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. 2010 Aug;62(4):307-11.
doi: 10.1007/s10616-009-9243-7. Epub 2009 Dec 19.

Epitope analysis of peanut allergen Ara h1 with human monoclonal IgM antibody 92-2

Hiroshi Shinmoto  1 , Yuji Matsuo, Yasunori Naganawa, Shinichi Tomita, Yuko Takano-Ishikawa
Affiliations

Epitope analysis of peanut allergen Ara h1 with human monoclonal IgM antibody 92-2

Hiroshi Shinmoto et al. Cytotechnology. 2010 Aug.

Abstract

A human-mouse hybridoma clone 92-2 secreting IgM-class human monoclonal antibody to peanut allergen protein Ara h1 was established. To detect antibody-binding sequences on Ara h1, we synthesized a series of peptides of the Ara h1 protein on a multi-pin apparatus for the pin-peptide ELISA. The 92-2 human monoclonal antibody was found to recognize a sequence of GREGEQEWGTPGSHVREETS. Further analysis with shorter pin-peptides with eight amino acid-long showed that the sequence of QEWGTPGS was an essential linear sequence of this epitope. When the QEW part of the sequence was replaced by alanine, the 92-2 monoclonal antibody did not bind to the substituted peptide, showing that those amino acids play an important role in the binding of the 92-2 monoclonal antibody.

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Figures

Fig. 1
Fig. 1
Amino acid sequence of peanut allergen protein Ara h1. IgE epitopes reported by by Burks et al. (1997) and Shin et al. (1998) are underlined and an IgM epitope found in this study was shown in bold letters (aa 156–163)
Fig. 2
Fig. 2
Pin peptide ELISA of Ara h1 20 amino-acid-overlapping peptides with antibody 92-2
Fig. 3
Fig. 3
Pin peptide ELISA of Ara h1-8 amino-acid-overlapping peptides with antibody 92-2
Fig. 4
Fig. 4
Pin peptide ELISA of Ara h1 epitope peptide with alanine substitution with antibody 92-2
See this image and copyright information in PMC

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