Comparison of enterotoxic activities of heat-stable enterotoxins from class 1 and class 2 Escherichia coli of swine origin

Whipp, S C; Moon, Harley W.; Argenzio, Robert A.

doi:10.1128/iai.31.1.245-251.1981

Cited by 40 publications

(17 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…More important, ST could be detected and quantitated in culture supernatants or purified toxin fractions by the RIA. In contrast to the immunological homogeneity observed in this work, ST preparations have been shown to vary with respect to molecular weight (1,11,23), biological activity in different animal models (10,16,17,19,26), heat stability (2), and methanol solubility (2). Five different STs produced by class I and II porcine enteropathogens and ENT' strains of bovine and human origins have been purified in our laboratory (Dreyfus et al, manuscript in preparation).…”

Section: Infect Immuncontrasting

confidence: 71%

Immunological properties of Escherichia coli heat-stable enterotoxins: development of a radioimmunoassay specific for heat-stable enterotoxins with suckling mouse activity

Frantz¹,

Robertson²

1981

Infect Immun

View full text Add to dashboard Cite

Antiserum was raised against the purified heat-stable enterotoxin (ST) produced by enterotoxigenic Escherichia coli strain 431, a class II porcine enteropathogen. The antiserum was used to examine the antigenic determinants of STs produced by enterotoxigenic strains of different host origins and develop a sensitive radioimmunoassay specific for ST having biological activity in suckling mice and piglets (STA). The antiserum neutralized one effective dose of toxin at a dilution of 1:5,000 and neutralized approximately 40 microgram of toxin per ml of serum. In the radioimmunoassay, protein A-bearing staphylococci was used as the primary solid-phase adsorbent. The purified STs produced by a class I enteropathogen (strain 667) and by a bovine enterotoxigenic strain (B-41) exhibited patterns of competitive inhibition identical to those of homologous unlabeled strain 431 ST in the radioimmunoassay when specific antibody to strain 431 ST was used. The levels of ST in culture supernatants determined by the suckling mouse assay correlated with the concentrations of toxin measured by the radioimmunoassay. The antiserum was specific for STA produced by enterotoxigenic E. coli of porcine, bovine, and human origins and did not react with heat-labile enterotoxin or with ST that had biological activity in piglets but not in suckling mice (STB). These results suggest that STA molecules having different host origins share at least one antigenic determinant.

show abstract

Section: Infect Immuncontrasting

confidence: 71%

Immunological properties of Escherichia coli heat-stable enterotoxins: development of a radioimmunoassay specific for heat-stable enterotoxins with suckling mouse activity

Frantz¹,

Robertson²

1981

Infect Immun

View full text Add to dashboard Cite

show abstract

“…soluble STa and methanol-insoluble STb (Burgess et al, 1978;Whipp et al, 1981). STas are 18-19-amino acid extracellular peptides that result from two independent proteolytic cleavages on a 72-amino acid precursor (pre-pro-STa) (Rasheed et al, 1990).…”

mentioning

confidence: 99%

The structure ofEscherichia coliheat-stable enterotoxin b by nuclear magnetic resonance and circular dichroism

Sarojadevi

Rizo²,

Wall

et al. 1995

Protein Sci.

View full text Add to dashboard Cite

The heat-stable enterotoxin b (STb) is secreted by enterotoxigenic Escherichia coli that cause secretory diarrhea in animals and humans. It is a 48-amino acid peptide containing two disulfide bridges, between residues I O and 48 and 21 and 36, which are crucial for its biological activity. Here, we report the solution structure of STb determined by two-and three-dimensional NMR methods. Approximate interproton distances derived from NOE data were used to construct structures of STb using distance-geometry and simulated annealing procedures. The NMRderived structure shows that STb is helical between residues 10 and 22 and residues 38 and 44. The helical structure in the region 10-22 is amphipathic and exposes several polar residues to the solvent, some of which have been shown to be important in determining the toxicity of STb. The hydrophobic residues on the opposite face of this helix make contacts with the hydrophobic residues of the C-terminal helix. The loop region between residues 21 and 36 has another cluster of hydrophobic residues and exposes Arg 29 and Asp 30, which have been shown to be important for intestinal secretory activity. CD studies show that reduction of disulfide bridges results in a dramatic loss of structure, which correlates with loss of function. Reduced STb adopts a predominantly random-coil conformation. Chromatographic measurements of concentrations of native, fully reduced, and single-disulfide species in equilibrium mixtures of STb in redox buffers indicate that the formation of the two disulfide bonds in STb is only moderately cooperative. Similar measurements in the presence of 8 M urea suggest that the native secondary structure significantly stabilizes the disulfide bonds.

show abstract

“…T h e stable toxin (ST)-producing Esclierichiu coli no. 1261 (a gift of Dr H. W. Moon, National Animal Disease Laboratory, Ames, IA), a known porcine Class 1 enterotoxin producer (Whipp et al, 1981), was used as a source of the crude enterotoxin preparation. The E. coli no.…”

Section: Enteroloxin Prepurutionmentioning

confidence: 99%

Effect of lidamidine‐HCl on Escherichia coli heat‐stable enterotoxin‐induced jejunal water and electrolyte secretion in neonatal piglets

Merritt

Berkhoff

Haskell

et al. 1985

Vet Pharm & Therapeutics

View full text Add to dashboard Cite

Neonatal piglets were anesthetized, and two jejunal loops, 20 cm in length, were prepared. Then, either water or 0.12, 0.25, 0.5 or 1.0 mg/kg of lidamidine-HCl was injected intraduodenally on a randomized basis, one treatment per pig. Following this, a crude heat-stable enterotoxin (ST) preparation produced from E. coli no. 1261 was injected into the proximal jejunal loop, and trypticase soy broth (TSB) (with osmolality adjusted to equal the enterotoxin preparation) was injected into the distal jejunal loop. Piglets remained anesthetized for 3 h and were then killed. Fluid was collected from the loops for measurement of volume and Na, K and Cl concentration. Empty loop lengths were measured. There was a significant dose-related reduction of volume and Cl content, and a dose-related, but not significant, reduction in Na content in St-treated loops. A comparison of the mean differences in responses between toxin- and TSB-treated loops indicated that the major 'counter-toxic' effect of the lidamidine was a dose-related increase in water and electrolyte absorption.

show abstract

Comparison of enterotoxic activities of heat-stable enterotoxins from class 1 and class 2 Escherichia coli of swine origin

Cited by 40 publications

References 18 publications

Immunological properties of Escherichia coli heat-stable enterotoxins: development of a radioimmunoassay specific for heat-stable enterotoxins with suckling mouse activity

Immunological properties of Escherichia coli heat-stable enterotoxins: development of a radioimmunoassay specific for heat-stable enterotoxins with suckling mouse activity

The structure ofEscherichia coliheat-stable enterotoxin b by nuclear magnetic resonance and circular dichroism

Effect of lidamidine‐HCl on Escherichia coli heat‐stable enterotoxin‐induced jejunal water and electrolyte secretion in neonatal piglets

Contact Info

Product

Resources

About