Skip to main content
Log in

Molecular characterization of major allergens Ara h 1, 2, 3 in peanut seed

  • Original Paper
  • Published:
Plant Cell Reports Aims and scope Submit manuscript

Abstract

Peanut is among the most commonly used dietary seeds, but peanut allergens, especially Ara h 1 (Arachis hypogaea allergy 1), 2 and 3, can cause severe IgE-mediated reactions. In this study, the molecular characterization and expression pattern of three allergens in peanut LUHUA 8, the representative of the cultivated lines in China, are reported. In situ hybridization and real time PCR analysis revealed high expression levels and different tissue expression patterns of the three allergens, which might be connected with many aspects, such as the strong conservation of intron phase of the allergen genes, the low energy of the mRNA’s regions, and the complicated post-translational modifications. Furthermore, the different sequences between the cloned allergens and the reported sequences previously involved the charged amino acids especially in IgE epitopes, which might alter specific physicochemical and physiological properties, and thus influence the immunity of the allergens. The identification of the specific features of the allergen genes would be of considerable importance to the basic understanding of the specific characteristics of peanut seed allergens.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3

Similar content being viewed by others

References

  • Azevedo H, Lino-Neto T, Tavares RM (2003) An improved method for high-quality RNA isolation from needles of adult maritime pine trees. Plant Mol Biol Rep 21:333–338

    Article  CAS  Google Scholar 

  • Barre A, Jacquet G, Sordet C, Culerrier R, Rougé P (2007) Homology modelling and conformational analysis of IgE-binding epitopes of Ara h 3 and other legumin allergens with a cupin fold from tree nuts. Mol Immunol 44:3243–3255

    Article  PubMed  CAS  Google Scholar 

  • Blom N, Gammeltoft S, Brunak S (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294:1351–1362

    Article  PubMed  CAS  Google Scholar 

  • Breathnach R, Benoist C, O’Hare K, Cannon F, Chambon P (1978) Ovalbumin gene: evidence for a leader sequence in mRNA and DNA sequences at the exon-intron boundaries. Proc Natl Acad Sci USA 75:4853–4857

    Article  PubMed  CAS  Google Scholar 

  • Breiteneder H, Radauer C (2004) A classification of plant food allergens. J Allergy Clin Immunol 113:821–830

    Article  PubMed  CAS  Google Scholar 

  • Burks AW, Shin D, Cockrell G, Stanley JS, Helm RM, Bannon GA (1997) Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. Eur J Biochem 245:334–339

    Article  PubMed  CAS  Google Scholar 

  • De Smit MH, van Duin J (1994) Control of translation by mRNA secondary structure in Escherichia coli. A quantitative analysis of literature data. J Mol Biol 244:144–150

    Article  PubMed  Google Scholar 

  • Guillaumie S, Mzid R, Méchin V, Léon C, Hichri I, Destrac-Irvine A, Trossat-Magnin C, Delrot S, Lauvergeat V (2010) The grapevine transcription factor WRKY2 influences the lignin pathway and xylem development in tobacco. Plant Mol Biol 72:215–234

    Article  PubMed  CAS  Google Scholar 

  • Kang IH, Gallo M (2007) Cloning and characterization of a novel peanut allergen Ara h 3 isoform displaying potentially decreased allergenicity. Plant Sci 172:345–353

    Article  CAS  Google Scholar 

  • Kang IH, Srivastava P, Ozias-Akins P, Gallo M (2007) Temporal and spatial expression of the major allergens in developing and germinating peanut seed. Plant Physiol 144:836–845

    Article  PubMed  CAS  Google Scholar 

  • Khuri S, Bakker FT, Dunwell JM (2001) Phylogeny, function, and evolution of the cupins, a structurally conserved, functionally diverse superfamily of proteins. Mol Biol Evol 18:593–605

    PubMed  CAS  Google Scholar 

  • Kyndt T, Haegeman A, Gheysen G (2008) Evolution of GHF5 endoglucanase gene structure in plant-parasitic nematodes: no evidence for an early domain shuffling event. BMC Evol Biol 8:305

    Article  PubMed  Google Scholar 

  • Lehmann K, Hoffmann S, Neudecker P, Suhr M, Becher WM, Rösch P (2003) High-yield expression in Escherichia coli, purification, and characterization of properly folded major peanut allergen Ara h 2. Protein Expr Purif 31:250–259

    Article  PubMed  CAS  Google Scholar 

  • Letunic I, Doerks T, Bork P (2009) SMART 6: recent updates and new developments. Nucleic Acids Res 37:D229–D232

    Article  PubMed  CAS  Google Scholar 

  • Li J, Shefcheck K, Callahan J, Fenselau C (2010) Primary sequence and site-selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2. Protein Sci 19:174–182

    PubMed  CAS  Google Scholar 

  • Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2−ΔΔCT method. Methods 25:402–408

    Article  PubMed  CAS  Google Scholar 

  • Marchler-Bauer A, Anderson JB, Chitsaz F et al (2009) CDD: specific functional annotation with the Conserved Domain Database. Nucleic Acids Res 37:205–210

    Article  Google Scholar 

  • Nolan RC, de Leon MP, Rolland JM, Loh RKS, O’Hehir RE (2007) What’s in a kiss: peanut allergen transmission as a sensitizer? J Allergy Clin Immunol 119:755

    Article  PubMed  Google Scholar 

  • Rabjohn P, Helm EM, Stanley JS, West CM, Sampson HA, Burks AW, Bannon GA (1999) Molecular cloning and epitope analysis of peanut allergen Ara h 3. J Clin Invest 103:535–542

    Article  PubMed  CAS  Google Scholar 

  • Shin DS, Compadre CM, Maleki SJ, Kopper RA, Sampson H, Huang SK, Burks AW, Bannon GA (1998) Biochemical and structural analysis of the IgE binding sites on Ara h 1, an abundant and highly allergic peanut protein. J Biol Chem 273:13753–13759

    Article  PubMed  CAS  Google Scholar 

  • Shreffler WG, Castro RR, Kucuk ZY, Charlop-Powers Z, Grishina G, Yoo S, Burks AW, Sampson HA (2006) The major glycoprotein allergen from Arachis hypogaea, Ara h 1, is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro. J Immunol 177:3677–3685

    PubMed  CAS  Google Scholar 

  • Tandang-Silvas MR, Fukuda T, Fukuda C, Prak K, Cabanos C, Kimura A, Itoh T, Mikami B, Utsumi S, Maruyama N (2010) Conservation and divergence on plant seed 11S globulins based on crystal structures. Biochim Biophys Acta 1804:1432–1442

    PubMed  CAS  Google Scholar 

  • Yan YS, Lin XD, Zhang YS, Wang L, Wu KQ, Huang SZ (2005) Isolation of peanut genes encoding arachins and conglutins by expressed sequence tags. Plant Sci 169:439–445

    Article  CAS  Google Scholar 

  • Zhang W, Xiao W, Wei H, Zhang J, Tian Z (2006) mRNA secondary structure at start AUG codon is a key limiting factor for human protein expression in Escherichia coli. Biochem Biophys Res Commun 349:69–78

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgments

The work was supported by Key Program of Excellent Talents Foundation of the Education Department of Anhui Province in China (2009SQRZ112ZD) and Key Construction Subject of Anhui Science and Technology University (AKXK20102-1). The work described has not been published before and its publication has been approved by all co-authors. The authors have no conflict of interest. We thank professor Guangming Jin, professor Xunhai Zhang and Mr. Xuan Wang for their assistance. We also appreciate comments and suggestions made by editors and anonymous reviewers.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Shengjuan Jiang.

Additional information

Communicated by P. Lakshmanan.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Jiang, S., Wang, S., Sun, Y. et al. Molecular characterization of major allergens Ara h 1, 2, 3 in peanut seed. Plant Cell Rep 30, 1135–1143 (2011). https://doi.org/10.1007/s00299-011-1022-1

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00299-011-1022-1

Keywords

Navigation