Cross-reactivity studies of a new group 2 allergen from the dust mite Glycyphagus domesticus, Gly d 2, and group 2 allergens from Dermatophagoides pteronyssinus, Lepidoglyphus destructor, and Tyrophagus putrescentiae with recombinant allergens
G. Gafvelin et al., Cross-reactivity studies of a new group 2 allergen from the dust mite Glycyphagus domesticus, Gly d 2, and group 2 allergens from Dermatophagoides pteronyssinus, Lepidoglyphus destructor, and Tyrophagus putrescentiae with recombinant allergens, J ALLERG CL, 107(3), 2001, pp. 511-518
Background: Dust mites are important inducers of allergic disease. Group 2
allergens are recognized as major allergens in several mite species, includ
ing Dermatophagoides pteroronyssinus, Lepidoglyphus destructor, and Tyropha
gus putrescentiae. No allergens have thus far been characterized on the mol
ecular level from the dust mite Glycyphagus domesticus.
Objective: We sought to examine the cross-reactivity among group 2 allergen
s of G domesticus, L destructor, T putrescentiae, and D pteronyssinus.
Methods: A group 2 allergen from G domesticus, Gly d 2, was cloned and expr
essed as a recombinant protein. Cross-reactivity between Gly d 2 and 3 othe
r group 2 allergens, Lep d 2,Tyr p 2, and Der p 2, was studied by using ind
ividual sera and a serum pool RAST-positive to G domesticus, L destructor,
T putrescentiae, and D pteronyssinus. Recombinant allergens were used as in
hibitors of IgE binding in immunoblotting experiments. Molecular modeling o
n the basis of the Der p 2 structure was carried out for Gly d 2, Lep d 2,
and Tyr p 2.
Results: Two cDNAs encoding isoforms of Gly d 2 were isolated, but only the
Gly d 2.02 isoform was used in this study Sixteen of 17 subjects had IgE t
o Gly d 2. The protein sequence of Gly d 2 revealed 79% identity to Lep d 2
and 46% and 41% identity to Tyr p 2 and Der p 2, respectively. Extensive c
rossreactivity was demonstrated among Gly d 2, Lep d 2, and Tyr p 2, but li
ttle cross-reactivity was found between these allergens and Der p 2. Accord
ing to the tertiary structure of Der p 2 and 3-dimensional models of Gly d
2, Lep d 2, and Tyr p 2, differences reside mainly in surface-exposed resid
ues.
Conclusion: Gly d 2 showed high sequence homology to Lep d 2. Cross-reactiv
ity was observed between Gly d 2, Lep d 2, and Tyr p 2, but only limited cr
oss-reactivity was demonstrated between these 3 allergens and Der p 2.