Publication: The minor house dust mite allergen Der p 13 is a fatty acid-binding protein and an activator of a TLR2-mediated innate immune response
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Issued Date
2016-10-01
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ISSN
13989995
01054538
01054538
Other identifier(s)
2-s2.0-84966351760
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Mahidol University
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SCOPUS
Bibliographic Citation
Allergy: European Journal of Allergy and Clinical Immunology. Vol.71, No.10 (2016), 1425-1434
Suggested Citation
P. Satitsuksanoa, M. Kennedy, D. Gilis, M. Le Mignon, N. Suratannon, W. T. Soh, J. Wongpiyabovorn, P. Chatchatee, M. Vangveravong, T. Rerkpattanapipat, A. Sangasapaviliya, S. Piboonpocanun, E. Nony, K. Ruxrungtham, A. Jacquet, Pattarawat Thantiworasit, Pinya Pulsawat, Tassalalpa Daengsuwan, Wannada Laisuan, Malinee Tongdee, Nizchapha Dchapaphapeaktak, Tadech Boonpiyathad The minor house dust mite allergen Der p 13 is a fatty acid-binding protein and an activator of a TLR2-mediated innate immune response. Allergy: European Journal of Allergy and Clinical Immunology. Vol.71, No.10 (2016), 1425-1434. doi:10.1111/all.12899 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/40719
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Title
The minor house dust mite allergen Der p 13 is a fatty acid-binding protein and an activator of a TLR2-mediated innate immune response
Author(s)
P. Satitsuksanoa
M. Kennedy
D. Gilis
M. Le Mignon
N. Suratannon
W. T. Soh
J. Wongpiyabovorn
P. Chatchatee
M. Vangveravong
T. Rerkpattanapipat
A. Sangasapaviliya
S. Piboonpocanun
E. Nony
K. Ruxrungtham
A. Jacquet
Pattarawat Thantiworasit
Pinya Pulsawat
Tassalalpa Daengsuwan
Wannada Laisuan
Malinee Tongdee
Nizchapha Dchapaphapeaktak
Tadech Boonpiyathad
M. Kennedy
D. Gilis
M. Le Mignon
N. Suratannon
W. T. Soh
J. Wongpiyabovorn
P. Chatchatee
M. Vangveravong
T. Rerkpattanapipat
A. Sangasapaviliya
S. Piboonpocanun
E. Nony
K. Ruxrungtham
A. Jacquet
Pattarawat Thantiworasit
Pinya Pulsawat
Tassalalpa Daengsuwan
Wannada Laisuan
Malinee Tongdee
Nizchapha Dchapaphapeaktak
Tadech Boonpiyathad
Abstract
© 2016 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd Background: The house dust mite (HDM) allergen Der p 13 could be a lipid-binding protein able to activate key innate signaling pathways in the initiation of the allergic response. We investigated the IgE reactivity of recombinant Der p 13 (rDer p 13), its lipid-binding activities, and its capacity to stimulate airway epithelium cells. Methods: Purified rDer p 13 was characterized by mass spectrometry, circular dichroism, fluorescence-based lipid-binding assays, and in silico structural prediction. IgE-binding activity and allergenic potential of Der p 13 were examined by ELISA, basophil degranulation assays, and in vitro airway epithelial cell activation assays. Results: Protein modeling and biophysical analysis indicated that Der p 13 adopts a β-barrel structure with a predominately apolar pocket representing a potential binding site for hydrophobic ligands. Fluorescent lipid-binding assays confirmed that the protein is highly selective for ligands and that it binds a fatty acid with a dissociation constant typical of lipid transporter proteins. The low IgE-binding frequency (7%, n = 224) in Thai HDM-allergic patients as well as the limited propensity to activate basophil degranulation classifies Der p 13 as a minor HDM allergen. Nevertheless, the protein with its presumptively associated lipid(s) triggered the production of IL-8 and GM-CSF in respiratory epithelial cells through a TLR2-, MyD88-, NF-kB-, and MAPK-dependent signaling pathway. Conclusions: Although a minor allergen, Der p 13 may, through its lipid-binding capacity, play a role in the initiation of the HDM-allergic response through TLR2 activation.