Lipocalin-type prostaglandin D synthase and egg white cystatin react with IgE antibodies from children with egg allergy

Makiko Suzuki, Hidehiko Fujii, Hidetsugu Fujigaki, Shinji Shinoda, Kanako Takahashi, Kuniaki Saito, Hisayasu Wada, Masumi Kimoto, Naomi Kondo, Mitsuru Seishima

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Background: Ovalbumin, ovomucoid, ovotransferrin, lysozyme, and ovomucin are known to be major allergens found in egg white. Egg white protein is composed of over 30 proteins; many of which have neither been identified nor their allergenicities characterized. This study set out to analyze whether unknown proteins that bind to IgE antibodies in serum from patients with egg allergy exist in egg white. Methods: Diluted egg white proteins were separated by 2-dimensional (2-D) gel electrophoresis. Immunola-beling was performed on individual patient sera from 19 child patients with egg white allergy and 11 negative control subjects. Spots of egg white proteins that bound to the patients' IgE were identified by mass spectrometry-based proteomics. Results: Egg white proteins were separated into 63 spots. Twenty-five of the 63 reacted with egg allergy patients' sera, and 10 of the 25 reactive spots showed IgE-reactivity to controls as well. Specific bindings to the IgE from egg allergy patients were found in 15 spots; one of which was confirmed as ovotransferrin. Among the other 14 protein spots, egg white cystatin and lipocalin-type prostaglandin D synthase (L-PGDS) were newly identified proteins that reacted with IgE in patients with egg allergy. Conclusions: We demonstrated that L-PGDS and cystatin reacted with serum IgE in patients with egg allergy. Our proteomics-based analysis in egg white gives a comprehensive map of proteins bound with IgE and should assist in enabling more accurate diagnoses and recommendations of desensitizing treatments for individual patients.

Original languageEnglish
Pages (from-to)175-183
Number of pages9
JournalAllergology International
Volume59
Issue number2
DOIs
Publication statusPublished - 01-01-2010
Externally publishedYes

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prostaglandin R2 D-isomerase
Egg Hypersensitivity
Lipocalins
Immunoglobulin E
Egg Proteins
Antibodies
Egg White
Conalbumin
Ovomucin
Proteins
Serum
Proteomics
Cystatins
egg-white cystatin
Ovalbumin
Electrophoresis, Gel, Two-Dimensional
Muramidase

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy

Cite this

Suzuki, Makiko ; Fujii, Hidehiko ; Fujigaki, Hidetsugu ; Shinoda, Shinji ; Takahashi, Kanako ; Saito, Kuniaki ; Wada, Hisayasu ; Kimoto, Masumi ; Kondo, Naomi ; Seishima, Mitsuru. / Lipocalin-type prostaglandin D synthase and egg white cystatin react with IgE antibodies from children with egg allergy. In: Allergology International. 2010 ; Vol. 59, No. 2. pp. 175-183.
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Lipocalin-type prostaglandin D synthase and egg white cystatin react with IgE antibodies from children with egg allergy. / Suzuki, Makiko; Fujii, Hidehiko; Fujigaki, Hidetsugu; Shinoda, Shinji; Takahashi, Kanako; Saito, Kuniaki; Wada, Hisayasu; Kimoto, Masumi; Kondo, Naomi; Seishima, Mitsuru.

In: Allergology International, Vol. 59, No. 2, 01.01.2010, p. 175-183.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Lipocalin-type prostaglandin D synthase and egg white cystatin react with IgE antibodies from children with egg allergy

AU - Suzuki, Makiko

AU - Fujii, Hidehiko

AU - Fujigaki, Hidetsugu

AU - Shinoda, Shinji

AU - Takahashi, Kanako

AU - Saito, Kuniaki

AU - Wada, Hisayasu

AU - Kimoto, Masumi

AU - Kondo, Naomi

AU - Seishima, Mitsuru

PY - 2010/1/1

Y1 - 2010/1/1

N2 - Background: Ovalbumin, ovomucoid, ovotransferrin, lysozyme, and ovomucin are known to be major allergens found in egg white. Egg white protein is composed of over 30 proteins; many of which have neither been identified nor their allergenicities characterized. This study set out to analyze whether unknown proteins that bind to IgE antibodies in serum from patients with egg allergy exist in egg white. Methods: Diluted egg white proteins were separated by 2-dimensional (2-D) gel electrophoresis. Immunola-beling was performed on individual patient sera from 19 child patients with egg white allergy and 11 negative control subjects. Spots of egg white proteins that bound to the patients' IgE were identified by mass spectrometry-based proteomics. Results: Egg white proteins were separated into 63 spots. Twenty-five of the 63 reacted with egg allergy patients' sera, and 10 of the 25 reactive spots showed IgE-reactivity to controls as well. Specific bindings to the IgE from egg allergy patients were found in 15 spots; one of which was confirmed as ovotransferrin. Among the other 14 protein spots, egg white cystatin and lipocalin-type prostaglandin D synthase (L-PGDS) were newly identified proteins that reacted with IgE in patients with egg allergy. Conclusions: We demonstrated that L-PGDS and cystatin reacted with serum IgE in patients with egg allergy. Our proteomics-based analysis in egg white gives a comprehensive map of proteins bound with IgE and should assist in enabling more accurate diagnoses and recommendations of desensitizing treatments for individual patients.

AB - Background: Ovalbumin, ovomucoid, ovotransferrin, lysozyme, and ovomucin are known to be major allergens found in egg white. Egg white protein is composed of over 30 proteins; many of which have neither been identified nor their allergenicities characterized. This study set out to analyze whether unknown proteins that bind to IgE antibodies in serum from patients with egg allergy exist in egg white. Methods: Diluted egg white proteins were separated by 2-dimensional (2-D) gel electrophoresis. Immunola-beling was performed on individual patient sera from 19 child patients with egg white allergy and 11 negative control subjects. Spots of egg white proteins that bound to the patients' IgE were identified by mass spectrometry-based proteomics. Results: Egg white proteins were separated into 63 spots. Twenty-five of the 63 reacted with egg allergy patients' sera, and 10 of the 25 reactive spots showed IgE-reactivity to controls as well. Specific bindings to the IgE from egg allergy patients were found in 15 spots; one of which was confirmed as ovotransferrin. Among the other 14 protein spots, egg white cystatin and lipocalin-type prostaglandin D synthase (L-PGDS) were newly identified proteins that reacted with IgE in patients with egg allergy. Conclusions: We demonstrated that L-PGDS and cystatin reacted with serum IgE in patients with egg allergy. Our proteomics-based analysis in egg white gives a comprehensive map of proteins bound with IgE and should assist in enabling more accurate diagnoses and recommendations of desensitizing treatments for individual patients.

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U2 - 10.2332/allergolint.09-OA-0121

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