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Allergenic Characterization of 27-kDa Glycoprotein, a Novel Heat Stable Allergen, from the Pupa of Silkworm, Bombyx mori

Authors
 Kyoung Yong Jeong  ;  Mina Son  ;  June Yong Lee  ;  Kyung Hee Park  ;  Jae-Hyun Lee  ;  Jung-Won Park 
Citation
 Journal of Korean Medical Science, Vol.31(1) : 18-24, 2016 
Journal Title
 Journal of Korean Medical Science 
ISSN
 1011-8934 
Issue Date
2016
MeSH
Adolescent ; Adult ; Allergens/chemistry* ; Allergens/immunology* ; Amino Acid Sequence ; Animals ; Bombyx/chemistry* ; Bombyx/genetics ; Bombyx/growth & development ; Bombyx/immunology* ; Epitopes/immunology ; Female ; Food Hypersensitivity/etiology ; Glycoproteins/chemistry* ; Glycoproteins/genetics ; Glycoproteins/immunology* ; Hot Temperature ; Humans ; Immunoglobulin E/immunology ; Male ; Molecular Sequence Data ; Molecular Weight ; Proteomics ; Pupa/chemistry ; Pupa/immunology ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/immunology ; Sequence Alignment
Keywords
27-kDa Glycoprotein ; Allergens ; Bombyx mori ; Hemolymph
Abstract
Boiled silkworm pupa is a traditional food in Asia, and patients with silkworm pupa food allergy are common in these regions. Still now only one allergen from silkworm, arginine kinase, has been identified. The purpose of this study was to identify novel food allergens in silkworm pupa by analyzing a protein extract after heat treatment. Heat treated extracts were examined by proteomic analysis. A 27-kDa glycoprotein was identified, expressed in Escherichia coli, and purified. IgE reactivity of the recombinant protein was investigated by ELISA. High molecular weight proteins (above 100 kDa) elicited increased IgE binding after heat treatment compared to that before heat treatment. The molecular identities of these proteins, however, could not be determined. IgE reactivity toward a 27-kDa glycoprotein was also increased after heating the protein extract. The recombinant protein was recognized by IgE antibodies from allergic subjects (33.3%). Glycation or aggregation of protein by heating may create new IgE binding epitopes. Heat stable allergens are shown to be important in silkworm allergy. Sensitization to the 27-kDa glycoprotein from silkworm may contribute to elevation of IgE to silkworm.
Files in This Item:
T201600162.pdf Download
DOI
10.3346/jkms.2016.31.1.18
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실) > 1. Journal Papers
5. Research Institutes (연구소) > Institute of Allergy (알레르기연구소) > 1. Journal Papers
Yonsei Authors
박경희(Park, Kyung Hee) ORCID logo https://orcid.org/0000-0003-3605-5364
박중원(Park, Jung Won) ORCID logo https://orcid.org/0000-0003-0249-8749
이재현(Lee, Jae Hyun) ORCID logo https://orcid.org/0000-0002-0760-0071
정경용(Jeong, Kyoung Yong) ORCID logo https://orcid.org/0000-0001-9887-1426
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URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/146283
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