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Influence of plant lipids on immune responses in mice to the major Brazil nut allergen Ber e 1
Author(s) -
Dearman R. J.,
Alcocer M. J. C.,
Kimber I.
Publication year - 2007
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.2007.02689.x
Subject(s) - immunoglobulin e , antibody , recombinant dna , lipopolysaccharide , immune system , biology , immunology , allergen , adjuvant , chemistry , microbiology and biotechnology , allergy , biochemistry , gene
Summary Background Lipids, particularly bacterial lipopolysaccharide, can impact on immune responses to proteins, with low doses enhancing type 2 responses. Objective We have examined the influence of natural plant lipid extracts on antibody responses provoked in mice by recombinant Ber e 1, the major allergen in Brazil nuts. Methods BALB/c strain mice were immunized (by intraperitoneal injection) with natural or recombinant Ber e l produced in Pichia pastoris and admixed with various lipid fractions isolated from Brazil nuts. Serum samples were analysed for specific IgE antibody by homologous passive cutaneous anaphylaxis assay and for IgG by enzyme‐linked immunosorbant assay. Results Exposure to recombinant (lipid‐free) Ber e 1 alone failed to induce detectable IgG or IgE antibody. Co‐administration of the total lipid fraction (with reduced triglyceride levels), sterol‐rich, or polar lipid fractions, resulted in marked adjuvant effects on IgG and IgE. However, the β‐sitosterol and glycolipid‐rich fractions were associated with only low‐level IgG antibody, and had little impact on IgE antibody production. Natural Ber e 1 containing endogenous lipids also provoked IgG and IgE antibody responses. Identical IgE and IgG antibody responses were detected regardless of whether natural or recombinant Ber e 1 was used as substrates for analyses. Conclusion Endogenous Brazil nut lipids are required for the induction of optimal antibody responses to Ber e 1 in the BALB/c strain mouse. Appropriate antibody binding sites are present on both natural and recombinant forms of Ber e 1, suggesting that the impact of lipid is at the induction phase, rather than antibody recognition, and is possibly required for efficient antigen presentation.