DETECTION AND CHARACTERIZATION OF ANTIBODIES SPECIFIC TO FOOD ANTIGENS (GLIADIN, OVALBUMIN AND BETA-LACTOGLOBULIN) IN HUMAN SERUM, SALIVA, COLOSTRUM AND MILK

Citation
M. Rumbo et al., DETECTION AND CHARACTERIZATION OF ANTIBODIES SPECIFIC TO FOOD ANTIGENS (GLIADIN, OVALBUMIN AND BETA-LACTOGLOBULIN) IN HUMAN SERUM, SALIVA, COLOSTRUM AND MILK, Clinical and experimental immunology, 112(3), 1998, pp. 453-458
Citations number
25
Categorie Soggetti
Immunology
ISSN journal
00099104
Volume
112
Issue
3
Year of publication
1998
Pages
453 - 458
Database
ISI
SICI code
0009-9104(1998)112:3<453:DACOAS>2.0.ZU;2-V
Abstract
Antibodies against food antigens are usually produced in healthy peopl e. This humoral response can be detected both in serum and secretions. The characterization of this response can be useful for a better unde rstanding of food-related immunological alterations. In this study, Ig A and Ige antibodies specific to ovalbumin, P-lactoglobulin or gliadin were measured in serum, saliva, colostrum and milk from 40 healthy br east-feeding women. Specific IgA and IgG to the three antigens were me asured by indirect ELISA. Specific IgG levels were highest in serum an d very low in the other biological fluids. No correlation between the IgG specific to the different antigens was found. Specific IgA reactiv ity was found in all the samples analysed. Levels observed were higher in colostrum and milk than in serum and saliva. In spite of being thr ee different unrelated food antigens, a correlation between the levels of specific IgA was found in saliva, colostrum and milk samples of al l subjects studied. The specificity of IgA anti-gliadin antibodies fro m serum, saliva and colostrum was analysed by immunoblotting of SDS-PA GE-separated wheat proteins. Each sample presented a unique pattern of recognition. No common pattern of recognition was found either among the same biological fluids of the different subjects tested, or among the different samples-either serum, colostrum or saliva-of the same in dividual. Different degrees of specificity to wheat proteins among IgA from colostrum, saliva or serum were observed, suggesting that the lo cal IgA-producing populations are functionally different in the differ ent tissues of the organism.