Type I skin reactivity to native and recombinant phospholipase A from honeybee venom is similar

Müller, Ulrich; Dudler, Thomas; Schneider, Theres; Crameri, Reto; Fischer, H.; Skrbic, Dejan; Maibach, Rudolf; Blaser, Kurt; Suter, Mark

doi:10.1016/s0091-6749(95)70059-5

Cited by 79 publications

(50 citation statements)

References 30 publications

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“…The evaluation of' recombinant allergens should ideally demonstrate 1) IgE-binding capacity (14,15) 2) ability to stimulate specific T cells (16) 3) capacity to induce specific basophil degranulation (17) 4) induction of IgE responses in experimental animal systems (18-20) 5) induction of skin reactivity in man (21)(22)(23)(24)(25)(26).…”

Section: Strategies For Obtaining Recombinant Allergensmentioning

confidence: 99%

Recombinant allergens

Valenta

Vrtala

Laffer

et al. 1998

Allergy

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A great variety of recombinant plant, mite, mold, mammal, and insect allergens have been expressed in heterologous hosts (e.g., Escherichia coli), their cDNA being used as a template. The number of biologically active recombinant allergens available for experimental, diagnostic, and therapeutic purposes is increasing tremendously. Recombinant allergens have proven to be valuable tools to investigate T‐cell and B‐cell recognition of allergens as well as to study mechanisms of specific IgE regulation. The immunologic equivalence of many relevant recombinant allergens with their natural counterparts has been demonstrated, and the three‐dimensional structures of several recombinant allergens have been described recently. As a result of extensive cross‐reactivities among the relevant allergens, it appears that the number of epitopes needed for diagnosis and specific immunotherapy is less diverse than originally anticipated and might be soon covered by recombinant molecules. Recombinant allergens have been used for successful in vitro, as well as in vivo, allergy diagnosis, and work is in progress to produce recombinant allergen derivatives with reduced anaphylactic potential to improve current forms of immunotherapy.

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Section: Strategies For Obtaining Recombinant Allergensmentioning

confidence: 99%

Recombinant allergens

Valenta

Vrtala

Laffer

et al. 1998

Allergy

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“…PLA represents the major antigen and allergen in individuals sensitized to bee sting and can induce both allergy and normal immunity (13,14). Normally, at an initial response to bee sting, low-affinity IgG1 anti-PLA antibodies are elicited (4).…”

Section: Introductionmentioning

confidence: 99%

“…Repeated exposure to BV generates high-affinity IgG4 anti-PLA antibodies (4,15,16). In contrast, individuals allergic to bee sting develop excessive IgE antibodies mainly to PLA (13,14).…”

Section: Introductionmentioning

confidence: 99%

Role of interleukin 10 in specific immunotherapy.

Akdiş¹,

Blesken²,

Akdiş³

et al. 1998

J. Clin. Invest.

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882

846

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The induction of allergen-specific anergy in peripheral T cells represents a key step in specific immunotherapy (SIT). Here we demonstrate that the anergic state results from increased IL-10 production. In bee venom (BV)-SIT the specific proliferative and cytokine responses against the main allergen, the phospholipase A 2 (PLA), and T cell epitopecontaining PLA peptides were significantly suppressed after

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“…Accordingly, the vaccine should be formulated in such a way that it does not carry any risk of side effects due to IgE cross-linking on mast cells and basophils. The Api m (1/2/3) chimeric protein is comprised of fragments of major BV allergens Api m 1, Api m 2 and Api m 3 [4,5]. The three-dimensional structures of BV allergens Api m 1 and Api m 2 are stabilized by intra-chain cysteine disulfide bridges in their native forms [12,14].…”

Section: Discussionmentioning

confidence: 99%

“…Phospholipase A 2 (Api m 1) and hyaluronidase (Api m 2) represent major allergens in BV [4,5]. The cytolytic peptide melittin (Api m 3) with potent pharmacological activity is the major component in BV and is possibly responsible for many of the side effects in BV allergen immunotherapy.…”

Section: Introductionmentioning

confidence: 99%

Prevention of allergy by a recombinant multi-allergen vaccine with reduced IgE binding and preserved T cell epitopes

Karamloo¹,

Schmid‐Grendelmeier

Kussebi³

et al. 2005

Eur. J. Immunol.

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Novel approaches for the prevention of allergy are required, because of the inevitably increasing prevalence of allergic diseases during the last 30 years. Here, a recombinant chimeric protein, which comprises the whole amino acid sequences of three bee venom major allergens has been engineered and used in prevention of bee venom sensitization in mice. Phospholipase A 2 (Api m 1), hyaluronidase (Api m 2) and melittin (Api m 3) fragments with overlapping amino acids were assembled in a different order in the Api m (1/2/3) chimeric protein, which preserved entire T cell epitopes, whereas B cell epitopes of all three allergens were abrogated. Accordingly, IgE cross-linking leading to mast cell and basophil mediator release was profoundly reduced in humans. Supporting these findings, the Api m (1/2/3) induced 100 to 1000 times less type-1 skin test reactivity in allergic patients. Treatment of mice with Api m (1/2/3) led to a significant reduction of specific IgE development towards native allergen, representing a protective vaccine effect in vivo. These results demonstrate a novel prototype of a preventive allergy vaccine, which preserves the entire T cell epitope repertoire, but bypasses induction of IgE against native allergen, and side effects related to mast cell/basophil IgE FceRI cross-linking in sensitized individuals.

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Type I skin reactivity to native and recombinant phospholipase A from honeybee venom is similar

Cited by 79 publications

References 30 publications

Recombinant allergens

Recombinant allergens

Role of interleukin 10 in specific immunotherapy.

Prevention of allergy by a recombinant multi-allergen vaccine with reduced IgE binding and preserved T cell epitopes

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