Profiles of toxin production by thermophilic Campylobacter of animal origin

McFarland, B.A.; Neill, S.D.

doi:10.1016/0378-1135(92)90119-e

Cited by 16 publications

(12 citation statements)

References 30 publications

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“…Thus, in spite of screening numerous freshly isolated local clinical strains and also control strains from various laboratories and using several media that were reported to promote enterotoxin production by C. jejuni, none of the strains produced any enterotoxin in our hands. This failure to demonstrate enterotoxin production is consistent with the findings of others (14,19,24,25,30).…”

Section: Resultssupporting

confidence: 93%

Identification of a Campylobacter jejuni Protein That Cross-Reacts with Cholera Toxin

Albert¹,

Haridas²,

Steer

et al. 2007

Infect Immun

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The question of whether Campylobacter jejuni produces a cholera toxin-like toxin (CTLT) has been controversial. The objective of this study was to identify the factor that cross-reacts with CT from C. jejuni. Filtrates of C. jejuni grown in four different liquid media reported to promote CTLT production were tested by Chinese hamster ovary (CHO) cell elongation assay and for reactivity with CT antibody using GM1 ganglioside enzyme-linked immunosorbent assay (ELISA) and immunoblotting. Protein sequence was determined by matrix-assisted laser desorption ionization-time of flight (MALDI TOF-TOF). Filtrates from seven reference strains reported to produce CTLT and from 80 clinical strains were negative in the CHO cell assay, but those from three reference strains and 16 clinical strains were positive by GM1 ELISA. All strains tested, including C. jejuni NCTC 11168, which does not contain a CT gene homologue, possessed a 53-kDa protein which reacted with CT antibody by immunoblotting. This band was identified as the major outer membrane protein, PorA, of C. jejuni. CT antibody reacted by immunoblotting with a recombinant PorA, but antibody to the recombinant PorA did not react with CT. Our results indicate that C. jejuni does not produce a functional CTLT, but the reactivity of PorA with CT antibody would lead to the erroneous conclusion that C. jejuni produces a functional CTLT.

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Section: Resultssupporting

confidence: 93%

Identification of a Campylobacter jejuni Protein That Cross-Reacts with Cholera Toxin

Albert¹,

Haridas²,

Steer

et al. 2007

Infect Immun

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“…The frequency of enterotoxin production in human isolates was compared to that in animal isolates. In strains isolated from poultry and other animals in the United Kingdom, no enterotoxin production was detected (76). In that study, one strain earlier described as enterotoxin positive was included, but its enterotoxin activity could not be confirmed (76).…”

Section: Incidence Of Enterotoxin Productionmentioning

confidence: 82%

Toxin production by Campylobacter spp

Wassenaar

1997

Clin Microbiol Rev

141

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Of all the virulence factors that were proposed for Campylobacter jejuni and related species to cause disease in humans, the discovery of toxin production was the most promising but led to a rather confusing and even disappointing stream of data. The discussion of whether proteinaceous exotoxins are relevant in disease remains open. One important reason for this lack of consensus is the anecdotal nature of the literature reports. To provide a basis for an unbiased opinion, this review compiles all described exotoxins, compares their reported properties, and provides a summary of animal model studies and clinical data. The toxins are divided into enterotoxins and cytotoxins and are sorted according to their biochemical properties. Since many Campylobacter toxins have been compared with toxins of other species, some key examples of the latter are also discussed. Future directions of toxin research that appear promising are defined.

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“…Cell extracts of C. jejuni displayed cytotoxicity in HeLa and Vero cells [4]. Polymyxin extracts of C. jejuni were toxic to CHO-KI and FCL cells [21]. One membrane-associated cytotoxin in C. jejuni killed CHO and HeLa cells and can be inactivated by trypsin [23].…”

Section: Discussionmentioning

confidence: 99%

Apoptotic Effect of Outer-Membrane Proteins from Campylobacter jejuni on Chicken Lymphocytes

et al. 1999

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Campylobacter jejuni is a significant cause of food-borne diseases in humans. The bacterium is considered a commensal organism in chickens, and it can heavily colonize chickens without causing inflammation. Poultry may be the major reservoir for the human infection in developed countries. Here we show that an outer-membrane protein extract prepared from the bacteria caused apoptosis of chicken lymphocytes detected in vitro with the terminal deoxynucleotidyl transferase-mediated dUTP nick end-labeling assay that preferentially labels individual apoptotic cells. Blood- and spleen-lymphocytes from different-aged chickens displayed a significantly greater percentage of apoptotic cells after culture with the outer-membrane proteins from C. jejuni than controls treated with phosphate-buffered saline, chicken ovalbumin, or outer-membrane proteins prepared from E. coli strain BL21. The C. jejuni extract also produced apoptosis of chicken lymphoblastoid tumor cell lines. Apoptosis was blocked by pretreating the extract with proteinase K or antiserum against outer-membrane proteins. The results suggest that C. jejuni may be capable of achieving immune avoidance in chickens by causing apoptosis of lymphocytes.

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Profiles of toxin production by thermophilic Campylobacter of animal origin

Cited by 16 publications

References 30 publications

Identification of a Campylobacter jejuni Protein That Cross-Reacts with Cholera Toxin

Identification of a Campylobacter jejuni Protein That Cross-Reacts with Cholera Toxin

Toxin production by Campylobacter spp

Apoptotic Effect of Outer-Membrane Proteins from Campylobacter jejuni on Chicken Lymphocytes

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