+
For Patients & Caregivers
For Lab Professionals
Welcome! Click here for Patient or Laboratory Professional content
Are you a healthcare professional?

The information in this website is intended only for healthcare professionals. By entering this site, you are confirming that you are a healthcare professional.

Are you a laboratory professional?

The information in this website is intended only for laboratory professionals. By entering this site, you are confirming that you are a laboratory professional.

d2 American house dust mite

Code d2
LOINC LP13994-6
Family Pyroglyphidae
Genus Dermatophagoides
Species Dermatophagoides farinae
Route of Exposure Inhalation
Source Material Whole body culture
Latin Name Dermatophagoides farinae
Other Names House dust mite, Dust mite
Categories Mites

Summary

House dust mites (HDMs) are the most important causes of allergic sensitization and allergic disease, including Dermatophagoides farinae as one of the principal species. Mites dominate in environments with temperate climates, damp, and humid dwellings. The HDM fecal pellets are reported to be the major source of allergens causing allergic reactions after inhalation. Mite allergens can trigger the symptoms in a sensitized individual through inhalation, ingestion and direct contact. Out of all the D. farinae allergens listed, Der f 1, Der f 2, Der f 11 and Der f 23 are the major allergens. A high degree of cross-reactivity is noted between D. pteronyssinus and D. farinae extracts, whereas the reactivity between Dermatophagoides and Blomia tropicalis is limited. Furthermore, a high degree of cross-reactivity is also observed between Der p 1 and Der f 1, Der p 2 and Der f 2, and between Der f 23 and Der p 23. Tropomyosins play an important role in the cross-reactivity. It has been reported that tropomyosin allergens from HDMs cross-react with crustaceans (shrimp, lobster, crab, crayfish) and mollusks (mussel, oyster, scallop, clams, abalone, snails, squid, octopus, cuttlefish). Furthermore, Der f 10 is found to be cross-reactive with Blo t 10, Lep d 10, Pen a 1, Per a 7 and Hom a 1.

Allergen

Nature

Globally, house dust mites (HDMs) are the most important causes of allergic sensitization and allergic diseases. The HDMs are reported to colonize to the indoor environment, and the allergens of HDM target the epithelium of humans, thus demonstrating the unique characteristics of HDMs (1).

The most important HDM species are Dermatophagoides farinae (D. farinae), Dermatophagoides pteronyssinus (D. pteronyssinus) and Euroglyphus maynei (E. maynei). The characteristics of D. farinae co-exists with that of the storage mite, Blomia tropicalis (B. tropicalis), found in the subtropical and tropical areas, as a major source of mite allergen (1, 2).

D. farinae produces one or two eggs in a day, however, it can sometimes even lay 5 or 6 eggs per day (3). The adult mites have nonsegmental bodies that measure between 250 to 350 μm in length. The HDMs move on 8 legs and possess hair-like structure on their entire body, that functions as feelers. Further, the suction cup-like feature on their feet help the mites to stick to the surfaces (1).

Habitat

House dust mites are most prevalent in the indoor environment of every household, located in the temperate areas. It is reported that mites survive the dry winters with humid, temperate climates. High allergen levels of mites are reported in older homes, and in homes that are devoid of air-conditioning, as compared to those with air-conditioners (1). The longevity of D. farinae male and female species differ, with the duration of survival between 18 to 64 days in males and 20 to 54 days in females (1, 3). Furthermore, the female species achieve its complete cycle of egg to adult in 35 days, when the optimum temperature is between 23-30°C (1, 3). However, the time duration of their survival might increase, with an increase in the temperature and humidity in environment (1).

Taxonomy

Taxonomic tree of D.farinae (1,4)
Domain Eukaryota
Kingdom Metazoa
Phylum Arthropoda
Subphylum Chelicerata
Class Arachnida
Order Sarcoptiformes
Family Pyroglyphidae
Genus Dermatophagoides
Species Dermatophagoides farinae

 

Tissue

Mites, including D. farinae, during its lifespan produces ~1000 solid wastes, each measuring about 25 µ diameter (1). The fecal pellets of HDM (including D. farinae) are reported to be the major source of allergen carrier in air, causing allergic reactions after inhalation (1, 5). Further, the pellets become transiently airborne during disturbance brought about by human activities, such as sweeping, dusting, vacuuming, or changing bedding (2). 

Epidemiology

Worldwide distribution

Generally, high altitudes are not favorable place for dust mites to live in, and hence it is important to know that, even before the dust mites were discovered, sanitaria were frequently built for patients with respiratory diseases, e.g., in the Alps (Europe) and Denver, CO (USA) (1). Low sensitization and growth of dust mites have been observed in the Alps than at sea level, due to the lower indoor humidity observed at high altitudes (6, 7). However, contrasting results were obtained in a study conducted at high altitudes in a tropical developing country. According to this cross-sectional study, 87.9% of asthmatic children were found positive to at least one HDM type (n=61). Further, out of the sensitized children, 70.7% showed sensitivity to D. farinae (8).

According to a systematic analysis conducted on 163 articles, involving 114,302 allergic cases in China, the rate of D. farinae sensitization was reported to be 75.2% in patients with allergic rhinitis (AR), whereas it was 78.5% in patients with allergic asthma (9).

Environmental Characteristics

Worldwide distribution

Dust mites are found worldwide, except in the Arctic and Antarctic (1). Mites dominate in the environment, that has temperate climate, with damp and humid dwellings. Countries with such environment, include Scotland, Europe (West and Central), New Zealand, Australia, England, areas of United States and South America, where homes are both warm and damp. In contrast, in northern region of Europe, where the climate is extremely cold and dry, the mites cannot survive the weather ​(5).

The species of Dermatophagoides are found throughout the world, including the United States, South America, Hawaii, the Middle East, Canada, Europe, Asia, parts of Australia, and Africa. D. farinae are most commonly found in the United States, whereas in United Kingdom, it is less commonly seen (3). 

Route of Exposure

Main

Airway inhalation is the primary route of exposure to HDM. It has been reported that post-inhalation of a dust mite allergen, reduction in mucociliary clearance is observed, which in turn is found to escalate the deposition of inhaled particles (10). Further, it has been found that exposure of HDM allergen can act as a trigger in exacerbating the existing condition of asthma (1).

Detection

Mite allergens can trigger the allergic symptoms in a sensitized person through various routes, including inhalation (asthma, AR, eczema), ingestion (anaphylaxis, urticaria), and direct contact (conjunctivitis, eczema) (1).

Mite-allergic patients with asthma might also have symptoms of AR. This supports the “unified airway” concept that asthma and AR may not be separate entities, but rather linked manifestations of allergic inflammation, occurring throughout the upper and lower airways (11).

According to a 13-month, multicenter survey, severe or very severe burden of AR and asthma, caused by HDM was noted in terms of irritability, tiredness, disturbed sleep, and troublesome professional life (12).

Allergic rhinitis

According to a study conducted in China (Qingdao region), D. farinae was responsible for causing AR in 66.4% of children (1887 out of 2841 children). It was reported that sensitization to HDM was more in older children with AR, particularly the males. Clinical manifestations of AR are likely to have an effect on studies, work productivity and efficiency, as well as the quality of life (13).

Asthma

Many patients are unaware that dust mites are a trigger for their asthma, yet report symptoms of sneezing, wheezing or eye irritation while performing their activities, such as house cleaning, or upon waking up (5).

Exposure to HDM during early childhood elevates immunoglobulin E (IgE) levels, which in turn predisposes to asthma. Mite allergy is a major risk factor for asthma, and sensitization to mites, early in life has a significant impact on pulmonary function (14).

A study was conducted in 2087 allergic patients, out of which, 82% of patients demonstrated a positive skin prick test (SPT) for HDM allergens. D. farinae was one of the predominant species, with a prevalence of 61%. The dust allergen load (>10 µg/g) was notably higher in Der f 1 (57.6%) than Der p 1 (20%), thus indicating as a risk factor for the development of asthma (15).

In a cross-sectional study, 31% of severely asthmatic children were found to have an obstruction (forced expiratory volume in one second/forced vital capacity [FEV1/FVC] <80%). A significant correlation (Rho: −0.34; CI 95%: −0.55 to −0.09; P=0.008) was observed between FEV1/FVC and positive SPT, indicating the presence of obstruction. Further, it has been observed that an elevated risk of progressive lung function loss could be noted in children with asthma, atopy, and reduced pulmonary function (8).

Atopic dermatitis

The prevalence of sensitization to mites can be very high in patients with atopic dermatitis (AD). The increase in the permeability of atopic skin and the ability of mite proteases to decrease skin barrier function may allow more effective sensitization with aeroallergens, initiating a vicious cycle of inflammation and further allergen exposure (1).

A retrospective, cohort study was conducted on 102 children with AD (median age at onset: 1.5 years). Children were majorly sensitized to HDMs, including D. farinae and D. pteronyssinus, across all the age groups (<2 years, between 2-7 years and >7 years), however, sensitization to HDMs was higher in children >7 years of age (16).

Other 

Unintentional ingestion of dust mites in the form of food (contaminated with mites), can cause systemic allergic symptoms (1). In a case of a 48-year-old male, ingestion of fried pastry, prepared from flour contaminated with D. farinae, led to anaphylaxis (1, 17).

Prevention and Therapy

Allergen immunotherapy

According to evidence, sublingual immunotherapy (SLIT) could be considered as a safe and effective route of administration. In a retrospective study conducted among 282 children with AR in China, SLIT with D. farinae drops was found to be safe and efficacious in pre-school and school-age children with AR, induced by HDMs (18).

Prevention strategies

Avoidance

The exposure of HDMs can be prevented or reduced by wrapping the mattresses, pillows, and box springs in coverings, that are allergen-proof, washing the bedding with hot water in a week, cleaning the house, wearing an appropriate mask while cleaning, changing furnace and air-conditioner filters, and using a dehumidifier, that help in decreasing the humidity in homes (2).

In a study conducted in Malaysia, use of commercial ionizer was found to be successful as well as effective in increasing the mortalities in mites (including D. farinae and D. pteronyssinus) by increasing the length of exposure time of ionizer. It has been reported that production of negative ions by the ionizer had the capability of killing the HDMs and further decreasing the population of natural mites on surfaces, such as clothes, mattresses, floors, curtains, etc. (19).

In mite-sensitized asthmatic patients, bronchial hyperreactivity and bronchospasm was found to be aggravated, upon exposure to mites, however, the symptoms got improved in mite-free environment (1). Decreased exposure to mites in patients with mite allergy can be an effective tool in managing allergic patients, such as asthma (20). 

Molecular Aspects

Allergenic molecules

The recognition of HDM-specific allergens helps in the diagnosis and treatment of allergic diseases, associated with HDM, especially identification and characterization of novel HDM allergens (21). The allergens of D. farinae listed in the WHO/IUIS database include (22). 

Allergen Biochemical name Molecular Weight (kDa) Allergenicity
Der f 1 Cysteine protease 27
  • Major allergen.
  • In a study, positive SPT with 10-5 ug/mL of Der f 1 was observed in 10 out of 13 mite-allergic patients. Further, 87% of 63 RAST-positive mite-allergic patients showed IgE antibodies to Der f 1 (22, 23).
Der f 2 NPC2 family 15
  • Major allergen.
  • In a study, 94% of 51 sera from mite-allergic patients showed IgE antibody to purified form of Der f 2, as measured by radioimmunoassay (24). After measuring via RAST, 18 out of 20 mite-allergic patients had IgE antibodies to purified form of Der f 2 (22, 25).
Der f 3 Trypsin 29  
Der f 4 Alpha-amylase 57.9  
Der f 5 Low molecular weight IgE binding protein 15.5  
Der f 6 Chymotrypsin 25  
Der f 7 Bactericidal permeability-increasing like protein 30-31  
Der f 8 Glutathione S-transferase 32  
Der f 10 Tropomyosin 37
  • In a study, 80.6% (25/31) of mite-allergic patients, demonstrated IgE binding to purified form of Der f 10, after testing via dot spot test. Six patients out of 13 had positive skin reactions to Der f 10 (22, 26).
Der f 11 Paramyosin 98
  • Major allergen.
  • In one panel, IgE binding to purified Der f 11 was observed in 87.5% (21 out of 24) sera from patients demonstrating with positive skin response to mites, after an immunodot assay (22, 27).
Der f 13 Fatty acid binding protein 15  
Der f 14 Apolipophorin     177  
Der f 15 Chitinase 98/109  
Der f 16 Gelsolin/villin 53  
Der f 17 Calcium-binding protein 53  
Der f 18 Chitin-binding protein 60  
Der f 20 Arginine kinase 40  
Der f 21 Not determined 14  
Der f 22 Not determined 14.7  
Der f 23 Peritrophin-like protein 19
  • Major allergen.
  • ELISA revealed that HDM-allergic sera from 72 of 129 (55.8%) allergic patients, showed sIgE-binding activity with Der f 23 (21).
Der f 24 Ubiquinol-cytochrome c reductase binding protein homologue 13  
Der f 25 Triosephosphate isomerase 34  
Der f 26 Myosin alkali light chain 18  
Der f 27 Serpin 48  
Der f 28 Heat Shock Protein 70  
Der f 29 Peptidyl-prolyl cis-trans isomerase (cyclophilin) 15  
Der f 30 Ferritin 15  
Der f 31 Cofilin 15  
Der f 32 Secreted inorganic pyrophosphatase 35  
Der f 33 Alpha-tubulin 52  
Der f 34 Enamine/imine deaminase 16  
Der f 35 Not determined 14.4  
Der f 36 Not determined 23  
Der f 37 Chitin binding protein 29  
Der f 38 Bacteriolytic enzyme 15  
Der f 39 Troponin C 18  

Der f: Dermatophagoides farinae; IgE: Immunoglobulin E; RAST: Radioallergosorbent; ELISA: Enzyme-linked immunosorbent assay; SPT; Skin prick test.

The prevalence of IgE reactivity was observed to be 94.7%, of the total HDM extract, in a study conducted on 129 HDM-allergic Korean patients. It was reported that 79.1% of patients showed specific IgE to Der f 1 and Der f 2. Further, 9.3%, 6.2%, 7%, and 7% of patients showed IgE reactivities to Der f 6, Der f 8, Der f 10, and Der f 20, respectively. In HDM-allergic patients having respiratory allergy and AD, Der f 2 was the most sensitized allergen. Further, the diagnostic sensitivity was reported to be increased with the combination of the group 1 (Der f 1) and 2 (Der f 2) major allergens (28).

Apart from the WHO/IUIS list, another allergen of D. farinae, Der f Alt a 10 has been described by a study. According to the findings reported in this study, 32.7% of AD patients were sensitized to Der f Alt a 10, in comparison to 3.0% in patients with allergic asthma/AR (29).

Cross-reactivity

The allergic sensitivity, following the ingestion of HDMs, show symptoms in two different forms - the ingestion of invertebrates demonstrating cross-reactivity with mite allergens, and the ingestion of foods that are contaminated with dust mites (1).A high degree of cross-reactivity is noted between D. pteronyssinus and D. farinae extracts, however, the reactivity between Dermatophagoides and B. tropicalis has been reported to be low (5).

According to a study, co-sensitization and cross-reactivity has been reported between B. tropicalis and two Dermatophagoides species, i.e., Der p and Der f. In this study, 70.14% of allergenic patients (1050 out of 1497 patients) were found to be co‐sensitized to B. tropicalis, Der p, and Der f. However, the cross-reactivity between B. tropicalis and  Dermatophagoides was limited (30).

The structural similarities between Der p 1 and Der f 1 was demonstrated with an X-ray crystal structure analysis. The analysis showed a surface conservation of a crystal structure of natural Der f 1 with Der p 1, having 71% of amino acid similarity, along with an overlapping catalytic area. This high structural similarity observed between Der p 1 and Der f 1 are commonly believed to be the basis for their cross-reactivity (31, 32).

A high degree of cross-reactivity has also been reported between Der p 2 and Der f 2 (from D. farinae) (33).

Group 11 allergens (Der p 11, Der f 11) are considered as major allergen molecules in patients with AD, having sensitization to HDM, and thus should be included among allergen components for the routine testing in the clinical laboratory (34).

A high amino acid sequence similarity has been found between Der p 23 and Der f 23 (87%). Different structural studies of Der p 23 and consecutive modelling of Der f 23 on its structure, might imply on the occurrence of considerable cross-reactivity between the two proteins (35).

Der f 10 (tropomyosin from Der f) and Der p 10 of HDM, both are found be cross-reactive with Lep d 10 (tropomyosin from the storage mites), due to high level of homology (36).

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 (37).

One of the most important cause of cross-reactivity, among mites, shellfish, helminths, and cockroaches is the Tropomyosin, although glutathione transferase may also be included. In cases where genuine sensitization is unclear, specific allergen components can be useful to identify primary allergy (5).

Tropomyosin allergens from HDMs are reported to show cross-reactivity with tropomyosin allergens of invertebrates, such as crustaceans (shrimp, lobster, crab, crayfish), mollusks (mussel, oyster, scallop, clams, abalone, snails, squid, octopus, cuttlefish) and insects (cockroaches) (1, 37).

Der f 10 allergen has shown sequence similarity with shrimp tropomyosin Pen a 1, American cockroach tropomyosin Per a 7, and lobster tropomyosin Hom a 1 (38).

Further, cross-reactivity has been reported between HDM and shrimp-reactive IgE antibodies, in patients with shrimp allergy (39). In patients with allergy to HDMs, reactivity to shrimp has also been revealed, especially in patients who were never been exposed to shrimps, because of religious dietary habits (40).

Compiled By

Author: Turacoz Healthcare Solutions

Reviewer: Dr. Christian Fischer

 

Last reviewed: January 2021

References
  1. Miller JD. The Role of Dust Mites in Allergy. Clin Rev Allergy Immunol. 2019;57(3):312-29.
  2. Portnoy J, Miller JD, Williams PB, Chew GL, Miller JD, Zaitoun F, et al. Environmental assessment and exposure control of dust mites: a practice parameter. Ann Allergy Asthma Immunol. 2013;111(6):465-507.
  3. Sarwar. House Dust Mites: Ecology, Biology, Prevalence, Epidemiology and Elimination. 2020.
  4. NCBI. Dermatophagoides farinae. 2020 [16.12.2020]. Available from: https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=6954&lvl=3&keep=1&srchmode=1&unlock&lin=s&log_op=lineage_toggle.
  5. Thomas Platts-Mills LC. DUST MITE ALLERGY B04. USING MOLECULAR ALLERGOLOGY IN THE CLINICAL PRACTICE. P M. Matricardi, J. Kleine-Tebbe. EACCI MOLECULAR ALLERGOLOGY USER’S GUIDE. 2016:105-13.
  6. Vervloet. Altitude and house dust mites. Journal of Allergy and Clinical Immunology, Volume 69, Issue 3. 1982:290-6.
  7. Charpin D, Birnbaum J, Haddi E, Genard G, Lanteaume A, Toumi M, et al. Altitude and allergy to house-dust mites. A paradigm of the influence of environmental exposure on allergic sensitization. Am Rev Respir Dis. 1991;143(5 Pt 1):983-6.
  8. Duenas-Meza E, Torres-Duque CA, Correa-Vera E, Suarez M, Vasquez C, Jurado J, et al. High prevalence of house dust mite sensitization in children with severe asthma living at high altitude in a tropical country. Pediatr Pulmonol. 2018;53(10):1356-61.
  9. Chen ZG, Li YT, Wang WH, Tan KS, Zheng R, Yang LF, et al. Distribution and Determinants of Dermatophagoides Mites Sensitization ofAllergic Rhinitis and Allergic Asthma in China. Int Arch Allergy Immunol. 2019;180(1):17-27.
  10. Bennett WD, Herbst M, Alexis NE, Zeman KL, Wu J, Hernandez ML, et al. Effect of inhaled dust mite allergen on regional particle deposition and mucociliary clearance in allergic asthmatics. Clin Exp Allergy. 2011;41(12):1719-28.
  11. Marple BF. Allergic rhinitis and inflammatory airway disease: interactions within the unified airspace. Am J Rhinol Allergy. 2010;24(4):249-54.
  12. Demoly. The disease burden in patients with respiratory allergies induced by house dust mites: a year-long observational survey in three European countries. . Clin Transl Allergy 10, 27 (2020) https://doiorg/101186/s13601-020-00331-0. 2020.
  13. Lin H, Lin R, Li N. Sensitization Rates for Various Allergens in Children with Allergic Rhinitis in Qingdao, China. Int J Environ Res Public Health. 2015;12(9):10984-94.
  14. Shin JW, Sue JH, Song TW, Kim KW, Kim ES, Sohn MH, et al. Atopy and house dust mite sensitization as risk factors for asthma in children. Yonsei Med J. 2005;46(5):629-34.
  15. Shafique RH, Akhter S, Abbas S, Ismail M. Sensitivity to house dust mite allergens and prevalence of allergy-causing house dust mite species in Pothwar, Pakistan. Exp Appl Acarol. 2018;74(4):415-26.
  16. Somanunt S, Chinratanapisit S, Pacharn P, Visitsunthorn N, Jirapongsananuruk O. The natural history of atopic dermatitis and its association with Atopic March. Asian Pac J Allergy Immunol. 2017;35(3):137-43.
  17. Erben AM, Rodriguez JL, McCullough J, Ownby DR. Anaphylaxis after ingestion of beignets contaminated with Dermatophagoides farinae. J Allergy Clin Immunol. 1993;92(6):846-9.
  18. Tang LX, Yang XJ, Wang PP, Ge WT, Zhang J, Guo YL, et al. Efficacy and safety of sublingual immunotherapy with Dermatophagoides farinae drops in pre-school and school-age children with allergic rhinitis. Allergol Immunopathol (Madr). 2018;46(2):107-11.
  19. Abidin SZ, Ming HT. Effect of a commercial air ionizer on dust mites Dermatophagoides pteronyssinus and Dermatophagoides farinae (Acari: Pyroglyphidae) in the laboratory. Asian Pac J Trop Biomed. 2012;2(2):156-8.
  20. van der Heide S, De Monchy JG, De Vries K, Dubois AE, Kauffman HF. Seasonal differences in airway hyperresponsiveness in asthmatic patients: relationship with allergen exposure and sensitization to house dust mites. Clin Exp Allergy. 1997;27(6):627-33.
  21. He Y, Dou C, Su Y, Chen J, Zhang Z, Zhao Z, et al. Identification of Der f 23 as a new major allergen of Dermatophagoides farinae. Mol Med Rep. 2019;20(2):1270-8.
  22. WHO/IUIS. ALLERGEN NOMENCLATURE. WHO/IUIS Allergen Nomenclature Sub-Committee. 2019. Available from: http://www.allergen.org/search.php?Species=Dermatophagoides%20farinae.
  23. Heymann PW, Chapman MD, Platts-Mills TA. Antigen Der f I from the dust mite Dermatophagoides farinae: structural comparison with Der p I from Dermatophagoides pteronyssinus and epitope specificity of murine IgG and human IgE antibodies. J Immunol. 1986;137(9):2841-7.
  24. Heymann PW, Chapman MD, Aalberse RC, Fox JW, Platts-Mills TA. Antigenic and structural analysis of group II allergens (Der f II and Der p II) from house dust mites (Dermatophagoides spp). J Allergy Clin Immunol. 1989;83(6):1055-67.
  25. Yasueda H, Mita H, Yui Y, Shida T. Isolation and characterization of two allergens from Dermatophagoides farinae. Int Arch Allergy Appl Immunol. 1986;81(3):214-23.
  26. Aki T, Kodama T, Fujikawa A, Miura K, Shigeta S, Wada T, et al. Immunochemical characterization of recombinant and native tropomyosins as a new allergen from the house dust mite, Dermatophagoides farinae. J Allergy Clin Immunol. 1995;96(1):74-83.
  27. Tsai LC, Chao PL, Shen HD, Tang RB, Chang TC, Chang ZN, et al. Isolation and characterization of a novel 98-kd Dermatophagoides farinae mite allergen. J Allergy Clin Immunol. 1998;102(2):295-303.
  28. Jeong KY, Lee JY, Son M, Yi MH, Yong TS, Shin JU, et al. Profiles of IgE Sensitization to Der f 1, Der f 2, Der f 6, Der f 8, Der f 10, and Der f 20 in Korean House Dust Mite Allergy Patients. Allergy Asthma Immunol Res. 2015;7(5):483-8.
  29. Park KH, Lee J, Lee JY, Lee SC, Sim DW, Shin JU, et al. Sensitization to various minor house dust mite allergens is greater in patients with atopic dermatitis than in those with respiratory allergic disease. Clin Exp Allergy. 2018;48(8):1050-8.
  30. Liu. Co‐sensitization and cross‐reactivity of Blomia tropicalis with two Dermatophagoides species in Guangzhou, China. Journal of Clinical Laboratory Analysis 33 101002/jcla22981 2019.
  31. Chruszcz M, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W, et al. Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding. J Mol Biol. 2009;386(2):520-30.
  32. Glesner J, Vailes LD, Schlachter C, Mank N, Minor W, Osinski T, et al. Antigenic Determinants of Der p 1: Specificity and Cross-Reactivity Associated with IgE Antibody Recognition. J Immunol. 2017;198(3):1334-44.
  33. Panzner P, Vachova M, Vlas T, Vitovcova P, Brodska P, Maly M. Cross-sectional study on sensitization to mite and cockroach allergen components in allergy patients in the Central European region. Clin Transl Allergy. 2018;8:19.
  34. Conti. Identification by serological proteome analysis of paramyosin as prominent allergen in dust mite allergy,. Journal of Proteomics, Volume 166, 2017 Pages 19-26. 2017.
  35. Mueller GA, Randall TA, Glesner J, Pedersen LC, Perera L, Edwards LL, et al. Serological, genomic and structural analyses of the major mite allergen Der p 23. Clin Exp Allergy. 2016;46(2):365-76.
  36. C. Hilger AK, M. Raulf, A. Pomés, and T. Jakob. Chapter 23. Cockroach, Tick, Storage Mite, and Other Arthropod Allergies: Molecular Aspects. J Kleine-Tebbe, T Jakob (eds), Molecular Allergy Diagnostics Springer International Publishing Switzerland 2017. 2017:429-44.
  37. Popescu FD. Cross-reactivity between aeroallergens and food allergens. World J Methodol. 2015;5(2):31-50.
  38. Ayuso R, Reese G, Leong-Kee S, Plante M, Lehrer SB. Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactive epitopes of shrimp, house dust mite and cockroach tropomyosins. Int Arch Allergy Immunol. 2002;129(1):38-48.
  39. van Ree R, Antonicelli L, Akkerdaas JH, Pajno GB, Barberio G, Corbetta L, et al. Asthma after consumption of snails in house-dust-mite-allergic patients: a case of IgE cross-reactivity. Allergy. 1996;51(6):387-93.
  40. Lopata AL, Kleine-Tebbe J, Kamath SD. Allergens and molecular diagnostics of shellfish allergy: Part 22 of the Series Molecular Allergology. Allergo J Int. 2016;25(7):210-8.