Structure of the O-chain polysaccharide of the phenol-phase soluble lipopolysaccharide of <i>Escherichia coli</i> 0:157:H7

Perry, Malcolm B.; MacLean, Leann L.; Griffith, Douglas W.

doi:10.1139/o86-004

Cited by 115 publications

(95 citation statements)

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“…We suggest that both epitopes are present on the LPS of Y. enterocolitica 09, but only one of these is exposed on the 0-antigen of E. coli 0157. The LPS of both organisms have been shown to contain the same sugar units [8,9]; however, as we have shown here, the physical structure of the two LPS types are quite different. These structural differences might influence the accessibility of antibodies to bind to epitopes on the LPS such that epitopes on the LPS of Y. enterocolitica 09 are more available for antibody binding than the same epitopes on the LPS of E. coli 0157.…”

Section: Elisamentioning

confidence: 53%

“…Chemical analyses of LPS have shown that certain bacteria share common sugar sequences, and strains of Y. enterocolitica, E. coli 0157 and Brucella abortuas have been shown to contain 4-amino-4,6-dideoxy-a-D-mannopyranosyl sugar units [8,9]. This similarity in LPS composition has been used to explain antigenic cross-reactions between Y. enterocolitica 09 and B. abortus, and E. coli 0157 and B. abortus, detected with hyperimmune rabbit sera [10][11][12].…”

Section: Introductionmentioning

confidence: 99%

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The serological relationship betweenYersinia enterocoliticaO9 andEscherichia coliO157 using sera from patients with yersiniosis and haemolytic uraemic syndrome

Chart¹,

Cheasty²,

Cope

et al. 1991

Epidemiol. Infect.

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SUMMARYSera from patients with yersiniosis, shown to contain antibodies to Yersinia enterocolitica 09; and sera from patients with haemolytic uraemic syndrome (HUS) caused by Escherichia coli 0157, were used to investigate serological crossreactions between Y. enterocolitica 09 and E. coli 0157. Lipopolysaceharide (LPS) was isolated from strains of Y. enterocolitica 09 and E. coli 0157 and reacted with sera by immunoblotting and ELISA. Sera from patients with HUS contained antibodies to the LPS of E. coli 0157 only; 80 % of sera from patients with yersiniosis contained antibodies to the LPS of Y. enterocolitica 09 and E. coli 0157. This one-way cross-reaction was also detected using hyperimmune rabbit antisera.

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Section: Elisamentioning

confidence: 53%

Section: Introductionmentioning

confidence: 99%

The serological relationship betweenYersinia enterocoliticaO9 andEscherichia coliO157 using sera from patients with yersiniosis and haemolytic uraemic syndrome

Chart¹,

Cheasty²,

Cope

et al. 1991

Epidemiol. Infect.

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“…This was presumably due to the accumulation of Und-PP-linked O16 antigen precursors that cannot be translocated across the plasma membrane, which may compromise the synthesis of cell wall peptidoglycan. However, viable colonies were obtained after 'vov et al, 1984), O111 (Eklund et al, 1978), O157 (Perry et al, 1986), Sal. enterica LT2 (Hellerqvist et al, 1971), Sh.…”

Section: Resultsmentioning

confidence: 99%

Wzx proteins involved in biosynthesis of O antigen function in association with the first sugar of the O-specific lipopolysaccharide subunit

2004

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One of the most common pathways for the export of O-specific lipopolysaccharide (LPS) across the plasma membrane requires the participation of the Wzx protein. Wzx belongs to a family of integral membrane proteins that share little conservation in their primary amino acid sequence, making it difficult to delineate functional domains. This paper reports the cloning and expression in Escherichia coli K-12 of various Wzx homologues from different bacteria as FLAG epitope-tagged protein fusions. A reconstitution system for O16 LPS synthesis was used to assess the ability of each Wzx protein to complement an E. coli K-12 Dwzx mutant. The results demonstrate that Wzx proteins from O-antigen systems that use N-acetylglucosamine or N-acetylgalactosamine for the initiation of the biosynthesis of the O repeat can fully complement the formation of O16 LPS. Partial complementation was seen with Wzx from Pseudomonas aeruginosa, a system that uses N-acetylfucosamine in the initiation reaction. In contrast, there was negligible complementation with the Wzx protein from Salmonella enterica, a system in which galactose is the initiating sugar. These results support a model whereby the first sugar of the O repeat can be recognized by the O-antigen translocation machinery.

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“…The inactivation of galE affects pilin glycosylation in Neisseria meningitidis C311 number 3. Meningococcal pilin are normally post-translationally modified at Ser 63 by the addition of the Gal␤1,4-Gal␣1,3-Bac trisaccharide (46 -48). In a galE mutant, the pilin were glycosylated with a lone Bac residue (47,48).…”

Section: Discussionmentioning

confidence: 99%

A Single Bifunctional UDP-GlcNAc/Glc 4-Epimerase Supports the Synthesis of Three Cell Surface Glycoconjugates in Campylobacter jejuni

Bernatchez

Szymanski

Ishiyama

et al. 2005

Journal of Biological Chemistry

113

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The major cell-surface carbohydrates (lipooligosaccharide, capsule, and glycoprotein N-linked heptasaccharide) of Campylobacter jejuni NCTC 11168 contain Gal and/or GalNAc residues. GalE is the sole annotated UDP-glucose 4-epimerase in this bacterium. The presence of GalNAc residues in these carbohydrates suggested that GalE might be a UDP-GlcNAc 4-epimerase. GalE was shown to epimerize UDP-Glc and UDP-GlcNAc in coupled assays with C. jejuni glycosyltransferases and in sugar nucleotide epimerization equilibria studies. Thus, GalE possesses UDP-GlcNAc 4-epimerase activity and was renamed Gne. The K m(app) values of a purified MalE-Gne fusion protein for UDP-GlcNAc and UDP-GalNAc are 1087 and 1070 M, whereas those for UDP-Glc and UDP-Gal are 780 and 784 M. The k cat and k cat /K m(app) values were three to four times higher for UDP-GalNAc and UDP-Gal than for UDP-GlcNAc and UDP-Glc. The comparison of the kinetic parameters of MalE-Gne to those of other characterized bacterial UDPGlcNAc 4-epimerases indicated that Gne is a bifunctional UDP-GlcNAc/Glc 4-epimerase. The UDP sugarbinding site of Gne was modeled by using the structure of the UDP-GlcNAc 4-epimerase WbpP from Pseudomonas aeruginosa. Small differences were noted, and these may explain the bifunctional character of the C. jejuni Gne. In a gne mutant of C. jejuni, the lipooligosaccharide was shown by capillary electrophoresis-mass spectrometry to be truncated by at least five sugars. Furthermore, both the glycoprotein N-linked heptasaccharide and capsule were no longer detectable by high resolution magic angle spinning NMR. These data indicate that Gne is the enzyme providing Gal and GalNAc residues with the synthesis of all three cell-surface carbohydrates in C. jejuni NCTC 11168.

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Structure of the O-chain polysaccharide of the phenol-phase soluble lipopolysaccharide of Escherichia coli 0:157:H7

Cited by 115 publications

References 0 publications

The serological relationship betweenYersinia enterocoliticaO9 andEscherichia coliO157 using sera from patients with yersiniosis and haemolytic uraemic syndrome

The serological relationship betweenYersinia enterocoliticaO9 andEscherichia coliO157 using sera from patients with yersiniosis and haemolytic uraemic syndrome

Wzx proteins involved in biosynthesis of O antigen function in association with the first sugar of the O-specific lipopolysaccharide subunit

A Single Bifunctional UDP-GlcNAc/Glc 4-Epimerase Supports the Synthesis of Three Cell Surface Glycoconjugates in Campylobacter jejuni

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