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Component‐resolved diagnosis of vespid venom‐allergic individuals: phospholipases and antigen 5s are necessary to identify V espula or P olistes sensitization
Author(s) -
Monsalve R. I.,
Vega A.,
Marqués L.,
Miranda A.,
Fernández J.,
Soriano V.,
Cruz S.,
DomínguezNoche C.,
SánchezMorillas L.,
ArmisenGil M.,
Guspí R.,
Barber D.
Publication year - 2012
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1111/j.1398-9995.2011.02781.x
Subject(s) - venom , sensitization , antigen , allergy , immunology , phospholipase , chemistry , medicine , biochemistry , enzyme
Background Cross‐reactivity between hymenoptera species varies according to the different allergenic components of the venom. The true source of sensitization must therefore be established to ensure the efficacy of venom immunotherapy. Objective In the Mediterranean region, P olistes dominulus and V espula spp. are clinically relevant cohabitating wasps. A panel of major vespid venom allergens was used to investigate whether serum‐specific IgE ( sIgE ) could be used to distinguish sensitization to either vespid. Methods Fifty‐nine individuals with allergic reactions to vespid stings and positive I mmuno CAP and/or intradermal tests to vespid venoms were studied. sIgE against recombinant and natural venom components from each wasp species was determined using the ADVIA C entaur ® system. Results sIgE against recombinant antigen 5s sensitization to be detected in 52% of the patients tested (13/25). The sensitivity increased to 80% (20/25), when using natural antigen 5s, and to 100% with the complete panel of purified natural components, because the sIgE was positive to either the antigen 5s ( P ol d 5/ V es v 5) or to the phospholipases ( P ol d 1/ V es v 1) of the two vespids, or to both components at the same time. In 69% of cases, it was possible to define the most probable sensitizing insect, and in the rest, possible double sensitization could not be excluded. V espula hyaluronidase was shown to have no additional value as regards the specificity of the assay. Conclusions The major allergens of P . dominulus ’ and V espula vulgaris ’ venom, namely phoshpholipases and antigen 5s, are required to discriminate the probable sensitizing species in vespid‐allergic patients.