The neuA/flmD gene cluster of Helicobacter pylori is involved in flagellar biosynthesis and flagellin glycosylation

被引:66
作者
Josenhans, C
Vossebein, L
Friedrich, S
Suerbaum, S
机构
[1] Univ Wurzburg, Inst Hyg & Mikrobiol, D-97080 Wurzburg, Germany
[2] Ruhr Univ Bochum, Abt Med Mikrobiol, D-44780 Bochum, Germany
关键词
flagellum; flagellin; protein glycosylation; type III secretion system; polysaccharide synthesis; RpoN; Helicobacter pylori;
D O I
10.1016/S0378-1097(02)00638-9
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Helicobacter pylori possesses a gene (HP0326/JHP309) homologous to neuA of other bacteria, encoding a cytidyl monophosphate-N-acetylneuraminic acid synthetase-homologous enzyme in its N-terminal portion. We analysed the function of this gene, which is controlled by a flagellar class 2sigma(54) promoter, in flagellar biosynthesis. HP0326/JHP309 actually represents a bicistronic operon consisting of a neuA and a flmD-like putative glycosyl transferase gene. An isogenic flmD mutant synthesized basal bodies but no filaments, was non-motile, and expressed severely reduced amounts of a FlaA flagellin of reduced molecular mass. FlaA flagellin was found to be glycosylated in its exported form within the flagellar filament, but not inside the cytoplasm. Glycosylated FlaA was not detectable in the flmD mutant. Together with other genes in the H. pylori genome, a proposed function of the neuA/flmD gene products could be to provide a pathway for glycosylation of flagellin and other extracytoplasmic molecules during type III secretion. (C) 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:165 / 172
页数:8
相关论文
共 32 条
[1]   Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori [J].
Alm, RA ;
Ling, LSL ;
Moir, DT ;
King, BL ;
Brown, ED ;
Doig, PC ;
Smith, DR ;
Noonan, B ;
Guild, BC ;
deJonge, BL ;
Carmel, G ;
Tummino, PJ ;
Caruso, A ;
Uria-Nickelsen, M ;
Mills, DM ;
Ives, C ;
Gibson, R ;
Merberg, D ;
Mills, SD ;
Jiang, Q ;
Taylor, DE ;
Vovis, GF ;
Trost, TJ .
NATURE, 1999, 397 (6715) :176-180
[2]   NUCLEOTIDE-SEQUENCE AND GENETIC-ANALYSIS OF THE NEUD AND NEUB GENES IN REGION-2 OF THE POLYSIALIC ACID GENE-CLUSTER OF ESCHERICHIA-COLI-K1 [J].
ANNUNZIATO, PW ;
WRIGHT, LF ;
VANN, WF ;
SILVER, RP .
JOURNAL OF BACTERIOLOGY, 1995, 177 (02) :312-319
[3]   A genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation [J].
Arora, SK ;
Bangera, M ;
Lory, S ;
Ramphal, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (16) :9342-9347
[4]   Flagellin polymerisation control by a cytosolic export chaperone [J].
Auvray, F ;
Thomas, J ;
Fraser, GM ;
Hughes, C .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 308 (02) :221-229
[5]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[6]   Cloning and comparison of fliC genes and identification of glycosylation in the flagellin of Pseudomonas aeruginosa a-type strains [J].
Brimer, CD ;
Montie, TC .
JOURNAL OF BACTERIOLOGY, 1998, 180 (12) :3209-3217
[7]   Characterization of a post-translational modification of Campylobacter flagellin: Identification of a sero-specific glycosyl moiety [J].
Doig, P ;
Kinsella, N ;
Guerry, P ;
Trust, TJ .
MOLECULAR MICROBIOLOGY, 1996, 19 (02) :379-387
[8]   MOLECULAR ANALYSIS OF THE BIOSYNTHESIS PATHWAY OF THE ALPHA-2,8 POLYSIALIC ACID CAPSULE BY NEISSERIA-MENINGITIDIS SEROGROUP-B [J].
EDWARDS, U ;
MULLER, A ;
HAMMERSCHMIDT, S ;
GERARDYSCHAHN, R ;
FROSCH, M .
MOLECULAR MICROBIOLOGY, 1994, 14 (01) :141-149
[9]   CONSTRUCTION OF ISOGENIC UREASE-NEGATIVE MUTANTS OF HELICOBACTER-PYLORI BY ALLELIC EXCHANGE [J].
FERRERO, RL ;
CUSSAC, V ;
COURCOUX, P ;
LABIGNE, A .
JOURNAL OF BACTERIOLOGY, 1992, 174 (13) :4212-4217
[10]   ULTRASTRUCTURE AND BIOCHEMICAL-STUDIES OF THE FLAGELLAR SHEATH OF HELICOBACTER-PYLORI [J].
GEIS, G ;
SUERBAUM, S ;
FORSTHOFF, B ;
LEYING, H ;
OPFERKUCH, W .
JOURNAL OF MEDICAL MICROBIOLOGY, 1993, 38 (05) :371-377