C-Terminal 23 kDa polypeptide of soybean Gly m Bd 28 K is a potential allergen

Ping Xiang, Eric J. Haas, Michael G. Zeece, John Markwell, Gautam Sarath

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Gly m Bd 28 K is a major soybean (Glycine max Merr.) glycoprotein allergen. It was originally identified as a 28 kDa polypeptide in soybean seed flour. However, the full-length protein is encoded by an open reading frame (ORF) of 473 amino acids, and contains a 23 kDa C-terminal polypeptide of as yet unknown allergenic and structural characteristics. IgE-binding (allergenic potential) of the Gly m Bd 28 K protein including the 23 kDa C-terminal portion as well as shorter fragments derived from the full-length ORF were evaluated using sera from soy-sensitive adults. All of these sera contained IgE that efficiently recognized the C-terminal region. Epitope mapping demonstrated that a dominant linear C-terminal IgE binding epitope resides between residues S256 and A270. Alanine scanning of this dominant epitope indicated that five amino acids, Y260, D261, D262, K264 and D266, contribute most towards IgE-binding. A model based on the structure of the β subunit of soybean β-conglycinin revealed that Gly m Bd 28 K contains two cupin domains. The dominant epitope is on the edge of the first β-sheet of the C-terminal cupin domain and is present on a potentially solvent-accessible loop connecting the two cupin domains. Thus, the C-terminal 23 kDa polypeptide of Gly m Bd 28 K present in soy products is allergenic and apparently contains at least one immunodominant epitope near the edge of a cupin domain. This knowledge could be helpful in the future breeding of hypo allergenic soybeans.

Original languageEnglish (US)
Pages (from-to)56-63
Number of pages8
JournalPlanta
Volume220
Issue number1
DOIs
StatePublished - Nov 1 2004

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allergens
Soybeans
Allergens
polypeptides
Immunoglobulin E
soybeans
epitopes
Peptides
Epitopes
open reading frames
Open Reading Frames
soybean products
amino acids
Epitope Mapping
Amino Acids
Immunodominant Epitopes
alanine
flour
glycoproteins
Glycine max

Keywords

  • Allergen
  • Cupin superfamily
  • Epitope mapping
  • Glycine max
  • IgE-binding
  • Recombinant fusion polypeptide

ASJC Scopus subject areas

  • Genetics
  • Plant Science

Cite this

Xiang, P., Haas, E. J., Zeece, M. G., Markwell, J., & Sarath, G. (2004). C-Terminal 23 kDa polypeptide of soybean Gly m Bd 28 K is a potential allergen. Planta, 220(1), 56-63. https://doi.org/10.1007/s00425-004-1313-7

C-Terminal 23 kDa polypeptide of soybean Gly m Bd 28 K is a potential allergen. / Xiang, Ping; Haas, Eric J.; Zeece, Michael G.; Markwell, John; Sarath, Gautam.

In: Planta, Vol. 220, No. 1, 01.11.2004, p. 56-63.

Research output: Contribution to journalArticle

Xiang, P, Haas, EJ, Zeece, MG, Markwell, J & Sarath, G 2004, 'C-Terminal 23 kDa polypeptide of soybean Gly m Bd 28 K is a potential allergen', Planta, vol. 220, no. 1, pp. 56-63. https://doi.org/10.1007/s00425-004-1313-7
Xiang, Ping ; Haas, Eric J. ; Zeece, Michael G. ; Markwell, John ; Sarath, Gautam. / C-Terminal 23 kDa polypeptide of soybean Gly m Bd 28 K is a potential allergen. In: Planta. 2004 ; Vol. 220, No. 1. pp. 56-63.
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AB - Gly m Bd 28 K is a major soybean (Glycine max Merr.) glycoprotein allergen. It was originally identified as a 28 kDa polypeptide in soybean seed flour. However, the full-length protein is encoded by an open reading frame (ORF) of 473 amino acids, and contains a 23 kDa C-terminal polypeptide of as yet unknown allergenic and structural characteristics. IgE-binding (allergenic potential) of the Gly m Bd 28 K protein including the 23 kDa C-terminal portion as well as shorter fragments derived from the full-length ORF were evaluated using sera from soy-sensitive adults. All of these sera contained IgE that efficiently recognized the C-terminal region. Epitope mapping demonstrated that a dominant linear C-terminal IgE binding epitope resides between residues S256 and A270. Alanine scanning of this dominant epitope indicated that five amino acids, Y260, D261, D262, K264 and D266, contribute most towards IgE-binding. A model based on the structure of the β subunit of soybean β-conglycinin revealed that Gly m Bd 28 K contains two cupin domains. The dominant epitope is on the edge of the first β-sheet of the C-terminal cupin domain and is present on a potentially solvent-accessible loop connecting the two cupin domains. Thus, the C-terminal 23 kDa polypeptide of Gly m Bd 28 K present in soy products is allergenic and apparently contains at least one immunodominant epitope near the edge of a cupin domain. This knowledge could be helpful in the future breeding of hypo allergenic soybeans.

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