A novel virulence-associated cell surface structure composed of 47-kd protein subunits in Yersinia enterocolitica.

Zaleska, Małgorzata; Lounatmaa, Kari; Nurminen, Marjatta; Wahlström, Eva; Mäkelä, P H

doi:10.1002/j.1460-2075.1985.tb03732.x

Cited by 53 publications

(43 citation statements)

References 39 publications

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“…We suspect that a form of phase variation may account for these observations. It is possible that antigen 43 represents for E. coli a novel type of S-layer (30) or surface appendage (36). If this is the case, it does not possess the distinctive morphology which normally characterizes such structures (11,30).…”

Section: Discussionmentioning

confidence: 99%

Identification and partial characterization of a novel bipartite protein antigen associated with the outer membrane of Escherichia coli

Owen¹,

Caffrey²,

Josefsson³

1987

J Bacteriol

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A study by crossed immunoelectrophoresis performed in conjunction with precipitate excision and polypeptide analysis identified a new antigen complex in the envelope of Escherichia coli ML308-225. This antigen corresponds to antigen 43 in the crossed immunoelectrophoresis profile of membrane vesicles (P. Owen and H. R. Kaback, Proc. Natl. Acad. Sci. USA 75:3148-3152, 1978). Immunoprecipitation experiments conducted with specific antiserum revealed that the complex was expressed on the cell surface and that it contained, in equal stoichiometry, two chemically distinct polypeptides termed a and (Mrs of 60,000 and 53,000, respectively). The polypeptide was heat modifiable, displaying an apparent Mr of 37,000 when solubilized at temperatures below 70°C. Analysis of fractions obtained following cell disruption, isopycnic centrifugation, and detergent extraction indicated that both a and polypeptides were components of the outer membrane. The two polypeptides were not linked by disulfide bonds, and neither was peptidoglycan associated. The complex contained no detectable lipopolysaccharide, enzyme activity, fatty acyl groups, or other cofactors. Neither correlated with E. coli proteins of similar molecular weight which had previously been shown to be associated with the outer membrane. Antibodies were raised to individual a and I1 polypeptides. Each of these sera was shown to be subunit specific when tested against denatured membrane proteins. In contrast, each immunoglobulin preparation coprecipitated both a and polypeptides when tested against undenatured proteins derived from Triton X-100-treated membranes. The results reveal the presence of a novel bipartite protein antigen in the outer membrane of E. coli.The outer membrane of Escherichia coli is known to contain a number of major protein species (1, 15). Several of these are porins involved in the passive accumulation of small hydrophilic solutes (2,19). Others, such as the ironregulated outer membrane proteins and the vitamin B12 receptor, are involved in the TonB-dependent uptake of more specific solutes (4). Other major proteins of the E. coli outer membrane include the Braun lipoprotein (the Lpp protein), peptidoglycan-associated lipoprotein, and the ompA gene product. In part at least, these appear to play a structural role for the cell envelope (1, 15). Several other minor proteins and enzymes have also been identified and studied (10,17,20,35). In addition to the above components, there exist in the outer membratne several additional proteins about which considerably less is known, e.g., protein III, an 83-kilodalton iron-regulated protein, and several proteins in the 60-to 40-kilodalton range (15,26).In an attempt to identify and characterize the major antigens of the cell envelope of aerobically grown E. coli, a crossed immunoelectrophoresis (CIE) reference profile has been established in which over half of the 50 or so resolved antigens have been identified in functional terms or partially characterized (for reviews, see references 21 to 23).

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Section: Discussionmentioning

confidence: 99%

Identification and partial characterization of a novel bipartite protein antigen associated with the outer membrane of Escherichia coli

Owen¹,

Caffrey²,

Josefsson³

1987

J Bacteriol

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“…It has been reported (38) into monomeric subunits that migrated with an apparent molecular mass of ca. 47 kDa.…”

Section: Methodsmentioning

confidence: 99%

Thermoregulation-dependent expression of Yersinia enterocolitica protein 1 imparts serum resistance to Escherichia coli K-12

Martı́nez

1989

J Bacteriol

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Resistance to the bactericidal action of normal human serum is one of the characteristics of virulent Yersinia enterocolitica. This property is attributable to the virulence plasmid harbored by pathogenic strains of the species. Serum resistance in Y. enterocolitica is thermoregulated, and its expression correlates well with the presence of virulence plasmid-encoded outer membrane proteins. To further examine the biochemical basis underlying resistance, we cloned a large segment (ca. 30 kilobases) of virulence plasmid DNA and studied the expression of plasmid-encoded outer membrane proteins in a serum-sensitive strain of Escherichia coli. The presence of the 160-kilodalton Y. enterocolitica-derived outer membrane protein 1 on E. coli transformants conferred a high degree of hydrophobicity, autoagglutinability, and resistance to serum killing. All of these properties were thermoregulated in E. coli with fidelity, suggesting that a functional thermoregulatory element was present in the cloned DNA. Elimination of protein 1 from the outer membrane of E. coli transformants by insertional inactivation of the structural gene with a Kanr gene cassette abrogated all of these properties and returned the serum-sensitive phenotype.

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“…We also studied the expression of virF itself and determined its nucleotide sequence. The (29,54). yopD encodes Yop37 (15).…”

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confidence: 99%

Homology between virF, the transcriptional activator of the Yersinia virulence regulon, and AraC, the Escherichia coli arabinose operon regulator

et al. 1989

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A novel virulence-associated cell surface structure composed of 47-kd protein subunits in Yersinia enterocolitica.

Cited by 53 publications

References 39 publications

Identification and partial characterization of a novel bipartite protein antigen associated with the outer membrane of Escherichia coli

Identification and partial characterization of a novel bipartite protein antigen associated with the outer membrane of Escherichia coli

Thermoregulation-dependent expression of Yersinia enterocolitica protein 1 imparts serum resistance to Escherichia coli K-12

Homology between virF, the transcriptional activator of the Yersinia virulence regulon, and AraC, the Escherichia coli arabinose operon regulator

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