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PubMed1988

The toxin binding inhibition test as a reliable in vitro alternative to the toxin neutralization test in mice for the estimation of tetanus antitoxin in human sera.

A method for the screening of human sera for tetanus antibodies has been developed and evaluated. The toxin binding inhibition test (ToBI-test) is based on inhibition of the binding of tetanus toxin to an antitoxin-coated immunoassay microtitre plate by tetanus antibodies. Serum samples from 191 healthy adults with different vaccination histories have been titrated for tetanus antibodies by the toxin neutralization (TN) test in mice, by toxoid-ELISA and by the ToBI-test. In every respect, the ToBI-test proved to be the best in vitro alternative to the TN-test in mice. Comparisons showed a higher degree of correlation between the ToBI-test and the TN-test than between the toxoid-ELISA and the TN-test. Furthermore, no overestimation of antibody content was seen in titrating low titre sera by the ToBI-test. In contrast, several false positive results were seen when using the toxoid-ELISA. It is concluded that the ToBI-test is a reliable and precise alternative to the TN-test and can be performed under simple laboratory conditions in a short time.

Animals↗
PubMed1979

Quantification of tetanus antitoxin in human sera. II. Comparison of counter-immunoelectrophoresis and passive haemagglutination with toxin neutralization in mice.

We described recently an improved counter-immunoelectrophoretic method for quantification of tetanus antitoxin. The toxin neutralization test in mice is considered to correlate well with protection in humans. In the present study, the correlation coefficient between the two methods was 0.89. Sera containing more than 7.0 I.U./ml could be quantified directly by counter-immunoelectrophoresis, while sera containing less tetanus antitoxin had to be concentrated prior to quantification. The passive haemagglutination test was also compared with the toxin neutralization test in mice. The correlation coefficient between the two methods was 0.76.

Antibodies, Bacterial↗
PubMed1988

Immunobiological relationships between Vibrio fluvialis and Vibrio cholerae enterotoxins.

A total of 26 strains of Vibrio fluvialis was included in this study, which were isolated from patients with diarrhoea and other sources. The GM1 enzyme linked immunosorbent assays performed with the culture filtrates of V. fluvialis yielded negative results, indicating that their receptor site is different from that of the known labile toxin. The cholera antitoxin failed to neutralize the skin permeability factor activities of all the V. fluvialis culture filtrates and none of the concentrated culture filtrates gave any precipitin band, when tested against the cholera antitoxin in Ouchterlony's gel diffusion test. These observations suggest that the toxin of V. fluvialis differs from the known cholera toxin in receptor site, mode of action and antigenicity.

Cholera Toxin↗
PubMed1963

Tarichatoxin: isolation and purification.

The potent neurotoxin occurring in the embryos of the California newt, Taricha torosa, has been obtained in crystalline form. With a lethal subcutaneous dose of approximately 0.14 micrograms for a 20-gram mouse, it is, along with saxitoxin and tetrodotoxin, one of the most toxic nonprotein substances known.

Animals↗