SEARCH · PubMed Health

Results for “ENTEROTOXINS”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 685 records · Page 38Linked to original sources

PubMed1966

Leukocytic response in monkeys challenged with staphylococcal enterotoxin.

Sugiyama, H. (University of Chicago, Chicago, Ill.), and E. M. McKissic, Jr. Leukocytic response in monkeys challenged with staphylococcal enterotoxin. J. Bacteriol. 92:349-352. 1966-The feeding of staphylococcal enterotoxin to monkeys elicited a leukocytosis which was evident within 0.5 hr of challenge. The peak neutrophilic leukocytosis was reached in 3 hr, and then subsided so that leukocyte counts were normal within 28 hr. Each of the three serological types of enterotoxin tested induced the same effects. Intravenous injection of enterotoxin slightly above the emetic ed(50) level produced an initial leukopenia followed by a neutrophilic leukocytosis which was maximal 9 or more hr postinjection. With smaller intravenous challenges, some animals responded with a leukopenia followed by a leukocytosis, some with only a leukocytosis, and others with no significant change in total leukocyte counts. The reversal of normal lymphocyte-to-neutrophile ratio toward a neutrophile-predominant white blood cell population occurred in all animals.

Journal Article↗

PubMed1984

Production of cholera-like enterotoxin by Aeromonas hydrophila.

A total of 249 strains of mesophilic Aeromonas including 179 A. hydrophila and 70 A. caviae were tested for production of cholera-like enterotoxin by reversed passive latex agglutination (RPLA) assay. A cholera-like enterotoxin neutralized with cholera antitoxin was demonstrated in the culture filtrates from eight (4.5%) of the 179 A. hydrophila strains, while none of A. caviae strains revealed the enterotoxin production in the test. Production of the cholera-like enterotoxin in the eight strains of A. hydrophila was also confirmed by enzyme-linked immunosorbent assay (ELISA).

Aeromonas↗

PubMed1983

[Staphylococcal coagglutination for the detection of the enterotoxin of Clostridium perfringens].

The staphylococcal coagglutination technique has been used in recent years for detecting various bacterial antigens and toxins. It is a simple and rapid technique which requires no specialized equipment. This report describes a staphylococcal coagglutination procedure for assaying C. perfringens enterotoxin. Its sensitivity and specificity were studied with the aid of various enterotoxin preparations and culture filtrates of C. perfringens and other Clostridium species. This assay detects between 1.9 and 3.8 micrograms of enterotoxin per ml. Only the enterotoxin preparations and the C. perfringens culture fluids were positive.

Agglutination Tests↗

PubMed1996

Hybridization of 2,659 Clostridium perfringens isolates with gene probes for seven toxins (alpha, beta, epsilon, iota, theta, mu, and enterotoxin) and for sialidase.

OBJECTIVE: To genetically characterize Clostridium perfringens isolates for association of pathologic type with various diseases. DESIGN: Prospective study. SAMPLE POPULATION: 2,659 C perfringens isolates from various nonhuman animals species, human beings, and foods. PROCEDURE: Colony hybridization with DNA probes for 7 toxin (alpha, beta, epsilon, iota (subunits a and b), theta, mu, and enterotoxin) genes and 1 sialidase gene were performed to group the isolates by pathologic type. RESULTS: Enterotoxin-negative type-A isolates were the most common (2,575/2,659), were isolated from all sources, and were separated into 5 pathologic types. In cattle and horses with enterotoxemia, essentially only these pathologic types were identified. The enterotoxin-negative isolates of types C or D each had a single pathologic type. Type-C isolates were isolated only from swine with necrotic enteritis and type-D isolates from small ruminants with enterotoxemia, except that 1 type-D isolate was also found from a healthy fish. Type-B or -E isolates were not found. Among the 47 enterotoxin-positive isolates, 5 isolates from sheep or deer were type D and the other 42 were type A. These 42 isolates were grouped into 3 pathologic types: 1 type was isolated from samples of almost all origins, but the other 2 types were found in only 5 fish, 4 human beings, and 1 dog. CONCLUSIONS AND CLINICAL RELEVANCE: Genetic characterization of these isolates allowed identification of 11 different pathologic types. This approach may be useful in molecular diagnosis and prophylaxis of clostridial disease.

Animals↗

PubMed1985

Comparison of receptors for cholera and Escherichia coli enterotoxins in human intestine.

Extraction of lipids from human small intestinal epithelial cells or brush borders removed specific binding sites for cholera toxin completely, but only about 50% of the receptor sites for Escherichia coli heat-labile enterotoxin. Both cholera toxin and E. coli heat-labile enterotoxin bound strongly to ganglioside GM1 in the lipid extract and, to a lesser extent, to another monosialoganglioside and to GD1b. The results suggest that E. coli heat-labile enterotoxin binds to both ganglioside and glycoprotein receptor sites of the human small intestinal epithelium, whereas cholera toxin binding was restricted to the ganglioside receptors.

Cholera Toxin↗

PubMed1992

A gradient in expression of the Escherichia coli heat-stable enterotoxin receptor exists along the villus-to-crypt axis of rat small intestine.

Binding of Escherichia coli heat-stable enterotoxin to its receptor is critical to the initiation of toxin-induced secretion and diarrheal disease; it is also likely, however, that this receptor binds an endogenous ligand. In order to characterize the expression of the heat-stable enterotoxin receptor in the small intestine, we isolated epithelial cells from villus tip to crypt in rat jejunum and ileum. Binding of radiolabeled toxin was maximal in the villus preparations and gradually decreased along the villus-to-crypt axis, paralleling the decline of sucrase activity. Northern blots of total RNA identified a single heat stable enterotoxin receptor transcript (3.8 kb), predominantly in the villus cell fractions. In situ hybridization demonstrated clear signal in the villus cells with no apparent signal in the crypt cells, lamina propria or muscularis. Expression of this receptor was greatest after enterocytes leave the proliferative cycle and enter villi. This pattern of gene and protein expression may reflect a role of this receptor in binding endogenous ligands which in turn may regulate intestinal ion flux along the villus-to-crypt axis.

Animals↗

PubMed1964

PRODUCTION OF ANTISERUM FOR STAPHYLOCOCCAL ENTEROTOXIN.

Immunization of rabbits with approximately 95% pure enterotoxin B and approximately 20 and 50% pure enterotoxin A yielded specific antisera which required no and little absorption, respectively, when used in the slide double-diffusion test. Methods for purifying enterotoxin A and for the production and absorption of antisera are presented.

Animals↗

PubMed1981

Specific receptor binding of staphylococcal enterotoxins by murine splenic lymphocytes.

We describe a reliable assay to measure the specific binding of 125I-labeled staphylococcal enterotoxin A (SEA) by murine spleen cells. Toxin binding by lymphocytes was specific in that it was inhibited by unlabeled SEA but not by unrelated proteins. The biological activity of SEA (T-lymphocyte mitogenesis) correlated with toxin binding to splenic lymphocytes. In the presence of high concentrations of [125I]SEA, specific binding increased rapidly and approached saturation after 2 h. Toxin binding was sensitive to temperature and pH and was directly proportional to the concentration of spleen cells in the incubation mixture. We estimated that there was a single class of toxin-binding sites, which had an apparent equilibrium dissociation constant (Kd) of 8 x 10(-7) M and numbered 3,600 sites per cell. SEA and the antigenically distinct compounds staphylococcal enterotoxins B and E in excess competitively inhibited binding of [125I]SEA to mouse spleen cells. Our data suggest a common class of binding sites for the three staphylococcal enterotoxins.

Animals↗

PubMed1992

Binding of class II Escherichia coli enterotoxins to mouse Y1 and intestinal cells.

The binding of class II Escherichia coli heat-labile enterotoxins (LT) to Y1 tissue-cultured cells and mouse intestinal cells was studied and compared with that of class I toxins, including cholera enterotoxin. All radioiodinated (125I) toxins retained their biological activities in both model systems, but only LTIIb could be shown to bind specifically to target cells. LTIIa could inhibit the binding of both class I and LTIIb toxins, a finding which correlates with its ability to bind to multiple gangliosides. LTIIb could not inhibit the binding of the other enterotoxins. The binding and activity of class II toxins could not be modulated by prior exposure of target cells to the B subunit of LTI.

Adrenal Glands↗

PubMed1987

Anti-idiotypic antibodies as staphylococcal enterotoxin receptor probes on monkey mast cells.

The immediate-type skin reaction in unsensitized monkeys upon challenge with staphylococcal enterotoxin B (SEB) was studied to define the role of mast cell receptors in the action of the toxin. For this purpose anti-idiotypic antibodies (anti-Id) were raised in BALB/c mice against monoclonal anti-SEB antibodies and purified by idiotype affinity chromatography. Anti-Id completely abolished skin reactions upon challenge with SEB without having biological functions itself. The data are compatible with the view that receptors for staphylococcal enterotoxin actually exist on the mast cell membrane of primates and anti-Id may be of potential value to influence the course of staphylococcal enterotoxin-mediated effects.

Animals↗

PubMed1991

Localization of the receptor-binding region of Clostridium perfringens enterotoxin utilizing cloned toxin fragments and synthetic peptides. The 30 C-terminal amino acids define a functional binding region.

In this study a short sequence encoding the receptor-binding activity of the much larger 35-kDa enterotoxin elaborated by Clostridium perfringens was localized by recombinant DNA techniques. Defined fragments corresponding to portions of the enterotoxin gene were cloned into an Escherichia coli expression vector system, and these lysates were analyzed for their ability to compete for binding with native C. perfringens enterotoxin (CPE). The lysate containing CPE290-319 (CPE sequence encompassing residues 290-319) was shown to compete with 125I-CPE for specific binding sites on rabbit intestinal brush border membranes. To confirm this finding, a peptide corresponding to the CPE amino acid sequence 290-319 was synthesized and found to completely block CPE specific binding. To demonstrate directly that CPE290-319 can act as a competitive antagonist of CPE cytotoxicity for physiologic receptors, Vero cells were preincubated with either E. coli lysates containing CPE290-319 or the synthetic peptide corresponding to this sequence. Preincubation of Vero cells with either the lysate or the peptide completely protected these cells from CPE challenge. This information localizes the C-terminal 30 residues of CPE (CPE290-319) as a linear sequence sufficient for recognition and binding to the eukaryotic CPE receptor.

Amino Acid Sequence↗

PubMed1985

STb enterotoxin of Escherichia coli: cyclic nucleotide-independent secretion.

Escherichia coli may produce a heat-labile enterotoxin (LT) or two heat-stable enterotoxins (STa, STb). Experimentally, STb is consistently active only in 5 h-weaned pig intestinal loops (WPIL), an effect that is largely removable by rinsing. At least three mechanisms initiate small intestinal secretion: cyclic AMP (LT), cyclic GMP (STa) and calcium (A23187). All three increase short-circuit current (SCC) in Ussing chambers by stimulating net Cl- secretion. STb significantly increases SCC within 2-5 minutes in Ussing chambers and is independent of cyclic AMP and cyclic GMP. When compared to crude culture filtrates of a non-toxigenic strain of E. coli, crude culture filtrates of STb did not alter Na+ or Cl- undirectional or net fluxes. However, the calculated residual ion flux (JRnet) increased significantly in STb-treated tissues and appeared to largely account for the STb-induced increase in SCC. Furosemide applied serosally (10(-3) M), the removal of extracellular calcium, and lanthanum chloride (10(-3) M) did not inhibit the effect of STb on SCC. Chlorpromazine (0.4 mM) completely inhibited STb-induced secretion in porcine loops. This inhibition was a non-specific reversal of the STb effect because in Ussing chambers, chlorpromazine simply induced an equal and opposite effect on SCC. These results indicate that STb initiates intestinal secretion in porcine jejunum in vitro by stimulating primarily non-chloride anion secretion in the absence of extracellular calcium. We postulate that STb causes bicarbonate secretion by a mechanism distinct from those of previously studied enterotoxins.

Animals↗

PubMed1992

Specificity of rat T cell receptor V beta chain usage in proliferative responses to staphylococcal enterotoxin B.

The staphylococcal enterotoxins (SE) are potent stimulators of T cell proliferative responses in humans and in mice. In these systems, the toxins function as superantigens and stimulate T cells bearing particular V beta. Although homology between the V beta of mice and humans is limited, related V beta families may respond to certain SE in a similar fashion. In this report, we have characterized the rat T cell response to staphylococcal enterotoxin B (SEB). Rat T cells from several lymphoid organs proliferated strongly in response to both commercially available and recombinant SEB. Using a polymerase chain reaction assay, we identified the predominant V beta families stimulated by this enterotoxin. The T cell receptor V beta elements used by rat T cells were similar to but not completely identical with those used by mice. The V beta profile stimulated depended on the purity of the SEB preparation used.

Animals↗

PubMed1995

B7.2 provides co-stimulatory functions in vivo in response to staphylococcal enterotoxin B.

Excessive T cell activation induced by bacterial superantigens plays an important role in the pathology associated with Gram-positive bacteremia. To gain insight into the early phases of T cell activation by bacterial enterotoxins in vivo, we investigated the ability of antibodies to well-defined co-stimulatory molecules to inhibit T cell activation and the subsequent toxic shock syndrome induced in BALB/c mice following the injection of staphylococcal enterotoxin B (SEB). We demonstrate here that a single dose of anti-B7.2 antibodies, but not anti-B7.1 antibodies, significantly inhibits T cell activation, as judged by lower systemic IL-2 release, blastogenesis and IL-2 receptor expression, and reduces the lethal effect of SEB in D-galactosamine-sensitized mice. These results demonstrate that co-stimulation through the B7.2 molecule plays an important role in the activation of T cells in response to SEB in vivo and suggest alternative therapies for septic shock caused by bacterial enterotoxins based on blocking antibodies to co-stimulatory molecules.

Animals↗

PubMed1994

Differential RNA regulation by staphylococcal enterotoxins A and B in murine macrophages.

Staphylococcal enterotoxin A (SEA) is significantly better than enterotoxin B (SEB) in activating tumor necrosis factor (TNF) secretion by B6MP102 cells. Both toxins bound to B6MP102 cells; however, SEB competed less effectively with SEA than SEA competed with SEB. This suggested that receptors unique to SEA were present on B6MP102 cells. Signal transduction occurred in response to both toxins. Within 30 s after addition, SEA and SEB significantly increased the F-actin concentration in B6MP102 cells. However, only SEA induced increased TNF mRNA levels. B6MP102 cells incubated with interferon-gamma and SEB secreted TNF. However, enhanced mRNA expression was delayed and the concentration of TNF secreted was less than that of B6MP102 cells stimulated with SEA. Although these data suggest that receptors unique to SEA are present on B6MP102 cells, they also indicate that staphylococcal enterotoxins differentially regulate TNF at the RNA level, perhaps because of differences in binding to the plasma membrane.

Actins↗

PubMed2000

The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules.

The X-ray structure of the superantigen staphylococcal enterotoxin H (SEH) has been determined at 1.69 A resolution. In this paper we present two structures of zinc-free SEH (apoSEH) and one zinc-loaded form of SEH (ZnSEH). SEH exhibits the conventional superantigen (SAg) fold with two characteristic domains. In ZnSEH one zinc ion per SEH molecule is bound to the C-terminal beta-sheet in the region implicated for major histocompatibility complex class II (MHC class II) binding in SEA, SED and SEE. Surprisingly, the zinc ion has only two ligating amino acid residues His206 and Asp208. The other ligands to the zinc ion are two water molecules. An extensive packing interaction between two symmetry-related molecules in the crystal, 834 A(2)/molecule, forms a cavity that buries the zinc ions of the molecules. This dimer-like interaction is found in two crystal forms. Nevertheless, zinc-dependent dimerisation is not observed in solution, as seen in the case of SED. A unique feature of SEH as compared to other staphylococcal enterotoxins is a large negatively charged surface close to the Zn(2+) site. The interaction of SEH with MHC class II is the strongest known among the staphylococcal enterotoxins. However, SEH seems to lack a SEB-like MHC class II binding site, since the side-chain properties of structurally equivalent amino acid residues in SEH and those in SEB-binding MHC class II differ dramatically. There is also a structural flexibility between the domains of SEH. The domains of two apoSEH structures are related by a 5 degrees rotation leading to at most 3 A difference in C(alpha) positions. Since the T-cell receptor probably interacts with both domains, SEH by this rotation may modulate its binding to different TcR Vbeta-chains.

Amino Acid Sequence↗

PubMed2000

Identification of Staphylococcus aureus enterotoxins A and B genes by PCR-ELISA.

We developed PCR-enzyme linked immunosorbent (ELISA) assays to detect Staphylococcus aureus enterotoxins A and B genes. The assays use internal biotin-labelled oligonucleotides as capture probes for immobilizing and subsequently detecting target sequences on microtiter plates. The detection limits of the PCR-ELISAs were approximately 250 gene copies, versus 2500 gene copies by agarose gel analysis. The sensitivity of the assays, as determined from a reference panel of 46 coded samples that included DNA purified from 31 different bacterial species and strains, SEA and SEB plasmid controls, and no-template controls was 100%. No cross-reactivity was observed with DNA from non-staphylococcal species. Using 27 clinical isolates of S. aureus, the SEA PCR-ELISA identified the enterotoxin A (sea) gene in 26 samples, and the SEB PCR-ELISA identified the enterotoxin B (seb) gene in all 27 samples. Compared with conventional antigen capture ELISAs for SEA and SEB toxins, the PCR-ELISAs showed overall superior detection limits. The sensitivity and specificity levels of the SEA PCR-ELISA and the SEA toxin ELISA were comparable within their respective detection thresholds, but the sensitivity and specificity of the SEB PCR-ELISA was much greater than that of SEB toxin ELISA.

Bacteria↗

PubMed1994

Molecular characterization of an enterotoxin from Salmonella typhimurium.

In this study, we describe the molecular and antigenic characteristics of a cloned enterotoxin from Salmonella typhimurium strain Q1. The full length Salmonella enterotoxin gene (stn), localized on a 2.8 kb ClaI/PstI DNA fragment, was cloned from a genomic library of Salmonella. Based on nucleotide sequence analysis, the stn gene contained 749 bp that would encode a protein having a molecular size of 29,073. The most unusual feature of the stn gene was the presence of a rare initiation codon (TTG) in lieu of the typical ATG codon, which required site-directed mutagenesis to confirm the precise initiation site. The expression of the stn gene in a bacteriophage T7 RNA polymerase/promoter system was enhanced by introducing a typical ATG start codon and an optimal Shine-Dalgarno sequence upstream of the stn gene by site-directed mutagenesis. The stn gene was located opposite the hydHG operon that regulates labile hydrogenase activity in Salmonella species and Escherichia coli. The overall amino acid sequence of the enterotoxin was quite dissimilar to any other published sequence, including cholera toxin or other adenylate cyclase-activating proteins. However, an intriguing similarity in a small region of the amino acid sequence of Stn was observed with portions of the amino acid sequences from several other protein toxins known to ADP-ribosylate host cell proteins. This region of homology may indicate a conserved motif, within the active site, that is involved in the stimulation of adenylate cyclase activity.

Amino Acid Sequence↗