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Title: The House Dust Mite Major Allergen der p 23 Displays O-Glycan-Independent IgE Reactivities but No Chitin-Binding Activity
Authors: Wai Tuck Soh
Maxime Le Mignon
Narissara Suratannon
Pattraporn Satitsuksanoa
Pantipa Chatchatee
Jongkonnee Wongpiyaboron
Mukda Vangveravong
Ticha Rerkpattanapipat
Atik Sangasapaviliya
Emmanuel Nony
Surapon Piboonpocanun
Kiat Ruxrungtham
Alain Jacquet
Pattarawat Thantiworasit
Pinya Pulsawat
Tassalalpa Daengsuwan
Wannada Laisuan
Malinee Tongdee
Nizchapha Dchapaphapeaktak
Tadech Boonpiyathad
Chulalongkorn University
Division of Allergy and Immunology
Queen Sirikit National Institute of Child Health
Mahidol University
Phramongkutklao College of Medicine
King Chulalongkorn Memorial Hospital, Faculty of Medicine Chulalongkorn University
Children Hospital
Faculty of Medicine, Ramathibodi Hospital, Mahidol University
Keywords: Immunology and Microbiology
Issue Date: 1-Mar-2016
Citation: International Archives of Allergy and Immunology. Vol.168, No.3 (2016), 150-160
Abstract: © 2016 S. Karger AG, Basel. Background: The in-depth characterization of the recently identified house dust mite (HDM) major allergen Der p 23 requires the production of its recombinant counterpart because the natural allergen is poorly extractable from fecal pellets. This study aimed to provide a detailed physico-chemical characterization of recombinant Der p 23 (rDer p 23) as well as to investigate its IgE reactivity in a cohort of HDM-allergic patients from Thailand. Methods: Purified rDer p 23, secreted from recombinant Pichia pastoris, was characterized by mass spectrometry and circular dichroism analyses as well as for its chitin-binding activity. The IgE-binding frequency and allergenicity of Der p 23 were determined by ELISA and RBL-SX38 degranulation assays, respectively. Results: Purified intact rDer p 23 carried O-mannosylation and mainly adopted a random coil structure. Polyclonal antibodies to rDer p 23 can detect the corresponding natural allergen (nDer p 23) in aqueous fecal pellet extracts, suggesting that both forms of Der p 23 share common B-cell epitopes. Despite its homologies with chitin-binding proteins, both natural Der p 23 and rDer p 23 were unable to interact in vitro with chitin matrices. Of 222 Thai HDM-allergic patients tested, 54% displayed Der p 23-specific IgE responses. Finally, the allergenicity of rDer p 23 was confirmed by the degranulation of rat basophil leukemia cells. Conclusion: Our findings highlighted important levels of Der p 23 sensitizations in Thailand. Our study clearly suggested that rDer p 23 is likely more appropriate for HDM allergy component-resolved diagnosis than HDM extracts.
ISSN: 14230097
Appears in Collections:Scopus 2016-2017

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