Aeromonas hydrophila flagella glycosylation: involvement of a lipid carrier
Autor: | Merino Montero, Susana, Fulton, Kelly M., Twine, S.M., Wilhelms, Markus, Molero Andrade, Raquel, Tomàs Magaña, Juan |
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Přispěvatelé: | Universitat de Barcelona |
Jazyk: | angličtina |
Rok vydání: | 2014 |
Předmět: |
Bacterial Diseases
Motilitat cel·lular Acetylgalactosamine polymerase chain reaction Glycobiology Gene Expression lcsh:Medicine DNA fragmentation Cell motility Biochemistry flagellin Bacteris protein purification Carbohydrate Conformation Gram Negative lcsh:Science Immune Response Enzyme Classes lipopolysaccharide Enzymes Bacterial Pathogens Aeromonas hydrophila Infectious Diseases Carbohydrate Sequence Medical Microbiology Flagella sequence alignment Bacteris patògens microscopy Medicine lipids (amino acids peptides and proteins) Research Article glycosylation Immunology Molecular Sequence Data Biophysics cell motility ubiquitination Microbiology protein modification epimerization plasmid bacterium isolation tandem mass spectrometry Regulació genètica Amino Acid Sequence enzyme specificity Biology Genetic regulation Bacteria ferredoxin nitrite reductase lcsh:R Glycosyltransferases Bacteriology molecular weight nucleotide sequence Flagellar Motility bacterial strain Lipid Metabolism carbohydrates (lipids) protein analysis Pathogenic bacteria bacteria lcsh:Q Glycolipids biosynthesis molecular model Bacterial Biofilms Carrier Proteins Protein Processing Post-Translational |
Zdroj: | PLoS ONE, Vol 9, Iss 2, p e89630 (2014) PLoS ONE Dipòsit Digital de la UB Universidad de Barcelona Recercat. Dipósit de la Recerca de Catalunya instname |
Popis: | Polar flagellin proteins from Aeromonas hydrophila strain AH-3 (serotype O34) were found to be O-glycosylated with a heterogeneous glycan. Mutants unable to produce WecP or Gne enzymes showed altered motility, and the study of their polar flagellin glycosylation showed that the patterns of glycosylation differed from that observed with wild type polar flagellin. This suggested the involvement of a lipid carrier in glycosylation. A gene coding for an enzyme linking sugar to a lipid carrier was identified in strain AH-3 (WecX) and subsequent mutation abolished completely motility, flagella production by EM, and flagellin glycosylation. This is the first report of a lipid carrier involved in flagella O-glycosylation. A molecular model has been proposed. The results obtained suggested that the N -acetylhexosamines are N-acetylgalactosamines and that the heptasaccharide is completely independent of the O34-antigen lipopolysaccharide. Furthermore, by comparing the mutants with differing degrees of polar flagellin glycosylation, we established their importance in A. hydrophila flagella formation and motility. |
Databáze: | OpenAIRE |
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