria or a horizontal transfer of genes to Cn, perhaps from H. influenzae spp. As in Hi, ChoP enhances adherence to and invasion of human epithelial cells via the receptor for platelet-activating factor. However, ChoP expression also increases susceptibility to serum killing mediated by complement and C-reactive protein. Taken together, these observations support the hypothesis that the ability of many organisms to switch off ChoP expression rapidly represents an important adaptation to different environments encountered during the colonization/infection process and that the ChoP moiety apparently synthesized by distinct means in pathogenic and commensal Neisseria represents an advantage in the colonization properties of these bacteria.
authors: Department of Pathology and Microbiology, School of Medical Sciences, University of Bristol, UK. Laura.Serino@bristol.ac.uk
authors: Laura
authors: L
authors: Serino
authors: Mumtaz
authors: M
authors: Virji
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology; D001422:Bacterial Adhesion; D054804:Cathelicidins; D002794:Choline / Q000378:metabolism; D004847:Epithelial Cells / Q000382:microbiology; D005798:Genes, Bacterial; D006193:Haemophilus influenzae; D006801:Humans; D008070:Lipopolysaccharides / Q000096:biosynthesis / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009343:Neisseria / Q000187:drug effects / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D010767:Phosphorylcholine / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
chemical_list: D023181:Antimicrobial Cationic Peptides; D054804:Cathelicidins; D008070:Lipopolysaccharides; D010767:Phosphorylcholine; D002794:Choline