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Updated: Jun 20, 2026
Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
Published on: January 3, 2012
Allergenicity of recombinant troponin C from Tyrophagus putrescentiae
Kyoung Yong Jeong1, Chung-ryul Kim, Sunjin Un
1Department of Environmental Medical Biology and Institute of Tropical Medicine, Korea National Arthropods of Medical Importance Resource Bank, Brain Korea 21 Project for Medical Science, Yonsei University College of Medicine, Seoul, Korea.
Background:
The storage mite, Tyrophagus putrescentiae, produces potent allergens, many of which have not been characterized. This study was undertaken to characterize the allergenicity of troponin C from T. putrescentiae.
Methods:
A cDNA encoding 17.7 kDa troponin C, with homology to cockroach allergen Bla g 6, was identified from T. putrescentiae-expressed sequence tags. Recombinant troponin C was expressed and IgE responses to the recombinant protein were assessed in the presence and absence of 10 mM CaCl(2). Cross-reactivity between T. putrescentiae troponin C and Bla g 6 was tested using an inhibition ELISA.
Results:
Recombinant T. putrescentiae troponin C shares 62.7-85.5% homology with troponin C from various arthropods. Sera from 5 of 47 subjects in our study group (10.6%) showed IgE binding to the recombinant protein. Interestingly, addition of 10 mM CaCl(2) increased the intensity of IgE binding approximately 2-fold. In an immune-inhibition ELISA with these sera, T. putrescetiae troponin C and Bla g 6 did not cross-react significantly.
Conclusions:
Troponin C is a new mite allergen with calcium-dependent IgE reactivity.
