Arginine kinase (AK) was first identified as an
allergen in the Indian-meal moth and subsequently shown to occur as
allergen in various invertebrates and shellfish. The
cDNA coding for AK from the house dust mite (HDM) species Dermatophagoides pteronyssinus, Der p 20, has been isolated, but no recombinant Der p 20 (rDer p 20)
allergen has been produced and characterized so far. We report the expression of Der p 20 as
recombinant protein in Escherichia coli. rDer p 20 was purified and shown to be a monomeric, folded
protein by size exclusion chromatography and circular dichroism spectroscopy, respectively. Using AK-specific
antibodies, Der p 20 was found to occur mainly in HDM bodies, but not in fecal particles. Thirty percent of clinically well-characterized HDM allergic patients (n = 98) whose
immunoglobulin E (
IgE) reactivity profiles had been determined with an extensive panel of purified HDM
allergens (
Der f 1, 2;
Der p 1, 2, 4, 5, 7, 10, 11, 14, 15, 18, 21, 23 and 37) showed
IgE reactivity to Der p 20.
IgE reactivity to Der p 20 was more frequently associated with lung symptoms. AKs were detected in several invertebrates with specific
antibodies and Der p 20 showed
IgE cross-reactivity with AK from shrimp (Litopenaeus vannamei). Thus, Der p 20 is a cross-reactive HDM
allergen and may serve as a diagnostic marker for HDM-induced lung symptoms such as
asthma.