Objective—To assess whether dogs with experimentally induced type I hypersensitivity against soy protein would respond to soy hydrolysate and develop cutaneous or gastrointestinal tract reactions after intradermal and oral challenge exposure.
Animals—12 naïve Beagle pups (9 sensitized and 3 control dogs).
Procedure—9 dogs were sensitized against soy protein by administration of allergens during a 90-day period. After the sensitization period, serum concentrations of soy-specific IgE were determined and an intradermal test was performed to confirm the dogs were sensitized against soy protein. An intradermal challenge test and an oral challenge test with native and hydrolyzed soy protein were conducted on 6 sensitized and 2 control dogs.
Results—High serum concentrations of soy-specific IgE and positive results for the intradermal test were observed for the 9 sensitized dogs after completion of the sesitization process. Sensitized dogs challenge exposed with hydrolyzed soy protein had a reduced inflammatory response after intradermal injection and no clinical response after an oral challenge exposure, compared with responses after intradermal and oral challenge exposure with native soy protein.
Conclusions and Clinical Relevance—Soy-sensitized dogs did not respond to oral administration of hydrolyzed soy protein. Thus, hydrolyzed soy protein may be useful in diets formulated for the management of dogs with adverse reactions to food.
Objective—To assess binding of IgE to native, whole hydrolyzed, and separated hydrolyzed fractions of soy protein in serum obtained from dogs with experimentally induced soy protein hypersensitivity.
Animals—8 naïve Beagles (6 experimentally sensitized to native soy protein and 2 control dogs).
Procedures—6 dogs were sensitized against soy protein by administration of allergens during a 90-day period. After the sensitization protocol was completed, serum concentrations of soy-specific IgE were measured and intradermal skin tests were performed in all 6 dogs to confirm that the dogs were sensitized against soy protein. Serum samples from each sensitized and control dog underwent western blot analysis to assess the molecular mass band pattern of the different allergenic soy fractions and evaluate reactivities to native and hydrolyzed soy protein.
Results—In sera from sensitized dogs, a characteristic band pattern with 2 major bands (approx 75 and 50 kd) and 2 minor bands (approx 31 and 20 kd) was detected, whereas only a diffuse band pattern associated with whole hydrolyzed soy protein was detected in the most reactive dog. Reactivity was evident only for the higher molecular mass peptide fraction. In control dogs, no IgE reaction to native or hydrolyzed soy protein was detected.
Conclusions and Clinical Relevance—Data suggest that the binding of soy-specific IgE to the hydrolyzed soy protein used in the study was significantly reduced, compared with binding of soy-specific IgE to the native soy protein, in dogs with experimentally induced soy hypersensitivity.
Objective—To characterize eosinophil granulederived
proteins in cats.
Sample Population—Eosinophils collected via peritoneal
lavage from 2 cats.
Procedure—The cats were infested orally with
Toxocara canis eggs and subsequently challengeexposed
with T canis antigen injected IP to induce
peritoneal eosinophilia; eosinophils were collected via
peritoneal lavage. Eosinophil granule proteins were
acid-extracted, separated by gel-filtration chromatography,
and examined for their peroxidase, ribonuclease,
and bactericidal activities; the N-terminal
sequence of some of these proteins was determined
and compared with homologue proteins from other
Results—3 protein peaks were separated in the chromatogram.
The first peak had both peroxidase and
bactericidal activities. The second peak had ribonuclease
and bactericidal activities, and the N-terminal
sequence of the major protein was homologous with
that of proteins of the ribonuclease A superfamily,
including eosinophil ribonucleases from humans and
other animal species. The third protein peak had bactericidal
activity, and the N-terminal sequence of the
major protein was homologous with that of human
and murine major basic proteins.
Conclusions and Clinical Relevance—Results indicated
that feline eosinophil granules contain major
basic protein and eosinophil-associated ribonuclease
and the granule proteins have peroxidase, ribonuclease,
and bactericidal activities. In cats, characterization
of eosinophil granule proteins may be useful in
elucidation of the mechanism of tissue damage in
eosinophil-associated diseases and development of
new treatment options for those diseases. In addition,
the identification of conserved structure and
function of eosinophil granule proteins in cats is relevant
from an evolutionary viewpoint. ( Am J Vet Res 2004;65:957–963)