| 1. |
- Rytkonen, J., et al.
(författare)
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BCG vaccine modulates intestinal and systemic response to ß-lactoglobulin
- 2004
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Ingår i: Pediatric Allergy and Immunology. - : Wiley. - 0905-6157 .- 1399-3038. ; 15:5, s. 408-414
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Tidskriftsartikel (refereegranskat)abstract
- ß-Lactoglobulin (BLG) is a clinically important antigen in cow's milk and one of the major allergens causing cow's milk allergy. Bacillus Calmette-Guérin (BCG) vaccination has been suggested to modify immune response possibly decreasing the risk of allergy to some antigens in both human and experimental animals. In the present study, we have analyzed whether the early BCG vaccination has any effect on the markers of systemic and gastrointestinal (GI) sensitization to BLG. We immunized two groups of Hooded-Lister rat puppets with intraperitoneal injections of native BLG at 43 and 62 days with pertussis vaccine as adjuvant, one group receiving additionally BCG. The animals were then fed native and denatured milk products twice weekly from 73 to 131 days of age, when they were killed. Control group was not vaccinated and received normal rat forage. Total immunoglobulin E (IgE) levels and BLG-specific IgG1 and IgG2a concentrations were determined in serum samples. Spontaneous interleukin (IL)-4 and interferon (IFN)-? production from duodenal specimens were measured, and the inflammatory cells were quantitated in specimens from different sections of the GI tract. Administration of BCG simultaneously with BLG resulted in reduced IgE concentration in serum, while the specific IgG1 and IgG2a antibody responses and the spontaneous secretion of IL-4 and IFN-? were not affected. Furthermore, BCG-induced eosinophilic infiltration and increase of intraepithelial lymphocytes (IEL) in the GI mucosa, and a trend toward increased number of lamina propria mononuclear inflammatory cells in the colon (BCG compared with BLG, p = 0.09, BCG compared with controls, p = 0.02). Controls showed increment of IgG1 response in comparison with the BLG group (p = 0.04) and increase of mucosal eosinophilic infiltration. The BCG modified the response to BLG both at the systemic level as shown by decrease of total IgE and at GI mucosa where increase of eosinophilic infiltration and increased number of IEL were seen. Increment of IgG1 level and eosinophils in the controls might be related with the lack of modulatory effect of pertussis vaccination. A shift of response toward the lower GI tract after BCG immunization as shown by a trend for increase of mononuclear inflammatory cells in colon lamina propria mimics disease development in some cases of clinical food allergy, and emphasizes the need for evaluation of the changes in the whole GI tract in food allergy models.
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| 2. |
- Suutari, T. J., et al.
(författare)
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IgE cross reactivity between reindeer and bovine milk beta-lactoglobulins in cow's milk allergic patients
- 2006
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Ingår i: J Investig Allergol Clin Immunol. - 1018-9068. ; 16:5, s. 296-302
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Tidskriftsartikel (refereegranskat)abstract
- BACKGROUND: Allergic reactions to cow's milk are common in small children. One of the main protein allergens found in cow's milk is beta-lactoglobulin (beta-Lg). Reindeer and bovine milk both contain related beta-Lg proteins, but the allergenicity of reindeer beta-Lg has not previously been studied. The purpose of this study was to analyze the immunological cross-reactivity of IgE antibodies from children with cow's milk allergy to reindeer and bovine beta-Lg. METHODS: Sera from 17 children and a serum pool of 4 patients with elevated cow's milk-specific IgE were investigated. Beta-Lg from bovine and reindeer milk was isolated in native form and an enzyme-linked immunosorbent inhibition assay was developed. Bovine beta-Lg was used as a capturing antigen and the inhibiting effects of reindeer and bovine beta-Lg on the IgE binding were measured. RESULTS: Cross-reactivity patterns of bovine milk beta-Lg specific IgE to reindeer beta-Lg varied among patients. In general, reindeer beta-Lg showed significantly lower inhibition (mean 43%) of IgE binding to the capturing antigen than did bovine beta-Lg (mean 89%). In some patients, even high concentrations of reindeer beta-Lg only partly eliminated the IgE binding to bovine beta-Lg. CONCLUSIONS: The partial cross-reactivity of human anti-bovine IgE with reindeer beta-Lg suggests that it lacks important bovine epitopes and those that are recognized are only weakly bound.
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| 3. |
- Suutari, T.J., et al.
(författare)
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IgE cross reactivity between reindeer and bovine milk ?-lactoglobulins in cow's milk allergic patients
- 2006
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Ingår i: Journal of investigational allergology & clinical immunology. - 1018-9068 .- 1698-0808. ; 16:5, s. 296-302
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Tidskriftsartikel (refereegranskat)abstract
- Background: Allergic reactions to cow's milk are common in small children. One of the main protein allergens found in cow's milk is ?-lactoglobulin (?-Lg). Reindeer and bovine milk both contain related ?-Lg proteins, but the allergenicity of reindeer ?-Lg has not previously been studied. The purpose of this study was to analyze the immunological cross-reactivity of IgE antibodies from children with cow's milk allergy to reindeer and bovine ?-Lg. Methods: Sera from 17 children and a serum pool of 4 patients with elevated cow's milk-specific IgE were investigated. ?-Lg from bovine and reindeer milk was isolated in native form and an enzyme-linked immunosorbent inhibition assay was developed. Bovine ?-Lg was used as a capturing antigen and the inhibiting effects of reindeer and bovine ?-Lg on the IgE binding were measured. Results: Cross-reactivity patterns of bovine milk ?-Lg specific IgE to reindeer ?-Lg varied among patients. In general, reindeer ?-Lg showed significantly lower inhibition (mean 43%) of IgE binding to the capturing antigen than did bovine ?-Lg (mean 89%). In some patients, even high concentrations of reindeer ?-Lg only partly eliminated the IgE binding to bovine ?-Lg. Conclusions: The partial cross-reactivity of human anti-bovine IgE with reindeer ?-Lg suggests that it lacks important bovine epitopes and those that are recognized are only weakly bound. © 2006 Esmon Publicidad.
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