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IgE Reactivity of Recombinant Pac c 3 from the Asian Needle Ant (Pachycondyla chinensis).

Authors
 Kyoung Yong Jeong  ;  Myung-hee Yi  ;  Mina Son  ;  Dongpyo Lyu  ;  Jae-Hyun Lee  ;  Tai-Soon Yong  ;  Jung-Won Park 
Citation
 International Archives of Allergy and Immunology, Vol.169(2) : 93-100, 2016 
Journal Title
 International Archives of Allergy and Immunology 
ISSN
 1018-2438 
Issue Date
2016
MeSH
Adult ; Allergens/immunology* ; Amino Acid Sequence ; Anaphylaxis/blood ; Anaphylaxis/immunology* ; Animals ; Ants/immunology* ; Case-Control Studies ; Cross Reactions/immunology ; Female ; Humans ; Immunoglobulin E/blood ; Immunoglobulin E/immunology* ; Insect Bites and Stings ; Insect Proteins/chemistry ; Insect Proteins/immunology* ; Male ; Middle Aged ; Molecular Sequence Data ; Recombinant Proteins/chemistry ; Recombinant Proteins/immunology* ; Sequence Alignment ; Young Adult
Keywords
Ant sting anaphylaxis ; Antigen 5 ; Pac c 3 ; Pachycondyla chinensis
Abstract
BACKGROUND: Stings from the Asian needle ant are an important cause of anaphylaxis in East Asia. A 23-kDa protein homologous to antigen 5 is the major allergen produced by these ants. In this study, we aimed to produce a recombinant antigen 5 allergen, Pac c 3. METHODS: Recombinant Pac c 3 allergen from the Asian needle ant was expressed in Pichia pastoris and purified by ammonium sulfate precipitation and Ni affinity chromatography. IgE reactivity was demonstrated by ELISA and immunoblotting. RESULTS: The recombinant protein was recognized in 5 of 6 (83.3%) serum samples from patients with demonstrated anaphylaxis to ants. IgE reactivity to an antigen 5 allergen from Asian needle ant venom sac extract was specifically inhibited by the recombinant protein. It was also able to inhibit IgE binding to the vespid allergen Ves v 5 by ImmunoCAP analysis, indicating the presence of cross-reactivity. CONCLUSION: A recombinant Pac c 3, cross-reactive with Ves v 5, from the Asian needle ant was successfully produced in the methylotrophic yeast P. pastoris. This protein could be useful for the development of component-resolved diagnostics.
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/146790
DOI
10.1159/000444364
Appears in Collections:
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실)
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실)
1. Journal Papers (연구논문) > 5. Research Institutes (연구소) > Institute of Allergy (알레르기연구소)
Yonsei Authors
박중원(Park, Jung Won) ; 용태순(Yong, Tai Soon) ; 이명희(Yi, Myung Hee) ; 이재현(Lee, Jae Hyun) ; 정경용(Jeong, Kyoung Yong)
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http://www.karger.com/Article/FullText/444364
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