Characterization of allergens of the cat flea, Ctenocephalides felis: detection and frequency of IgE antibodies in canine sera.

Flea allergens, fractionated by polyacrylamide gel electrophoresis and transferred to nitrocellulose, were identified using 20 flea-allergic dog sera in an enhanced chemiluminescent assay for canine IgE antibodies. At least 15 different flea components in the molecular weight range of 14-150 K bound IgE and every serum demonstrated a different pattern of binding. Three of the components with apparent molecular weights of 25, 40 and 58 K were each bound by at least 40% of the sera. No reactivity was seen when normal dog sera were used. These results demonstrate a greater number of flea allergens and a far greater diversity of the IgE antibody response to flea allergens than has previously been described, and suggest that immediate hypersensitivity may be an important mechanism in the pathogenesis of canine flea allergy.

Electroimmunoblotting of myelin basic protein peptides: a novel approach to the rapid characterisation of antigenic specificities of monoclonal and polyclonal anti-MBP antibodies.

A rapid and sensitive method for the identification of antigenic determinants recognised by monoclonal and polyclonal antibodies directed against myelin basic protein (MBP) is described. By electroimmunoblotting a series of overlapping peptides covering the entire MBP molecule with monoclonal anti-MBP antibodies, the binding pattern of immunoreactive peptides can be rapidly determined and the reactive antigenic determinant identified. This procedure, which can be performed with both native and synthetic peptides, can also with appropriate modification, be applied to the analysis of naturally occurring or experimentally induced polyclonal anti-MBP autoantibodies.