Food:

BIOCHEMICAL INFORMATION for Almond

Allergen Name:
Amandin
Alternatve Allergen Names:
Almond major protein, Prunin, 11S globulin
Allergen Designation:
Major
Protein Family:
Pfam PF00190; Cupin 11S
Sequence Known?:
Yes
Allergen accession No.s:

http://ca.expasy.org/cgi-bin/niceprot.pl?Q43607 (PIR S51941)

PIR S51942 http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=protein&val=1076482
PIR CAA55009 http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=protein&val=460806

3D Structure Accession No.:
Not determined
Calculated Masses:
63017 Da (precursor)
Experimental Masses:

63 and 65 kDa (non-reduced)
20-22 and 38-42 kDa (reduced)

Oligomeric Masses:
Probably hexamer
Allergen epitopes:
Not determined
Allergen stability:
Process, chemical, enzymatic
Venkatachalam et al. (2002) [726] show that binding to rabbit monoclonal antibodies and to human IgE partially survives roasting, blanching, autoclaving, and microwave heating. Binding to the 39 kDa to 66 kDa bands is more stable than to the lower Mr. bands.
Nature of main cross-reacting proteins:
Not determined
Allergen properties & biological function:
Amandin is the major almond storage protein and is one of the legumin family of 11S seed storage globulins.
Allergen purification:
Defatted almond flour was extracted with 10 volumes of 0.02 M Tris-HCl (pH 8.1 buffer) with constant magnetic stirring, filtered through glass wool, and the filtrate was centrifuged. The supernatant was loaded onto a DEAE DE-53 column equilibrated in 0.02 M Tris-HCl buffer and then eluted with a 0-0.5 M NaCl gradient. Fractions containing the almond major protein, AMP, were pooled and concentrated. Aliquots were loaded on a Sephacryl S300 column in Tris buffer with 0.1 M NaCl. Fractions containing the AMP were pooled, dialyzed, and lyophilized (Acosta et al. 1999 [732]).
Other biochemical information:

Sathe et al. (2001) [730] present clear evidence for IgE binding to proteins in the 39-66 kDa range. Sathe et al. (2001) [730], Roux et al. (1999) [731] and Roux et al. (2001) [727] attribute this to the almond major protein, amandin. Poltronieri et al. (2002) [725] suggest that binding is due to conglutin gamma at 45 kDa.

Roux et al. (2003) [694] note that >50% of patients with serious symptoms bind amandin and that the 66 kDa band corresponds to unprocessed amandin.

Prunin, described as the major storage protein of almond (Garcia-Mas et al., 1995 [923]), is taken above as a synonym of amandin.


References (8)

Acosta MR, Roux KH, Teuber SS, Sathe SK.
Production and characterization of rabbit polyclonal antibodies to almond (Prunus dulcis L.) major storage protein. J Agric Food Chem. 47(10): 4053-4059. 1999
PUBMED ID: 10552764
[732]
Garcia-Mas J, Messeguer R, Arus P, Puigdomenech P.
Molecular characterization of cDNAs corresponding to genes expressed during almond (Prunus amygdalus Batsch) seed development. Plant Mol Biol. 27(1):205-210. 1995
PUBMED ID: 7865791
[923]
Poltronieri P, Cappello MS, Dohmae N, Conti A, Fortunato D, Pastorello EA, Ortolani C, Zacheo G.
Identification and characterisation of the IgE-binding proteins 2S albumin and conglutin gamma in almond (Prunus dulcis) seeds. Int Arch Allergy Immunol. 128(2): 97-104 2002
PUBMED ID: 12065909
[725]
Roux KH, Teuber SS, Robotham JM, Sathe SK.
Detection and stability of the major almond allergen in foods. J Agric Food Chem. 49(5): 2131-2136. 2001
PUBMED ID: 11368566
[727]
Roux KH, Teuber SS, Sathe SK.
Tree nut allergens. Int Arch Allergy Immunol. 131(4):234-244. 2003
PUBMED ID: 12915766
[694]
Roux, K. H.; Sathe, S. K.; Peterson, W. R.; Teuber, S. S.
The major seed storage protein of almond (Almond Major Protein) is an allergen. J. Allergy Clin. Immunol. 103, S66, abstract 255 1999
PUBMED ID: unknown
[731]
Sathe SK, Teuber SS, Gradziel TM, Roux KH.
Electrophoretic and immunological analyses of almond (Prunusdulcis l.) genotypes and hybrids. J Agric Food Chem. 49(4): 2043-2052. 2001
PUBMED ID: 11308365
[730]
Venkatachalam M, Teuber SS, Roux KH, Sathe SK.
Effects of roasting, blanching, autoclaving, and microwave heating on antigenicity of almond (Prunus dulcis L.) proteins. J Agric Food Chem. 50(12): 3544-3548. 2002
PUBMED ID: 12033826
[726]
This record was last modified on 18-Oct-2006
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