AF050: Prolamin superfamily

List allergens from this family:

Routes of exposure:
Include only IUIS approved allergens.

Biochemical properties

The prolamin superfamily derives its name from the alcohol-soluble proline and glutamine rich storage proteins of cereals. Members of the this family are characterized by the presence of an α-helical globular domain that contains a conserved pattern of six or eight cysteine residues that form three or four intra-molecular disulfide bonds [1]. Apart from the conserved cysteine pattern, there exist little sequence similarities between members of different subfamilies. Members of the prolamin superfamily include the cereal prolamin seed storage proteins and several families of disulfide-rich small proteins. The prolamin seed storage proteins (gliadins and glutenins) contain a repetitive coiled-coil domain rich in proline and glutamine residues and a globular disulfide-rich domain. Families of low molecular weight sulfur-rich proteins are the grain softness proteins, indolines, non-specific lipid transfer proteins, soybean hydrophobic protein, bifunctional α-amylase/protease inhibitors, and 2S albumin seed storage proteins.

Allergens from this family

Several families that belong to the prolamin superfamily were described as allergens.

Due to their stability to heat and gastro-intestinal digestion, many allergens from the prolamin superfamily are important food allergens and may account for severe allergic reactions [11].



  1. Mills EN, Jenkins JA, Alcocer MJ, Shewry PR:
    Structural, biological, and evolutionary relationships of plant food allergens sensitizing via the gastrointestinal tract.
    Crit Rev Food Sci Nutr 2004, 44, 379-407. [PubMed] [Full Text]
  2. Sandiford CP, Tatham AS, Fido R, Welch JA, Jones MG, Tee RD, Shewry PR, Newman Taylor AJ:
    Identification of the major water/salt insoluble wheat proteins involved in cereal hypersensitivity.
    Clin Exp Allergy 1997, 27, 1120-9. [PubMed]
  3. Pastorello EA, Robino AM:
    Clinical role of lipid transfer proteins in food allergy.
    Mol Nutr Food Res 2004, 48, 356-62. [PubMed] [Full Text]
  4. Breiteneder H, Mills C:
    Nonspecific lipid-transfer proteins in plant foods and pollens: an important allergen class.
    Curr Opin Allergy Clin Immunol 2005, 5, 275-9. [PubMed]
  5. Vejvar E, Himly M, Briza P, Eichhorn S, Ebner C, Hemmer W, Ferreira F, Gadermaier G:
    Allergenic relevance of nonspecific lipid transfer proteins 2: Identification and characterization of Api g 6 from celery tuber as representative of a novel IgE-binding protein family.
    Mol Nutr Food Res 2013, 57, 2061-70. [PubMed] [Full Text]
  6. Giangrieco I, Alessandri C, Rafaiani C, Santoro M, Zuzzi S, Tuppo L, Tamburrini M, D'Avino R, Ciardiello MA, Mari A:
    Structural features, IgE binding and preliminary clinical findings of the 7kDa Lipid Transfer Protein from tomato seeds.
    Mol Immunol 2015, 66, 154-63. [PubMed] [Full Text]
  7. James JM, Sixbey JP, Helm RM, Bannon GA, Burks AW:
    Wheat alpha-amylase inhibitor: a second route of allergic sensitization.
    J Allergy Clin Immunol 1997, 99, 239-44. [PubMed]
  8. Gonzalez R, Varela J, Carreira J, Polo F:
    Soybean hydrophobic protein and soybean hull allergy.
    Lancet 1995, 346, 48-9. [PubMed]
  9. Bhave M, Morris CF:
    Molecular genetics of puroindolines and related genes: regulation of expression, membrane binding properties and applications.
    Plant Mol Biol 2008, 66, 221-31. [PubMed] [Full Text]
  10. Pastorello EA, Farioli L, Conti A, Pravettoni V, Bonomi S, Iametti S, Fortunato D, Scibilia J, Bindslev-Jensen C, Ballmer-Weber B, Robino AM, Ortolani C:
    Wheat IgE-mediated food allergy in European patients: alpha-amylase inhibitors, lipid transfer proteins and low-molecular-weight glutenins. Allergenic molecules recognized by double-blind, placebo-controlled food challenge.
    Int Arch Allergy Immunol 2007, 144, 10-22. [PubMed] [Full Text]
  11. Breiteneder H, Mills EN:
    Molecular properties of food allergens.
    J Allergy Clin Immunol 2005, 115, 14-23; quiz 4. [PubMed] [Full Text]


Links to Pfam

Family-defining Pfam domains (at least one of these domains is present in each family member):

Pfam domain Pfam clan
PF00234 Protease inhibitor/seed storage/LTP family CL0482 Di-sulfide bond pairrings
PF03157 High molecular weight glutenin subunit -
PF13016 Cys-rich Gliadin N-terminal CL0482 Di-sulfide bond pairrings
PF14368 Probable lipid transfer CL0482 Di-sulfide bond pairrings
PF14547 Hydrophobic seed protein CL0482 Di-sulfide bond pairrings

Links to Wikipedia


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