DERP5 Protein, Dermatophagoides pteronyssinus (His)

The DERP5 protein exhibits a monomeric structure and further forms a trimer of homodimers, oligomerizing in a concentration-dependent manner. Notably, DERP5 is implicated in causing allergic reactions in humans, with common symptoms of mite allergy including bronchial asthma, allergic rhinitis, and conjunctivitis. It binds to IgE in individuals allergic to house dust mite (HDM), as evidenced by various studies. Recombinant DERP5 protein demonstrates IgE binding in a significant percentage of patients tested across different populations. Moreover, skin tests with the recombinant protein result in positive reactions in patients with asthma and allergic rhinitis. Importantly, DERP5 does not exhibit relevant cross-reactivity with the Der p 21 allergen. Additionally, DERP5 induces histamine release from human peripheral blood mononuclear leukocytes and up-regulates the expression of the CD203c activation marker on basophils. These findings underscore DERP5's role in allergic responses and its potential significance in understanding and managing mite-induced allergic conditions.