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

Kyoung Yong Jeong; Myung Hee Yi; Mina Son; Dongpyo Lyu; Jae Hyun Lee; Tai Soon Yong; Jung Won Park

doi:10.1159/000444364

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

Kyoung Yong Jeong, Myung Hee Yi, Mina Son, Dongpyo Lyu, Jae Hyun Lee, Tai Soon Yong, Jung Won Park

Research output: Contribution to journal › Article

8 Citations (Scopus)

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.

Original language	English
Pages (from-to)	93-100
Number of pages	8
Journal	International Archives of Allergy and Immunology
Volume	169
Issue number	2
DOIs	https://doi.org/10.1159/000444364
Publication status	Published - 2016 Apr 1

All Science Journal Classification (ASJC) codes

Immunology and Allergy
Immunology

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Jeong, K. Y., Yi, M. H., Son, M., Lyu, D., Lee, J. H., Yong, T. S., & Park, J. W. (2016). IgE Reactivity of Recombinant Pac c 3 from the Asian Needle Ant (Pachycondyla chinensis). International Archives of Allergy and Immunology, 169(2), 93-100. https://doi.org/10.1159/000444364

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title = "IgE Reactivity of Recombinant Pac c 3 from the Asian Needle Ant (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.",

author = "Jeong, {Kyoung Yong} and Yi, {Myung Hee} and Mina Son and Dongpyo Lyu and Lee, {Jae Hyun} and Yong, {Tai Soon} and Park, {Jung Won}",

year = "2016",

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doi = "10.1159/000444364",

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AU - Jeong, Kyoung Yong

AU - Yi, Myung Hee

AU - Son, Mina

AU - Lyu, Dongpyo

AU - Lee, Jae Hyun

AU - Yong, Tai Soon

AU - Park, Jung Won

PY - 2016/4/1

Y1 - 2016/4/1

N2 - 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.

AB - 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.

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