Expression in escherichia coli and purification of folded rDer p 20, the arginine kinase from dermatophagoides pteronyssinus: A possible biomarker for allergic asthma


  • Sarzsinszky E.
  • Lupinek C.
  • Vrtala S.
  • Huang H.J.
  • Hofer G.
  • Keller W.
  • Chen K.W.
  • Panaitescu C.B.
  • Resch-Marat Y.
  • Zieglmayer P.
  • Zieglmayer R.
  • Lemell P.
  • Horak F.
  • Duchêne M.
  • Valenta R.
Дата публикации:01.01.2021
Журнал: Allergy, Asthma and Immunology Research
БД: Scopus
Ссылка: Scopus

Аннтотация

Copyright © 2021 The Korean Academy of Asthma, Allergy and Clinical Immunology. 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.


Вернуться назад