rTri a 14 Wheat

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Latin name: Triticum aestivum
Source material: A Pichia pastoris strain carrying a cloned cDNA encoding Triticum aestivum allergen Tri a 14.
Common names: Lipid-transfer protein.

Wheat 

Recombinant allergens

  • rTri a 14
  • rTri a 19 Omega-5 Gliadin

Tri a 14

Allergen

rTri a 14. (1, 2)

Biological function

A lipid transfer protein.

Mw

Approximately 9.7 kDa.

Other allergens isolated

The following allergens have been isolated and characterised to date.

 

Allergen

Common name / biological function

References

Tri a 12

A profilin, an actin-binding protein, found in wheat seed and pollen.

(3, 4, 5, 6)

Tri a 14

A lipid-transfer protein, resulting in allergic reactions via ingestion, skin contact, and inhalation of wheat flour.

(3, 7, 8, 9, 10, 11)

Tri a 18

A hevein-like protein.

(3, 4)

Tri a 19

Also known as gluten, gliadin, gamma-gliadin, omega-gliadin.

(12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24)

Tri a Chitinase

A chitinase.

(25)

Tri a Bd 17K

An alpha-amylase inhibitor CM16.

(26, 27)

Tri a 25

A thioredoxin.

(3, 4, 28, 29)

Tri a 26

A glutenin.

(3, 30)

Tri a 27

A thiol reductase homologue.

(3, 31)

Tri a 28

An alpha-amylase inhibitor, dimeric alpha-amylase inhibitors.

(3, 32)

Tri a 29

An alpha-amylase inhibitor, Tetrameric alpha-amylase Inhibitors CM1/CM2.

(3, 33)

Tri a 30

Unknown function.

(3, 34)

Tri a aA/TI

An alpha-amylase/trypsin inhibitor, an approximately 14-15 kDa low-molecular-weight (LMW) allergen, resulting in allergic reactions via ingestion and inhalation of wheat, e.g. as flour.

(35, 36, 37)

Tri a LMW Glu

A glutenin.

(3, 13, 30, 38, 39, 40, 41, 42 )

Tri a Germin

A germin.

(43)

Tri a Peroxidase

A peroxidase purified from wheat albumin and an inhalant allergen. A 36 kDa protein.

(44)

Tri a TPIS

A triosephosphate isomerase, an allergen via inhalation in bakers.

(45)

Tri a alphabeta_Gliadin

A gliadin, also known as gliadin or gluten, resulting in allergic reactions via inhalation of wheat, e.g. as flour.

(46)

Tri a alpha_Gliadin

A gliadin, also known as gliadin, gluten.

(4, 12, 13, 14, 42, 47, 48)

Tri a beta_Gliadin

 

(13, 42, 47, 48)

Tri a gamma_Gliadin

 

(12, 13, 20, 21, 39, 42, 47)

Tri a omega2_Gliadin

 

(12, 13, 47, 48)

Tri a DH

A dehydrin.

(49)

Tri a GST

A glutathione-S-transferase.

(49)

Tri a PER

A peroxiredoxine.

(49)

 

See Wheat f4 for a description of the individual allergens found in the wheat kernel, and Cultivated Wheat g15 for those present in wheat pollen.

Allergen description

Tri a 14, a protein of approximately 20 kDa in size, belongs to the lipid-transfer protein family and is found in the wheat kernel. Tri a 14 has been also described as one of the main allergens linked to wheat ingestion. (40)

Tri a 14 has been shown to be a major allergen associated with baker's asthma. (7) In a study exploring the involvement of wheat LTPs in baker's asthma caused by wheat-flour sensitisation, 40 patients with occupational asthma caused by wheat-flour inhalation were studied. Specific IgE to purified Tri a 14 was found in 60% of 40 individual sera from patients with baker's asthma, and the purified allergen elicited positive skin-prick test reactions in 62% of 24 of these patients. (1, 7) Importantly, none of the 40 patients with baker’s asthma described symptoms after eating wheat-derived products. In addition, around 60% of the subgroup of these patients who showed specific IgE to Tri a 14, Pru p 3, or both, exhibited no sensitisation to non-cereal plant foods. (7) (See below).

Tri a 14 was also reported to be a major allergen associated with baker's asthma in Spanish patients,  (7) and a relevant allergen in wheat IgE-mediated food allergy in Italian subjects, where 9 of 22 patients with wheat food allergy were confirmed to be sensitised to purified wheat LTP by skin-prick testing. (40) A French study reported that 28% of 60 patients with wheat food allergy showed IgE reactions with purified wheat LTP. (48) This suggests that Tri a 14 could be a useful tool for diagnosis of wheat allergy, at least in the Mediterranean population. (1)

Lipid-transfer proteins (LTPs) are small molecules of approximately 9 kDa to 10 kDa that demonstrate great stability and are very resistant to digestion and heat treatment. (50) Lipid-transfer proteins facilitate the transport of phospholipids and galactolipids across membranes. Non-specific lipid-transfer proteins belong to the PR 14 family of pathogenesis-related proteins.

Lipid transfer proteins (LTP) are highly conserved and widely distributed throughout the plant kingdom. They have been identified as allergens in the Rosaceae subfamilies of the Prunoideae (peach, apricot, plum) and of the Pomoideae (apple). They belong to a family of structurally highly-conserved proteins that are also present in non-Rosaceae vegetable foods. They have been linked to severe and systemic symptoms, and induce sensitisation by the oral route in fruit-allergic patients who do not have associated pollen allergy.

The high resistance of LTPs to both heat treatment and digestive proteolytic digestion probably allows the allergens to reach the intestinal tract in an almost unmodified form, and this is thought to be responsible for the capability of these allergens to induce severe symptoms in many patients. (51)

This is in contrast with LTPs from pollen aeroallergens, which sensitise via the respiratory tract as a result of allergen inhalation, (52, 53) resulting in primary sensitisation, though they have also been linked in some cases to plant food and pollen cross-reactions. (51, 54, 55)

Allergy to ingestion of lipid-transfer protein (LTP) is quite common in the Mediterranean countries, but virtually absent in Northern Europe. (56) Lipid-transfer protein is usually associated with more severe systemic reactions than oral allergy syndrome. For example, peach LTP (Pru p 3) is a minor allergen in Northern European countries but a major allergen in the South, affecting over 60% of patients allergic to peach in the Spanish population. (57) In peach-allergic patients who have experienced systemic reactions to peach, up to 100% may be sensitised to LTP. (58)

Allergenic LTPs from peach fruit and mugwort (Artemisia vulgaris) pollen are responsible for clinical symptoms in Mediterranean patients as a result of cross-reactivity. (59, 60)

A high level of cross-reactivity occurs among fruits and vegetables containing lipid-transfer proteins, including sweet chestnut, (59) cabbage (with 50% identity to peach LTP), (61) walnut, (62) lettuce, (63) and hazelnut. (64) Grape and wine may contain lipid transfer protein homologous to and cross-reactive with peach LTP. (65)

However, the amino acid sequence of the mature wheat LTP (Tri a 14) shows only a 45% identity with that of the peach LTP allergen Pru p 3, (7) and that only a limited IgE cross-reactivity between Tri a 14 and peach Pru p 3 exists. (7) The authors suggest that the low cross-reactivity between both allergens detected in several individual sera evaluated in the study reflected great differences in their 3-dimensional IgE-binding regions. (7)

Tri a 14 differs from peach fruit and mugwort pollen LTP for a number of reasons, including that some patients lose their IgE-binding capacity towards the LTP when wheat protein is heated. This is attributed to the unfolding of wheat LTP following extensive heating. (66) Future research will clarify the cross-reactive potential of wheat LTP with other LTPs.

Nonetheless, cross-reactivity with LTP allergens from fruits and vegetables cannot be completely disregarded as the cause of sensitisation to Tri a 14 in some patients with baker’s asthma. (7)

Native Tri a 14 was shown to exhibit similar IgE-binding capacity to recombinant Tri a 14. Specific IgE determination for both allergen forms performed in 26 individual sera from patients with baker's asthma demonstrated positive assays in 61% (16 of 26) and 54% (14 of 26) of sera for nTri a 14 and rTri a 14 respectively. (1)

Allergy to wheat is common. Depending on the route of allergen exposure and the underlying immunologic mechanisms, wheat allergy is classified into classic food allergy affecting the skin, gastrointestinal tract, or respiratory tract; food-dependent, exercise-induced anaphylaxis (FDEIA); occupational asthma (‘baker's asthma’) and rhinitis; or contact urticaria. (67)

In addition, ingestion of wheat gluten may cause celiac disease, T-cell-mediated intestinal inflammation, or dermatitis herpetiformis, a blistering skin eruption. (67)

See Wheat f4 for clinical information and further details on wheat dander allergy. See also Cultivated wheat g15 (for allergy to the pollen), Gluten f79, rTri a 19 Omega-5 Gliadin, Wheat f416 (allergy to the food).

In a population-based birth cohort in Stockholm, the prevalence of sensitisation to wheat in 2336 4-year-old children was reported to be 4%. (68, 69) In the German Multi-Centre Allergy Study (MAS) which analysed longitudinal data of sera from 273 children from ages 2 to 10 years, the prevalence of IgE to wheat increased progressively with age: from 2 to 9%. (70) The investigators speculated that IgE sensitisation to wheat occurs primarily in early infancy, whereas it is mostly secondary to pollen sensitisation at school age. Although sensitisation to wheat is thought to be primarily a childhood disease, in adults the prevalence of sensitisation to wheat as assessed by IgE in several studies was reported to be greater than 3%. (67)

Studies of wheat food allergy in patients sensitised through other routes than gastrointestinal tract have been reported. (47, 71, 72) Patients with baker's asthma, which is induced by inhalation of raw wheat flour, never have problems with ingestion of cooked wheat. Baker’s asthma is an occupational allergy caused mainly by an IgE-mediated allergic response to inhalation of cereal flours. It mostly affects bakers, millers, and pastry factory workers, and is one of the most common forms of occupational asthma, affecting up to 15% of this group. Although many allergens have been implicated as sensitising proteins, and although sensitisation if often as a result of heterogeneous sensitisation to more than a single allergen, Tri a 14 has been reported to be a major allergen as described above. (7)

However, some patients with baker’s asthma may develop symptoms other than respiratory symptoms after ingesting meals contaminated by uncooked wheat flour. (71)

Recombinant allergens, which are genetically engineered isoforms resembling allergen molecules from known allergen extracts, have immunoglobulin E (IgE) antibody binding comparable to that of natural allergens, and generally show excellent reactivity in in vitro and in vivo diagnostic tests. (73 )To date, many different recombinant allergens of various pollens, moulds, mites, and foods, as well as of latex and bee venom, have been cloned, sequenced, and expressed.

Recombinant allergens have a wide variety of uses, from the diagnosis and management of allergic patients, to the development of immunotherapy, to the standardisation of allergenic test products as tools in molecular allergology. Recombinant allergens are particularly useful for investigations of allergies manifesting wide cross-reactivity.

As the number of important allergens in commercial wheat extracts may vary extensively, (74) and as natural preparations may be contaminated with other components, potentially causing false-positive skin-specific IgE test results, recombinant Tri a 14 has a role to play in assessing allergy to wheat.

Importantly, wheat-allergic individuals are sensitised to a heterogeneous range of wheat allergens. Recombinant allergens enable assessment of sensitisation to specific allergens in the repertoire range; and specifically, Tri a 14 provides a means for investigating differences in the immune response to lipid-transfer protein allergens, but also provides an important reagent for the diagnosis of wheat allergy and baker’s asthma. (67) Sensitisation to Tri a 14 indicates primary sensitisation to wheat and is less useful in the evaluation of cross-reactivity, in particular with peach and other major lipid-transfer protein-containing plants. (75) Future studies may clarify the role of Tri a 14 in cross-reactivity with other lipid-transfer proteins.

Compiled by Dr Harris Steinman, harris@allergyadvisor.com

References

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As in all diagnostic testing, the diagnosis is made by the physican based on both test results and the patient history.