Dermatophagoides pteronyssinus and Tyrophagus putrescentiae allergy in allergic rhinitis caused by cross-reactivity not dual-sensitization.
Tyrophagus putrescentiae and Dermatophagoides pteronyssinus are causative factors for the development of airway hypersensitivity. The main objective in this study was to identify the cross-reactive allergens between T. putrescentiae and D. pteronyssinus and investigate their sensitization in patients with allergic rhinitis. The prevalence of sensitization to mites was determined by skin prick tests and histamine release assays. Both immunoblot and ELISA inhibition assays were performed by using the recombinant allergens of T. putrescentiae and D. pteronyssinus. The cross-reactive allergens were identified by using IgE-binding inhibition analysis. The correlations of specific IgE between T. putrescentiae and D. pteronyssinus to group 2 and group 3 mite allergens were compared. A total of 117 allergic rhinitis patients, aged between 16 and 40 years old were recruited to be included in this study. The results showed that 70% (82/117) of allergic rhinitis subjects had skin test positive reactions to D. pteronyssinus or T. putrescentiae. Among these mite-sensitive subjects, there were 81 subjects (81/82) sensitive to D. pteronyssinus and 34 subjects (34/82) sensitive to T. putrescentiae. Among the T. putrescentiae hypersensitive subjects, 97% (33/34) were also sensitized to D. pteronyssinus. In the IgE-binding inhibition analysis, 59% (13/22) subjects had IgE-binding activity of T. putrescentiae that was completely absorbed by D. pteronyssinus, especially components with MW at 16 kDa. In ELISA inhibition testing, 69% of IgE-binding was inhibited by rTyr p 2, and 45% inhibited by rTyr p 3. The titers of IgE antibodies to rTyr p 2 and rDer p 2 were well correlated, but not rTyr p 3 and rDer p 3. In conclusion, most T. putrescentiae sensitized subjects were also sensitized to D. pteronyssinus in young adult allergic rhinitis patients. The complete absorption of IgE binding activity by D. pteronyssinus indicates that T. putrescentiae hypersensitivity might be due to the cross-reactivity, not dual-sensitization of D. pteronyssinus and T. putrescentiae. The IgE-binding titers of group 2 allergens were well correlated and the binding activity of Tyr p 2 could be absorbed by Der p 2, suggesting that group 2 allergens are the major cross-reactive allergen of D. pteronyssinus and T. putrescentiae.
Liao
En-Chih
EC
Institute of Clinical Medicine, National Yang Ming University, Taipei, Taiwan.
Ho
Chau-Mei
CM
Lin
Meei-Yn
MY
Tsai
Jaw-Ji
JJ
D000293:Adolescent; D000328:Adult; D000818:Animals; D039741:Antigens, Dermatophagoides / Q000276:immunology*; D060829:Arthropod Proteins; D003429:Cross Reactions; D040002:Dermatophagoides pteronyssinus / Q000276:immunology*; D006636:Histamine Release; D006801:Humans; D007114:Immunization; D007073:Immunoglobulin E / Q000378:metabolism*; D015995:Prevalence; D011485:Protein Binding / Q000276:immunology; D011506:Proteins / Q000276:immunology*; D012221:Rhinitis, Allergic, Perennial / Q000175:diagnosis / Q000453:epidemiology / Q000276:immunology*; D012882:Skin Tests
D039741:Antigens, Dermatophagoides; D060829:Arthropod Proteins; C451163:Dermatophagoides pteronyssinus antigen p 2; D011506:Proteins; C110921:Tyr p 2 protein, Tyrophagus putrescentiae; D007073:Immunoglobulin E