Localization of enterobacterial common antigen in Yersinia enterocolitica by the immunoferritin technique

Acker, Georg; Knapp, W.; Wartenberg, Klaus; Mayer, Hubert

doi:10.1128/jb.147.2.602-611.1981

Cited by 26 publications

(5 citation statements)

References 20 publications

(12 reference statements)

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“…Therefore, it is assumed that Ospecific chains cover ECA in Ye 75S cells cultivated at 22 ° C, but to a much lesser extent in the 40 ° C culture when a high amount of rough LPS is present. Correspondingly, a much higher label density is found in an (incomplete) R mutant (Ye 75R) of this strain [49].…”

Section: Localization Of Eca In the Bacte-rial Cellmentioning

confidence: 76%

“…Earlier studies on the LPS of this strain showed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), that the number of (Ounsubstituted R-core stubs is drastically increasing when cells are grown at higher temperatures [48]. With regard to ECA, a definite label is visible in electron microscopy with Yersinia enterocolitica (Ye 75S) grown at a high temperature (40 o C) but no ferritin label at all is observed with cells grown at 22°C [49]. Therefore, it is assumed that Ospecific chains cover ECA in Ye 75S cells cultivated at 22 ° C, but to a much lesser extent in the 40 ° C culture when a high amount of rough LPS is present.…”

Section: Localization Of Eca In the Bacte-rial Cellmentioning

confidence: 94%

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ECA, the enterobacterial common antigen

Kuhn¹,

Meier-Dieter²,

Mayer³

1988

FEMS Microbiology Letters

171

186

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Enterobacterial common antigen (ECA) is a family‐specific surface antigen shared by all members of the Enterobacteriaceae and is restricted to this family. It is found in freshly isolated wild‐type strains as well as in laboratory strains like Escherichia coli K‐12. The family specificity of ECA can be used for taxonomic and diagnostic purposes. ECA is located in the outer leaflet of the outer membrane. It is a glycophospholipid built up by an aminosugar heteropolymer linked to an l‐glycerophosphatidyl residue. In a few rough mutants, in addition, the sugar chain can be bound to the complete lipopolysaccharide (LPS) core. Recently, for Shigella sonnei a lipid‐free cyclic form of ECA was reported. The genetical determination of ECA is closely related to that of lipopolysaccharide. For biosynthesis of ECA and LPS partly the same sugar precursors and the same carrier lipid is used.

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Section: Localization Of Eca In the Bacte-rial Cellmentioning

confidence: 76%

Section: Localization Of Eca In the Bacte-rial Cellmentioning

confidence: 94%

ECA, the enterobacterial common antigen

Kuhn¹,

Meier-Dieter²,

Mayer³

1988

FEMS Microbiology Letters

171

186

View full text Add to dashboard Cite

show abstract

“…Recently, the chemical structure of the inner core polysaccharide composed of seven sugar residues was determined (Radziejewska-Lebrecht et aL, 1994) and preliminary structural analysis showed that there are six sugar residues in the outer core (J. Radziejewska-Lebrecht, M. Skurnik, A. S. Shashkov, and H. Mayer, unpublished). The expression of the hornopolymeric O-antigen is temperature regulated such that the number of repeating units per LPS molecule is higher when bacteria are grown at 22°C (Acker et aL, 1981;AI-Hendy et al, 1991b;Kawaoka et al, 1983;Wartenberg et aL, 1983). Acker and co-workers (Acker et al, 1981) demonstrated that the enterobacterial common antigen (ECA) of Y. enterocolitica serotype 0:3 strain was sterically blocked by abundant O-antigen from ECA-specific antibody molecules in bacteria grown at 22°C but not in bacteria grown at 37°C.…”

Section: Discussionmentioning

confidence: 99%

“…The expression of the hornopolymeric O-antigen is temperature regulated such that the number of repeating units per LPS molecule is higher when bacteria are grown at 22°C (Acker et aL, 1981;AI-Hendy et al, 1991b;Kawaoka et al, 1983;Wartenberg et aL, 1983). Acker and co-workers (Acker et al, 1981) demonstrated that the enterobacterial common antigen (ECA) of Y. enterocolitica serotype 0:3 strain was sterically blocked by abundant O-antigen from ECA-specific antibody molecules in bacteria grown at 22°C but not in bacteria grown at 37°C. For a number of years we have conducted studies on the genetics of the lipopolysaccharide biosynthesis and regulation of Y. enterocolitica (AI-Hendy et al, 1991a,b;Skurnik and Toivanen, 1993;Zhang et aL, 1993) and, during these studies, became interested in the temperature regulation of the O-antigen.…”

Section: Discussionmentioning

confidence: 99%

A novel locus of Yersinia enterocolitica serotype O:3 involved in lipopolysaccharide outer core biosynthesis

Skurnik

Venho

Toivanen

et al. 1995

Molecular Microbiology

126

169

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Yersinia enterocolitica serotype O:3 strain 6471/76-c (YeO3-c) was sensitive to bacteriophage phi R1-37 when grown at 37 degrees C but not when grown at 22 degrees C because of steric hindrance by abundant lipopolysaccharide (LPS) O-side chain (O-antigen) expressed at 22 degrees C. The transposon library of YeO3-c was grown at 37 degrees C and screened for phage phi R1-37-resistant transposon insertion mutants. Three types of mutant were isolated: (i) phage receptor mutants expressing O-antigen (LPS-smooth), (ii) phage receptor mutants not expressing O-antigen (LPS-rough), and (iii) LPS-smooth mutants with the phage receptor constitutively sterically blocked. Mutant type (i) was characterized in detail; the transposon insertion inactivates an operon, named the trs operon. The main findings based on this mutant are: (i) the frs operon is involved in the biosynthesis of the LPS outer core in YeO3-c; the nucleotide sequence of the trs operon revealed eight novel genes showing similarly to known polysaccharide biosynthetic genes of various Gram-negative bacteria as well as to capsule biosynthesis genes of Staphylococcus aureus; (ii) the biosynthesis of the core of YeO3-c involves at least two genetic loci; (iii) the trs operon is required for the biosynthesis of the bacteriophage phi R1-37 receptor structures; (iv) the homopolymeric O-antigen of YeO3-c is ligated to the inner core in Y. enterocolitica O:3; (v) the trs operon is located between the adk-hemH and galE-gsk gene pairs in the Y. enterocolitica chromosome; and (vi) the phage phi R1-37 receptor is present in many but not in all Y. enterocolitica serotypes. The results also allow us to speculate that the trs operon is a relic of the ancestral rfb region of Y. enterocolitica O:3 carrying genes indispensable for the completion of the core polysaccharide biosynthesis.

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“…However, the latter alternative might not be valid as the bacteria are most likely degraded and processed by rabbit antigen-presenting cells during immunization. Acker et al reported that on whole bacteria, ECA is better exposed on the cell surface of Rc mutant Ye75R bacteria than on the parental S strain Ye75S bacteria ( Acker et al 1981 ).…”

Section: Resultsmentioning

confidence: 99%

ECA-immunogenicity of Proteus mirabilis strains

Duda

Beczała

et al. 2009

Arch. Immunol. Ther. Exp.

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Introduction: Bacteria of the genus Proteus are opportunistic pathogens and cause mainly urinary tract infections. They also play a role in the pathogenesis of reactive arthritis (RA). Patients suffering from Yersinia-triggered RA often carry high titers of antibodies specific to enterobacterial common antigen (ECA). The immunogenicity of ECA has not received much attention thus far and studies have focused mainly on the ECA of Escherichia coli and Yersinia enterocolitica. In this paper the ECA-immunogenicity of Proteus mirabilis is elucidated using two wild-type strains (S1959 and O28) as well as their rough (R) derivative strains R110/1959, which expresses lipopolysaccharide (LPS) with a full core, and R4/O28, which expresses LPS with only an inner core. Materials and Methods: Rabbit polyclonal antisera were produced by immunization with boiled suspensions of the four P. mirabilis strains. The antisera were tested for the presence of antibodies specific to ECA by Western blotting using glycerophospholipid-linked ECA (ECA PG ) of Salmonella montevideo as antigen. Lipopolysaccharide (LPS) was isolated from the four strains by the hot phenol/water procedure in which ECA PG is co-extracted with LPS and by the phenol/chloroform/petroleum ether extraction that results in the isolation of LPS and/or LPS-linked ECA (ECA LPS ) free of ECA PG . The LPS preparations were tested for the presence of ECA by Western blotting using ECA-specific antibodies. Results:The results demonstrated that all four P. mirabilis strains were ECA immunogenic. The rabbit antisera immunized by the four strains all contained ECA-specific antibodies. Analysis of the LPS preparations demonstrated that the P. mirabilis wild-type strains O28 and S1959 and the Ra mutant strain R110/1959 expressed ECA LPS , suggesting that it induced the anti-ECA antibody responses. Only the presence of ECA PG could be demonstrated in the Rc mutant strain R4/O28. Conclusions: These results therefore suggest that, similar to E. coli, LPS with a full core is also required as the acceptor of ECA for P. mirabilis strains to produce ECA LPS . Since ECA PG is not immunogenic unless combined with some proteins, it is likely that ECA PG -protein complexes formed during the intravenous immunization with the Rc mutant strain R4/O28.

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Localization of enterobacterial common antigen in Yersinia enterocolitica by the immunoferritin technique

Cited by 26 publications

References 20 publications

ECA, the enterobacterial common antigen

ECA, the enterobacterial common antigen

A novel locus of Yersinia enterocolitica serotype O:3 involved in lipopolysaccharide outer core biosynthesis

ECA-immunogenicity of Proteus mirabilis strains

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