Major outer membrane protein of Campylobacter fetus: physical and immunological characterization

McCoy, Elena C.; Wiltberger, H A; Winter, Josef

doi:10.1128/iai.13.4.1258-1265.1976

Cited by 30 publications

(19 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This was not reported in the previous study, probably as a result of the smaller number of organisms studied. Our study confirms that C. jejuni and C. coli isolates cannot be differentiated from one another on the basis of OMP profiles but that these are distinct from those of C. fetus (20) and C. faecalis, two closely related catalase-positive Campylobacter species.…”

Section: Discussionsupporting

confidence: 78%

Identification and characterization of Campylobacter jejuni outer membrane proteins

Hopkins¹,

Berka²,

Vasil³

et al. 1983

Infect Immun

138

View full text Add to dashboard Cite

Outer membrane proteins from isolates of Campylobacter jejuni were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sarcosinate-insoluble membrane preparations were outer membrane enriched based on increased ketodeoxyoctonate concentrations, the presence of surface-exposed 125I-labeled proteins that were hydrophobic, and similarity to membrane vesicle (bleb) sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles. Most isolates contained a single major band with molecular weight of 41,000 to 45,000. Profiles of C. jejuni and Campylobacter coli isolates were indistinguishable, but either could be easily differentiated from Campylobacter fetus and Campylobacter faecalis. The profiles were stable for strains under a variety of growth, incubation and passage conditions. We classified 110 isolates from patients with sporadic campylobacter enteritis into nine subtypes based on differences in outer membrane sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles. Two categories accounted for 76% of the isolates. Complete concordance was observed in subtypes of strains obtained from epidemiologically related cases. Thus, comparison of the major outer membrane proteins of C. jejuni is a useful technique for investigating the transmission of this organism and may provide a basis for immunological characterization of the outer membrane proteins.

show abstract

Section: Discussionsupporting

confidence: 78%

Identification and characterization of Campylobacter jejuni outer membrane proteins

Hopkins¹,

Berka²,

Vasil³

et al. 1983

Infect Immun

138

View full text Add to dashboard Cite

show abstract

“…Extraction of S protein. An S protein was extracted from each strain by the method of McCoy et al (16). In short, bacterial cells cultured for 48 h were suspended in 100 ml of 0.2 M glycine-hydrochloride buffer (pH 2.2) at a concentration of 5 x 109 CFU/ml.…”

Section: Methodsmentioning

confidence: 99%

Correlation between molecular size of the surface array protein and morphology and antigenicity of the Campylobacter fetus S layer

1991

View full text Add to dashboard Cite

The correlation between the molecular size of the surface layer protein (S protein) and both structure and antigenicity of the Campylobacter fetus surface layer (S layer) was investigated in several clinical strains and their spontaneous variants which produce S proteins of molecular weights (MW) different from those of the parents. Only three molecular sizes of the S proteins were observed (98, 127, and 149 kDa) in the parental and variant strains. Immunologically, the 98-kDa protein and the 149-kDa protein but not the 127-kDa protein were cross-reactive. Freeze-etching analysis showed that the 98-kDa S protein formed a hexagonal arrangement with a 24-nm center-to-center space and that the S proteins with larger MW (127 or 149 kDa) formed tetragonal ones with an 8-nm center-to-center space. Thus, the MW changes of the S proteins seen in the variant strains were associated with both morphological and antigenic changes in S layer. These observations support the hypothesis that the pattern and antigenicity of the C. fetus S layer is determined by the particular type of S protein. Furthermore, the presence of the two different S layer patterns on a single bacterial cell indicates that multiple S proteins can be produced and expressed in a single cell.

show abstract

“…The principal classes of structural proteins in the outer membrane of Escherichia coli are matrix porins (OmpC and OmpF), a heat-modifiable protein (OmpA), and murein lipoprotein (6,45). With certain modifications, as, for example, in the absence of murein-linked lipoprotein (22,36,57), counterpart proteins have been detected in a wide variety of gram-negative genera (4,6,8,15,21,25,26,28,34,37,53) and appear to be essential constituents of gram-negative bacteria. Virtually no information is yet available on the nature of comparable proteins in Brucella abortus.…”

mentioning

confidence: 99%

Outer membrane proteins of Brucella abortus: isolation and characterization

Verstreate¹,

Creasy²,

Caveney³

et al. 1982

Infect Immun

147

124

View full text Add to dashboard Cite

Outer membrane proteins were derived from one rough and four smooth strains of Brucella abortus by sequential extraction of physically disrupted cells with N-lauroylsarcosinate and dipolar ionic detergent. Extraction of outer membrane proteins was ineffective, however, without predigestion with lysozyme. Three groups of proteins were present and could be separated in their native state by sequential anion-exchange chromatography and gel filtration. Membrane proteins contained substantial quantities of tightly adherent lipopolysaccharide which could be reduced but not eliminated by extraction of cells with trichloroacetic acid before disruption. Group 2 proteins, apparently trimers in their native state, gave rise to 43,000- and 41,000-molecular-weight bands after complete denaturation in sodium dodecyl sulfate. They were antigenically identical among all the strains, showed close resemblance in amino acid composition to each other and a general similarity to OmpF of Escherichia coli, and are proposed to be the porins of B. abortus. Group 3 proteins occurred as 30,000-molecular-weight bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, although additional bands were frequently observed in this region. In none of the strains did group 3 proteins manifest heat-modifiable characteristics. Proteins of different strains bore a high degree of similarity to each other in amino acid composition, except in methionine, isoleucine, tyrosine, and histidine. Differences occurred consistently in amino acid composition between group 2 and 3 proteins, and some of these correspond to differences between OmpF and OmpA. Group 2 and 3 proteins were antigenically distinct from each other, but the principal group 3 antigens were shared among all the strains. Despite the lack of heat modifiability, perhaps influenced by adherent lipopolysaccharide, group 3 proteins are proposed as counterparts to OmpA. Most of the group 1 proteins, minor components, were physically associated with those of group 3 unless in sodium dodecyl sulfate. Group 1 proteins produced a major band at 94,000 and exhibited heat modifiability. No evidence was found of a low-molecular-weight lipoprotein in the outer membrane of B. abortus, but this is not taken to exclude its occurrence.

show abstract

Major outer membrane protein of Campylobacter fetus: physical and immunological characterization

Cited by 30 publications

References 26 publications

Identification and characterization of Campylobacter jejuni outer membrane proteins

Identification and characterization of Campylobacter jejuni outer membrane proteins

Correlation between molecular size of the surface array protein and morphology and antigenicity of the Campylobacter fetus S layer

Outer membrane proteins of Brucella abortus: isolation and characterization

Contact Info

Product

Resources

About