Type:
Component
Component
Component
Der p 10
Inhalation
Group 10 (Tropomyosin)
d205
37 kDa
Located in the bodies of house dust mite. Native sourced from the extracts of Dermatophagoides pteronyssinus or recombinant
Der p 10 is one of the minor allergens of house dust mite (HDM) with a reported prevalence among Dermatophagoides pteronyssinus sensitized patients to be between 5-18%. Specific immunoglobulin E (sIgE) to Der p 10 is associated with respiratory symptoms including rhinitis, conjunctivitis, cough, dyspnea, and asthma. A high degree of cross-reactivity between Der p 10, Der f 10 and Blo t 10 and Lep d 10 is observed. Der p 10 is tropomyosin and can cause cross-reaction with tropomyosin from crustaceans (shrimp, crab, lobster, prawn, escargot, crayfish) mollusks (mussel, oyster, scallop, snails, abalone, squid, cuttlefish, octopus). Der p 10 might be a diagnostic biomarker for patients with mite-allergy with add-on sensitization to allergens except, Der p 1 and Der p 2. Therefore, while initiating the immunotherapy with allergen extracts in these patients, special attention is needed.
Der p 10 is one of the minor (panallergen) allergens of house dust mite (HDM) (1). However, it is a major allergen in shrimps and other crustaceans (2).
The prevalence of Der p 10 among Dermatophagoides pteronyssinus (Der p) sensitized patients is reported to be between 5-18% (3). Der p 10 are muscle proteins of the HDM, responsible for the allergic reactions (1).
According to a study conducted in China including 130 allergic rhinitis patients, the prevalence of positive serum specific immunoglobulin E (sIgE) was 11.5% for Der p 10 (4).
In a study conducted, 201 out of 1322 (15.2%) Der p allergic patients in Vienna, Austria (showing respiratory symptoms like rhinitis, conjunctivitis, cough, dyspnoea and asthma) demonstrated specific IgE antibodies to Der p 10 (5).
Der p 10 is the minor allergen component extracted from the mite allergen crude extracts. It is found to be located in the body (muscles) of the Der p (6).
Affinity chromatography was one of the methods used for purification of natural Der p from an HDM extract. Der p 10 was expressed in Escherichia coli and was further characterized by mass spectrometry and circular dichroism. The molecule can also be generated by recombinant expression systems (5).
Tropomyosins are a large family of heat-resistant alpha-helical proteins. These proteins form a coiled-coil structure of two parallel helices that includes two sets of seven alternating actin-binding sites. This feature plays a vital role in regulating the function of actin filaments (6).
Der p 10 is composed of 284 amino acids. 65% similarity in Der p 10 tropomyosin residues is observed with that of other invertebrate tropomyosins. Higher sequence similarity within the HDM tropomyosins is noted that any other mite allergen (6).
A high degree of cross-reactivity between Der p 10 (from Der p), Der f 10 (from Dermatophagoides farinae), and Blo t 10 (from Blomia tropicalis), belonging to the HDM tropomyosins family is observed (6, 7).
Tropomyosin from crustaceans (shrimp, crab, lobster, prawn, escargot) exhibits cross-reactivity with Der p 10 (2). The allergic reactions to crustaceans, mites, cockroaches and parasites can be explained by the IgE to Der p 10, Bla g 7 (cockroach), Pen m 1 (prawn), and Ani s 3 (Anisakis) (2).
Cross-reactivity between the shrimp-reactive IgE antibodies and HDM in shrimp-allergic patients is also noted (8). In patients with HDM allergy, the reactivity to shrimp has been revealed, especially in patients who have never been exposed to shrimps due to religious eating habits (9).
Cross-reactivity of tropomyosin allergens from HDMs is observed with the following crustaceans (6):
Family |
Whole allergen |
Allergen component |
---|---|---|
Penaeidae |
Brown shrimp |
Pen a 1 |
Black tiger shrimp |
Pen m 1 |
|
Indian prawn |
Pen i 1 |
|
White leg shrimp |
Lit v 1 |
|
Sand shrimp |
Met e 1 |
|
Crangonidae |
Common shrimp |
Cra c 1 |
Pandalidae |
Northern shrimp |
Pan b 1 |
Nephropidae |
European lobster |
Hom g 1 |
American lobster |
Hom a 1 |
|
Palinuridae |
Chinese spiny lobster |
Pan s 1 |
Portunidae |
Coral crab |
Cha f 1 |
Cambaridae |
Red swamp crayfish |
Pro cl 1 |
Cross-reactivity of tropomyosin allergens from HDMs is also reported with mollusks (6):
Family |
Whole allergen |
Allergen component |
---|---|---|
Mytilidae |
Blue mussel |
Myt e 1 |
Mediterranean mussel |
Myt g 1 |
|
Asian green mussel |
Per v 1 |
|
Osteridae |
Pacific oyster |
Cra g 1 |
Pectinidae |
Scallop |
Mim n 1 |
Solecurtidae |
Razor clams |
Sin c 1 |
Haliotidae |
Disk abalone |
Hal di 1 |
Japanese abalone |
Hal d 1 |
|
Turbinidae |
Horned turban snails |
Tur c 1 |
Helicidae |
Brown garden snail |
Hel as 1 |
Ommastrephidae |
Japanese flying squid |
Tod p 1 |
Sepiidae |
Golden cuttlefish |
Sep e 1 |
Octopodidae |
Common octopus |
Oct v 1 |
Der p 10 of HDM has a molecular weight of 37 kDa (1).
Der p 10.0101 is the major isoform Der p 10 (10).
A high degree of cross-reactivity is noted between Dermatophagoides pteronyssinus and Dermatophagoides farinae extracts; however, the reactivity between Dermatophagoides and Blomia tropicalis is low. One of the leading causes of reactivity among mites, cockroaches, shellfish, and helminths is Tropomyosin (Der p 10); however, glutathione transferase may also be included. In cases where genuine sensitization is unclear, specific allergen components can be useful to identify primary allergy (3).
Lep d 10 (tropomyosin from storage mites) demonstrates a high degree of identity with both Der p 10 and Der f 10 in HDM, and thus supports the known cross-reactivity (2).
A similarity in the sequence of Der p 10 is observed with tropomyosin from cockroach, and a high cross-reactivity was found between these two allergens (2, 11). In a study conducted including 118 cockroach-sensitized patients, a strong association was observed between the levels of both specific IgE antibodies (r = 0.90, P < 0.001) and specific IgG antibodies (r = 0.46, P < 0.001) for Per a 7 and Der p 10 (11).
A similarity in the amino acid sequences of Der p 10 has been reported with Pen a 1 (71%), Pen s 7 (80%), Cha f 1 (82%), Hel s 1 (64%), Oct v 1 (63%), Per v 1 (55%), Bla g 7 (80%) and Asc l 3 (73%) (3).
Der p 10 might be a diagnostic biomarker for patients with mite-allergy with add-on sensitization to mite allergens with an exception for Der p 1 and Der p 2. Therefore, when initiating the immunotherapy with allergen extracts in these types of patients, special attention is needed (5, 6).
According to a study conducted, 79 out of 80 HDM sensitized allergic patients (history of allergic rhinitis, atopic dermatitis, asthma and urticaria) in Korea demonstrated detectable IgE to Dermatophagoides pteronyssinus. A total of 7 patients (8.8%) reacted to Der p 10. Furthermore, the total IgE in Der p 10 sensitized patients were significantly higher than the non-sensitized patients (1,264.0 ± 1,502.9 IU/mL vs. 408.1 ± 463.8 IU/mL; p = 0.042). A noticeable correlation of Der p 10 serum IgE level was observed with serum IgE level to crab and shrimp (p < 0.0001 and p < 0.0001, respectively) (12).
The IgE reactivity to Der p 10 plays an essential role in identifying a subset of patients allergic to HDM with a broad range of sensitization to HDM allergens other than Der p 1 and Der p 2. This property of Der p 10 may have relevance for HDM-specific immunotherapy because the immunotherapy with the currently available HDM extracts might not be suitable for Der p 10-sensitized patients (5, 13).
Der p 10 as immunotherapy vaccines can be a feasible treatment option for polysensitized patients (13).
Author: Turacoz Healthcare Solutions
Reviewer: Dr. Christian Fischer
Last reviewed: November 2020