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Cross-reactivity between IgE-binding proteins from Anisakis simplex and Dermatophagoides pteronyssinus
R Bernardini1, G Mistrello, E Novembre
1Pediatric Allergy and Pulmonary Center, Anna Meyer Children's Hospital, Department of Pediatrics, University of Florence, Italy. r.bernardini@meyer.it
International Journal of Immunopathology and Pharmacology
|January 4, 2006
Summary
Cross-reactivity between Anisakis simplex (As) and Dermatophagoides pteronyssinus (Dp) involves proteins of 35-50 kD and >100 kD. Tropomyosin (tr) was not found to be responsible for this cross-reaction in allergic patients.
Area of Science:
- Allergy and Immunology
- Parasitology
- Molecular Biology
Background:
- Sensitization to Anisakis simplex (As) and Dermatophagoides pteronyssinus (Dp) can coexist.
- Tropomyosin (tr) has been implicated as a potential cross-reactive protein between As and Dp.
Purpose of the Study:
- To confirm cross-reactivity between Dp and As.
- To investigate the role of tropomyosin (tr) in As-Dp cross-reactivity.
Main Methods:
- SDS-PAGE analysis of As and Dp extracts.
- IgE immunoblotting with patient serum.
- Immunoblotting inhibition assays using Dp extract and tr.
Main Results:
- Patient IgE recognized As antigens (25 kD, >100 kD, 35-50 kD, 20 kD) and Dp proteins (35-55 kD).
- Dp extract inhibited reactivity to As antigens (>100 kD, 35-50 kD) and As extract inhibited reactivity to Dp proteins (35-55 kD).
- Tropomyosin (tr) did not inhibit IgE binding, indicating it's not involved in the observed cross-reactivity.
Conclusions:
- Proteins with molecular weights of approximately 35-50 kD and greater than 100 kD mediate cross-reactivity between As and Dp.
- Tropomyosin (tr) is not a significant factor in the cross-reactivity between Anisakis simplex and Dermatophagoides pteronyssinus sensitization.
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