Table of Contents

d205 Der p 10 Scientific Information Summary Epidemiology Environmental Characteristics Clinical Relevance Diagnostic Relevance Compiled By

Component

d205 Der p 10

d205 Der p 10 Scientific Information

Type:

Component

Name; WHO/IUIS:

Der p 10

Biological function:

Group 10 (Tropomyosin)

Allergen code:

d205

Molecular Weight:

37 kDa

Route of Exposure:

Inhalation

Source Material:

Located in the bodies of house dust mite. Native sourced from the extracts of Dermatophagoides pteronyssinus or recombinant

Summary

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.

Epidemiology

Worldwide distribution

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).

Environmental Characteristics

Source and tissue

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).

Clinical Relevance

Specific molecules

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).

Cross-reactive molecules

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
Nephropidae	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

Family	Whole allergen	Allergen component

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
Haliotidae	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

Family	Whole allergen	Allergen component

Biochemistry

Der p 10 of HDM has a molecular weight of 37 kDa (1).

Isoforms, epitopes, antibodies

Der p 10.0101 is the major isoform Der p 10 (10).

Cross-reactivity

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).

Diagnostic Relevance

Disease Severity

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).

AIT Prescription

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).

Compiled By

Author: Turacoz Healthcare Solutions

Reviewer: Dr. Christian Fischer

Last reviewed: November 2020

References

Burney P, Potts J, Kummeling I, Mills E, Clausen M, Dubakiene R, et al. The prevalence and distribution of food sensitization in E uropean adults. Allergy. 2014;69(3):365-71.
Ballmer-Weber BK, Lidholm J, Lange L, Pascal M, Lang C, Gernert S, et al. Allergen recognition patterns in walnut allergy are age dependent and correlate with the severity of allergic reactions. The Journal of Allergy and Clinical Immunology: In Practice. 2019;7(5):1560-7. e6.
Lee J, Jeong K, Jeon S-a, Lee S. Component resolved diagnosis of walnut allergy in young children: Jug r 1 as a major walnut allergen. Asian Pacific Journal of Allergy and Immunology. 2019.
Ciprandi G, Pistorio A, Silvestri M, Rossi GA, Tosca MA. Walnut anaphylaxis: the usefulness of molecular-based allergy diagnostics. Immunology letters. 2014;161(1):138-9.
Jeong K, Lee SY, Ahn K, Kim J, Lee HR, Suh DI, et al. A multicenter study on anaphylaxis caused by peanut, tree nuts, and seeds in children and adolescents. Allergy. 2017;72(3):507-10.
Sato S, Yamamoto M, Yanagida N, Ito K, Ohya Y, Imai T, et al. Jug r 1 sensitization is important in walnut-allergic children and youth. The Journal of Allergy and Clinical Immunology: In Practice. 2017;5(6):1784-6. e1.
Sordet C, Culerrier R, Granier C, Rancé F, Didier A, Barre A, et al. Expression of Jug r 1, the 2S albumin allergen from walnut (Juglans regia), as a correctly folded and functional recombinant protein. Peptides. 2009;30(7):1213-21.
Rasi Varaee FS, Gholamin M, Vakili Moghadam M, Mohammadi M, Mokhtarian K, Jafari R, et al. Cloning and Expression of 2S Albumin As a Major Allergen of Persian Walnut. Immunoregulation. 2020;3(1):51-60.
Costa J, Carrapatoso I, Oliveira M, Mafra I. Walnut allergens: molecular characterization, detection and clinical relevance. Clinical & Experimental Allergy. 2014;44(3):319-41.
Comstock S, McGranahan G, Peterson W, Teuber SS. Extensive in vitro cross‐reactivity to seed storage proteins is present among walnut (Juglans) cultivars and species. Clinical & Experimental Allergy. 2004;34(10):1583-90.
Rosenfeld L, Shreffler W, Bardina L, Niggemann B, Wahn U, Sampson HA, et al. Walnut allergy in peanut-allergic patients: significance of sequential epitopes of walnut homologous to linear epitopes of Ara h 1, 2 and 3 in relation to clinical reactivity. International archives of allergy and immunology. 2012;157(3):238-45.
Elizur A, Appel MY, Nachshon L, Levy MB, Epstein-Rigbi Na, Pontoppidan B, et al. Walnut oral immunotherapy for desensitisation of walnut and additional tree nut allergies (Nut CRACKER): a single-centre, prospective cohort study. The Lancet Child & Adolescent Health. 2019;3(5):312-21.
Robotham JM, Hoffman GG, Teuber SS, Beyer K, Sampson HA, Sathe SK, et al. Linear IgE-epitope mapping and comparative structural homology modeling of hazelnut and English walnut 11S globulins. Molecular immunology. 2009;46(15):2975-84.
Guo X, Jiang S, Li X, Yang S, Cheng L, Qiu J, et al. Sequence analysis of digestion-resistant peptides may be an efficient strategy for studying the linear epitopes of Jug r 1, the major walnut allergen. Food Chemistry. 2020:126711.
Downs ML, Semic-Jusufagic A, Simpson A, Bartra J, Fernandez-Rivas M, Rigby NM, et al. Characterization of low molecular weight allergens from English walnut (Juglans regia). Journal of agricultural and food chemistry. 2014;62(48):11767-75.
Mew R, Borres M, Sjölander S, du Toit G. A retrospect study into the utility of allergen components in walnut allergy. Pediatric allergy and immunology: official publication of the European Society of Pediatric Allergy and Immunology. 2016;27(7):750.
Weinberger T, Sicherer S. Current perspectives on tree nut allergy: a review. Journal of asthma and allergy. 2018;11:41.
Treudler R. Update on in vitro allergy diagnostics. JDDG: Journal der Deutschen Dermatologischen Gesellschaft. 2012;10(2):89-99.