Dermatophagoides farinae

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Code: d2
Latin name: Dermatophagoides farinae
Source material: Whole body culture
Family: Pyroglyphidae
Common names: House dust mite, dust mite

Allergen Exposure

Geographical distribution

See common geographical background to mites in the Introduction.

The most important House dust mites are Dermatophagoides farinae, which is more common in drier areas, and D. pteronyssinus. D. farinae has many of the same characteristics as D. pteronyssinus, which co-exists with the Storage mite Blomia tropicalis in subtropical and tropical regions as a major source of allergens. Recent evidence shows that even these very general boundaries are blurring and that in many instances all 3 mite species may be highly relevant, causing frequent sensitisation.

The prevalence of allergic reactions to the mite species D. farinae is shown to be extremely high in North America and Japan. However, large numbers of this species have also been found in parts of Italy and Turkey, and in the Far East outside Japan.

The Dermatophagoides species are very similar but have differences in some physical characteristics: for example, in the male ventral posterior idiosoma and the aedeagus, and in the female genital opening and bursa copulatrix. The morphologically most conspicuous difference in the 3 Dermatophagoides species is that there are no 4 long train hairs on the abdomen end.

D. farinae is found worldwide but it is more abundant in North America than in Europe. It seems to prefer more continental and barren climates than D. pteronyssinus does. The duration of the life cycle from egg to adult is 35 days, and the female longevity is approx 70 days, but these periods depend on the temperature and humidity of the environment. D. farinae lays eggs over a 30- day period, producing about an egg a day, while D. pteronyssinus lays about 80 -120 eggs over a 45-day period.


See common environmental background to mites in the Introduction.


The most important allergenic proteins in D. farinae are Der f 1 and Der f 2. It has been shown that approximately 80% of tested sera from mite-sensitive patients have IgE antibodies to Der p 1 and Der p 2, and the situation is very likely similar for Der f 1 and Der f 2, as the Group 1 and 2 allergens are highly homologous between D. farinae and D. pteronyssinus (1). About 20% of patients, however, do not have IgE antibodies to the Group 1 and 2 allergens, and even though this is a minority, it constitutes a large population. There are many other House dust mite allergens which have high IgE binding activity, but these are present in low and variable concentrations in mite extracts, usually at less than 1% of

the levels of the Group 1 and 2 allergens. But importantly, mite extracts are preparations that do not accurately represent the relative concentrations of allergens in inhaled air. In fact, mite extracts used for commercial testing may not mimic the native mite allergen environment in general at all accurately. All that can broadly be said about the concentrations of most allergens is that these are unknown but are probably sparse (1).

The results of studies on allergen groups other than 1 and 2 may be extrapolated to D. pteronyssinus and D. farinae. Experiments measuring the trypsin enzymatic activity of Der p 3 and demonstrating a 200-fold higher concentration in spent mite media (2) will likely hold for Der f 3. The case would be similar for studies of further relevant allergens: Der p 5, 10, 11 and 14, which appear to be present in low quantities (3-5). There is evidence that Der p 3, 7 and 14 are unstable in the extracts (1); nonetheless, allergens present in low amounts in extracts can induce high titres of IgE. Also, nonallergenic polypeptides such as the ferritin heavy chain may be highly immunogenic and induce a balanced Th1/Th2 cytokine response (6)

The following recombinant allergens have been characterised:

  • rDer f 1 (8-10,12,15-16).
  • rDer f 2 (12,19).
  • rDer f 3 (26).
  • rDer f 6 (31).
  • rDer f 7 (33).
  • rDer f 11 (35-37,48-49).
  • rDer f 14 (40).
  • rDer f 16 (44).

The major House dust mite Group 1 allergens Der p 1 and Der f 1 are the most potent of indoor allergens (15). Both allergens are major allergens and result in sensitisation in approximately 80% or greater of D. farinae-sensitised patients (1,30). Although Der p 1 and Der f 1 were first isolated as cysteine proteases, some studies reported that natural Der f 1, similarly to Der p 1, exhibits mixed cysteine and serine protease activity (7).

Der f 1 and Der f 2 sensitise approximately 80% to 90% of D. farinaesensitised individuals. Most patients (80%) appear to have IgE antibodies to more than 1 allergen. Similarly to Der p 1 and Der p 2, Der f 1 and Der f 2 exist as a number of isoforms. rDer f 1 and rDer f 2 are highly homologous to the native forms. The Group 2 allergens induce humoral and cellular responses in 80-90% of mite-allergic individuals (13).

Although Der p 3 was reported to sensitise approximately 50% of D. pteronyssinus-sensitised patients (1), and although the same may hold true for Der f 3, IgE to Der f 3 was detected in only 16% of the sera tested in one study (13).

In sera from 88 mite-allergic patients, IgE antibodies to Der p 6 and/or Der f 6 were detected in only 41% of the sera (30).

The Group 7 mite allergens react with IgE antibodies in 50% of sera from allergic patients (32).

Der f 10, a tropomyosin, is a major allergen and has been shown to react with IgE antibodies in over 80% of mite-sensitised patients (3).

Der f 11, a paramyosin, has been shown to be a major allergen (37). IgE reactivity to Der f 11 was reported for more than 80% of mite-sensitive asthmatic patients (4). Skin reactivity and IgE antibodies showed that 62% (13/21) and 50% (10/20) of mitesensitive asthmatic patients reacted positively with the recombinant Der f 11, respectively (37). This is similar to findings about rDer p 11, which detected IgE antibodies in a range of 41.7% to 66.7% in different allergic patient groups (36). In a preliminary study of 18 asthmatic children, 72.2% reacted positively to rDer f 11, and 88.9% showed positive reactivity to D. farinae extracts. Further evaluation of rDer f 11 in 24 asthmatic children who were skin test-positive to mite found that, whereas 70.8% had positive skin tests to rDer f 11, 75% had positive serum IgE reactivity to rDer f 11. Serum IgE reactivity to rDer f 11 was further investigated in a large panel of 49 mite skin test-positive asthmatic children, and similarly to before, 77.6% had positive serum IgE reactivity to rDer f 11 (49).

Der f 14 has also been demonstrated to be a major allergen, detecting IgE antibodies in 65.8% of 38 sera samples from patients allergic to mites. Der f 14 is a proteasesensitive allergen. The breakdown products of this allergen provoked higher allergenic activity than did the intact allergen (5).

The House dust mites D. pteronyssinus and D. farinae cause allergic disease in dogs as well as humans. In geographical regions where the 2 mite species coexist, they both elicit specific IgE responses in humans, whereas dogs preferentially react to D. farinae extracts. In dogs the main IgE binding is directed to the D. farinae chitinase allergens Der f 15 and Der f 18, and not to the groups 1 and 2 allergens, as is found for humans (42). However, one study, aimed at characterising the chitinase allergens Der p 15 and Der p 18 of D. pteronyssinus and discovering whether they are important allergens for humans, as they are for dogs, reported that Der p 15-specific IgE was detected in 70% and Der p 18-specific IgE in 63% of a panel of 27 human allergic sera. The D. pteronyssinus chitinases Der p 15 and Der p 18 show a high frequency of binding to IgE in allergic human sera. Theyare therefore potentially important allergens for humans as well as dogs (42).

rDer f 16 protein was shown to bind IgE from mite-allergic patients at a 47% (8/17) frequency (44).

rDer f 18 binds IgE in 54% of the sera from patients with D farinae allergy (45).

Potential cross-reactivity

Allergens from mites have both common and species-specific determinants. Allergenic determinants in D. farinae are shared with other mites belonging to the Pyroglyphidae family and are highly cross-reactive with other Dermatophagoides species (50-51). There seems to be a limited cross-reactivity with Storage (nonpyroglyphid) mites (51). Allergen cross-reactivity has been reported between House dust mites and other invertebrates (52).

In a study that investigated the individual allergens responsible for the cross-reactivity between D. siboney and other mite allergens in mite-allergic patients, IgE inhibition was shown to be higher with D. farinae (86%), D. pteronyssinus (54%) and D. microceras (49%) extracts than with Lepidoglyphus destructor (20%), Tyrophagus putrescens (11%), Acarus siro (18%) and Blomia tropicalis (6%) extracts. A diverse pattern for the individual allergens was demonstrated. The N-terminal sequences of Der s 1, 2 and 3 allergens showed higher homology to D. farinae and D. microceras than to D. pteronyssinus. The homology of the Group 2 allergens was higher than that of the Group 1 allergens. The individual allergens of D. siboney were more similar to those of D. farinae and D. microceras than to those of D. pteronyssinus. There was a limited and variable cross-reactivity with nonpyroglyphid mites. No single allergen was unique to D. siboney (53).

Although a high prevalence of sensitisation occurs to the Group 1 mite allergen Blo t 1 from Blomia, there was a low correlation of IgE reactivity between this allergen and the Group 1 mite allergen Der p 1 (54), and presumably Der f 1, an allergen highly homologous to Der p 1. Pso o 1 from the Sheep scab mite (Psoroptes ovis) displays strong homology to the Group 1 House dust mite allergens Der p 1, Der f 1 and Eur m 1 (55).

Der f 7 has a predicted 213 residue polypeptide with 86% homology to and serological cross-reactivity with Der p 7 (33).

D f 10 is a tropomyosin. The tropomyosin of the American cockroach Periplaneta americana has an 80%, 81%, and 82% sequence identity to the tropomyosins from D. pteronyssinus, D. farinae, and Shrimp, respectively, which have been previously shown to be important allergens (56). The IgE recognition by Shrimp-allergic individuals of similar amino acid sequences, homologous to Pen a 1 epitopes in mite, Cockroach and Lobster tropomyosins, indicates the basis of the in vitro crossreactivity among invertebrate species. On the evidence of amino acid sequence similarity and epitope reactivity, Lobster tropomyosin has been shown to have the strongest and Cockroach the weakest crossreactivity with Shrimp (57). In sera of 30 patients tested and found to harbour P. fuliginosa-specific IgE, the IgE binding reactivity of the P. fuliginosa extract was inhibited as much as 79.4% by a B. germanica extract and as much as 63.3% by a D. farinae extract. The deduced amino acid sequence of cloned cDNA was identical to that of Periplaneta americana tropomyosin (58).

rDer p 11 showed positive IgE binding reactivity in 78% of 50 D. pteronyssinussensitive asthmatic children. Der p 11, a paramyosin, has an 89% sequence identity with Der f 11 and Blo t 11 (35,38). A second study reported the sequence identity of Der f 11 with other known paramyosins to be 34-60% (48).

Clinical Experience

IgE-mediated reactions

In 1964, when D. pteronyssinus and D. farinae were identified in house dust samples from all over the world, it became clear that mites of the genus Dermatophagoides were the main cause of asthmatic reactions (50,59-61). A large body of evidence suggests that exposure to the House dustmite allergens D. pteronyssinus and D. farinae is an important risk factor for allergic sensitisation, asthma development, and asthma symptom exacerbation (59,62-69).

Studies of house dust-allergic individuals around the world have shown that House dust mites cause symptoms such as perennial-type asthma, rhinitis and conjunctivitis, often with nocturnal or early morning episodes (70-73). A study of D. pteronyssinus allergens found that House dust mite extract constituents other than Der p 1 or Der p 2, with no significant influence on the IgE-mediated early asthmatic response, contribute significantly to the allergen-induced late asthmatic response and bronchial hyper-reactivity (74).

D. pteronyssinus has also been reported to play an important role as a trigger in patients with atopic dermatitis, including adult patients (75). However, in a crosssectional study of 1669 school beginners 6 to 7 years old in Augsburg (Bavaria, Germany), it was concluded that current eczema in these children were related to Der f 1 exposure and not to Der p 1 exposure (76). Patients in whom the House dust miteinduced reaction continues for more than 48 hours and contributes to eczematous eruptions are characterised by considerably increased levels of IgE antibodies for House dust mite antigens, high activity of atopic dermatitis, and increased exposure to House dust mite (77).

It is possible that a number of features ascribed to D. pteronyssinus will be applicable to D. farinae but have not specifically been investigated for this mite. The reader is referred to the entry on D. pteronyssinus d1.

Various studies have reported that the rate of sensitisation is higher among atopic children, and that high mite infestation increases the rate of sensitisation (70). The European Community Respiratory Health Survey, an international study of asthma prevalence and risk factors for asthma, collected information on IgE antibodies to common allergens in over 13,000 adults living in 37 centres in 16 countries, and found a median prevalence of 20.3% (range 6.7 - 35.1%) for sensitisation to D. pteronyssinus (78). In a follow-up study, home visits with 3580 participants from 22 study centres in the European Community Respiratory Health Survey II were conducted; mattress dust was sampled and analysed for Der p 1, Der f 1, and Der 2 allergens. Der 1 and Der 2 allergens were detectable (>/=0.1 mug/g) in 68% and 53% of the samples, respectively. Large differences in allergen levels among study centres were observed, and geographic patterns for Der p 1 and Der f 1 were different. Low winter temperatures reduced Der p 1 but not Der f 1 (79).

D. pteronyssinus and D. farinae appear to be significant allergens in most geographic regions but may vary within these regions. In a study in the homes of 111 asthmatic children in 3 climatic regions in Sweden, the major allergen Der m 1, together with Der p 1 from D. pteronyssinus and Der f 1 from D. farinae, was analysed. Der f 1 was the predominant House dust mite allergen, Der p 1 was the least often found, and Der m 1 represented 31% of the allergen load. However, in the Linkoping area Der m 1 was the major House dust mite allergen (58%). Of the children with IgE antibodies against House dust mite, 67% reacted to all 3 mites. Mite sensitisation rates were marginally increased (7%) by the addition of IgE analysis of D. microceras to the routine analysis of IgE antibodies against D. pteronyssinus and D. farinae. The authors concluded that Der m 1 may in this instance be an important House dust mite allergen and should be considered when House dust mite exposure data are assessed in areas with a climate like that of Sweden (80).

However, in another Scandinavian population, in Denmark, a study found that both immunochemically and microscopically, D. farinae was dominant, D. pteronyssinus less frequent but important, and D. microceras insignificant (81).

In a study assessing specific allergen content in dust samples from the homes of 106 allergy clinic patients in Baltimore in the USA, House dust mite allergens were detected in 99% of homes. D. farinae was found in 95%, D. pteronyssinus in 88% andD. microceras in 31%. Although sensitisation to these allergens was not evaluated, the study indicates that D. microceras may be an important allergen in this geographical region (82).

In tropical Singapore, a prospective evaluation was made of 175 newly diagnosed allergic rhinitis patients, of whom 39% reported a concomitant diagnosis and/ or clinical complaints of bronchial asthma, and 48% of atopic dermatitis; skin reactivity for D. pteronyssinus and D. farinae mix was detected in 85% of patients (and 62% for B. tropicalis) (83).

In studies of house dust in Bursa, Turkey, approximately 34% of houses were found to be infested with House dust mites. The rate of infestation was 18.75% and 50% in the houses with and without central heating systems, respectively. The prevalence of D. pteronyssinus was found to be 58.34%, compared with 16.67% for Glycophagus domesticus and 4.16% for D. farinae (84).

In an evaluation of house dust collected from dwellings at 7 locations in Upper Silesia, Poland, mites were found in 56.1% of the samples. D. farinae was predominant (75.3%), followed by D. pteronyssinus (18.6%) and Euroglyphus maynei (1.5%) (85).

A number of studies in South America have documented the significance of D. pteronyssinus sensitisation. In Valdivia, Chile, out of 100 consecutive paediatric asthma patients evaluated, 80 were confirmed to have skin reactivity to at least 1 mite species. All patients with skin reactivity for mites were positive to D. pteronyssinus, and 99% to D. farinae. All of the patients with severe persistent asthma had skin reactivity to mites, as did 85% in the moderate group, and 73% in the mild group. Ninety-five percent of patients with asthma and allergic rhinitis were shown to have skin reactivity to mites, as were 92% of patients with asthma and eczema and 100% of patients with asthma, allergic rhinitis and eczema (86). In a study of patients with allergic respiratory disease attending an allergy clinic in Brazil, out of 212 medical records evaluated, 61.7% showed sensitisation to Der p, 59.9% to Der f and 54.7% to Blomia tropicalis (87).

In a study of 579 asthmatic patients in Taiwan, it was shown through measuring allergen-specific IgE antibodies that almost 59% were sensitised to D. microceras, compared to 59.8% to D. pteronyssinus and 56.8% to D. farinae. Sensitisation to Cockroach was found in 38.3%, to Dog dander in 26.3%, to Candida albicans in 13.3%, to Cat dander in 10%, and to Cladosporium herbarum in 6.6%. The study indicates the importance of considering D. microceras when evaluating allergic individuals (88).

Among 93 Taiwanese asthmatic children aged 3 to 15 years evaluated for sensitisation to 5 species of mites, 63 were found to have IgE antibodies to at least 1 of the following mites: D. pteronyssinus, D. farinae, D. microceras, Euroglyphus maynei, and Blomia tropicalis. Sensitisation to D. pteronyssinus was found in 87%, to D. farinae in 85%, to D. microceras in 84%, to Euroglyphus maynei in 77%, and to Blomia tropicalis in 65% (89). Similarly, in a Taiwanese study of 498 atopic children aged 2 to 16 years, high prevalences of sensitisation were documented: 90.2% to D. pteronyssinus, 88.2% to D. farinae, 79.5% to D. microceras, and 76.7% to Blomia tropicalis (90).

A group of 25 atopic children under 11 years of age in Oxford in the UK was studied for skin reactivity and IgE antibodies to 4 species of House dust mites: D. pteronyssinus, D. farinae, D. microceras and Euroglyphus maynei. All of the children were sensitised to D. pteronyssinus, and 80% of these children were also sensitised to D. farinae and D. microceras. Importantly, dust samples from various sites in the homes of the children revealed D. pteronyssinus in all the homes, but no D. farinae or D. microceras. A control group of 20 atopic children of similar ages who were not sensitised to House dust mite allergens had similar exposure to the 4 mite species. These results suggest that factors in addition to mite exposure are important in the development of specific IgE responses to House dust mites (91).

Interestingly, in habitats were conditions are not favourable for mites, mites have still managed to survive and may cause sensitisation. The presence of D. farinae and D. pteronyssinus have been reported in Egypt (92).

A large body of studies from around the world has demonstrated the relevance of this allergen (93-94). The reader is referred to references listed in the first paragraph of this section for more detailed clinical information.

Other reactions

Systemic anaphylaxis can occur after the ingestion of heated or unheated mitecontaminated foods. This problem may be more prevalent in tropical and subtropical countries than previously recognised. The most common symptoms following the ingestion of mite-contaminated flour were breathlessness, angioedema, wheezing, and rhinorrhea, and these started between 10 and 240 minutes after eating (95).

Compiled by Dr Harris Steinman,


  1. Thomas WR, Smith WA, Hales BJ. The allergenic specificities of the house dust mite. Chang Gung Med J 2004;27(8):563-9
  2. Stewart GA, Kollinger MR, King CM, Thompson PJ. A comparative study of three serine proteases from Dermatophagoides pteronyssinus and D. farinae. Allergy 1994;49(7):553-60
  3. Aki T, Kodama T, Fujikawa A, Miura K, Shigeta S, Wada T, Jyo T, Murooka Y, Oka S, Ono K. Immunochemical characterization of recombinant and native tropomyosins as a new allergen from the house dust mite. J Allergy Clin Immunol 1995;96(1):74-83
  4. Tsai LC, Chao PL, Shen HD, Tang RB, Chang TC, Chang ZN, Hung MW, Lee BL, Chua KY. Isolation and characterization of a novel 98- kd Dermatophagoides farinae mite allergen. J Allergy Clin Immunol 1998;102(2):295-303
  5. Fujikawa A, Uchida K, Yanagidani A, Kawamoto S, Aki T, Shigeta S, Wada T, Suzuki O, Jyo T, Ono K. Altered antigenicity of M-177, a 177-kDa allergen from the house dust mite Dermatophagoides farinae, in stored extract. Clin Exp Allergy 1998;28(12):1549-58
  6. Epton MJ, Smith W, Hales BJ, Hazell L, Thompson PJ, Thomas WR. Non-allergenic antigen in allergic sensitization: responses to the mite ferritin heavy chain antigen by allergic and non-allergic subjects. Clin Exp Allergy 2002;32(9):1341-7
  7. Takai T, Kato T, Sakata Y, Yasueda H, Izuhara K, Okumura K, Ogawa H. Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine protease activity. Biochem Biophys Res Commun 2005;328(4):944-52
  8. Yasuhara T, Takai T, Yuuki T, Okudaira H, Okumura Y. Cloning and expression of cDNA encoding the complete prepro-form of an isoform of Der f 1, the major group 1 allergen from house dust mite Dermatophagoides farinae. Biosci Biotechnol Biochem 2001;65(3):563-9
  9. Yasuhara T, Takai T, Yuuki T, Okudaira H, Okumura Y. Biologically active recombinant forms of a major house dust mite group 1 allergen Der f 1 with full activities of both cysteine protease and IgE binding. Clin Exp Allergy 2001;31(1):116-24
  10. Best EA, Stedman KE, Bozic CM, Hunter SW, Vailes L, Chapman MD, McCall CA, McDermott MJ. A recombinant group 1 house dust mite allergen, rDer f 1, with biological activities similar to those of the native allergen. Protein Expr Purif 2000;20(3):462-71
  11. Le Mao J, Mayer CE, Peltre G, Desvaux FX, David B, Weyer A, Senechal H. Mapping of Dermatophagoides farinae mite allergens by two-dimensional immunoblotting. J Allergy Clin Immunol 1998;102(4 Pt 1):631-6
  12. Noguchi E, Shibasaki M, Nishiyama C, Okumura Y, Takita H. IgE responsiveness to Dermatophagoides farinae in young asthmatic children: IgE binding study using recombinant allergens of Der f1, Der f2 and mutant proteins of Der f2. Int Arch Allergy Immunol 1996;110(4):380-7
  13. 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
  14. Dilworth, R. J., K. Y. Chua, W. R. Thomas. Sequence analysis of cDNA coding for a major house dust allergn Der f I. Clin Exp Allergy 1991;21:25-32
  15. Takai T, Kato T, Yasueda H, Okumura K, Ogawa H. Analysis of the structure and allergenicity of recombinant pro- and mature Der p 1 and Der f 1: Major conformational IgE epitopes blocked by prodomains. J Allergy Clin Immunol 2005;115(3):555-63
  16. Yang QG, Li CP. Cloning, sequencing and subcloning of cDNA coding for group I allergen of Dermatophagoides farinae. [Chinese] Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi 2004;22(3):173-5
  17. Nishiyama, C., T. Yunki, T. Takai, Y. Okumura, and H. Okudaira. Determination of three disulfide bonds in a major house dust mite allergen, Der f II. Int Arch Allergy Immunol 1993;101:159-166
  18. Trudinger, M., K. Y. Chua, W. R. Thomas. cDNA encoding the major dust mite allergen Der f II. Clin Exp Allergy 1991;21:33-38
  19. Jin HS, Yong TS, Park JW, Hong CS, Oh SH. Immune reactivity of recombinant group 2 allergens of house dust mite, Dermatophagoides pteronyssinus, and Dermatophagoides farinae. J Investig Allergol Clin Immunol 2003;13(1):36-42
  20. Jeong KY, Lee IY, Ree HI, Hong CS, Yong TS. Localization of Der f 2 in the gut and fecal pellets of Dermatophagoides farinae. Allergy 2002;57(8):729-31
  21. Johannessen BR, Skov LK, Kastrup JS, Kristensen O, Bolwig C, Larsen JN, Spangfort M, Lund K, Gajhede M. Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE crossreactivity. FEBS Lett 2005;579(5):1208-12
  22. Suzuki M, Tanaka Y, Korematsu S, Mikami B, Minato N. Crystal structure and some properties of a major house dust mite allergen, Derf 2. Biochem Biophys Res Commun. 2006; 339(2):679-686
  23. Thomas WR, Smith WA, Hales BJ, Mills KL, O’Brien RM. Characterization and immunobiology of house dust mite allergens. Int Arch Allergy Immunol 2002;129(1):1-18
  24. Nishiyama C, Yasuhara T, Yuuki T, Okumura Y. Cloning and expression in Escherichia coli of cDNA encoding house dust mite allergen Der f 3, serine protease from Dermatophagoides farinae. FEBS Lett 1995;377(1):62-6
  25. Ando T, Homma R, Ino Y, Ito G, Miyahara A, Yamakawa H, Iwaki M, Okumura Y, Suko M, Haida M, et al. Is a trypsin-like protease of mites a Der f III allergen? Arerugi 1992;41(6):704-7
  26. Smith WA, Chua KY, Kuo MC, Rogers BL, Thomas WR. Cloning and sequencing of the Dermatophagoides pteronyssinus group III allergen, Der p III. Clin Exp Allergy 1994;24(3):220-8
  27. Smith WA, Thomas WR. Comparative analysis of the genes encoding group 3 allergens from Dermatophagoides pteronyssinus and Dermatophagoides farinae. Int Arch Allergy Immunol 1996;109:133-40
  28. Stewart GA, Bird CH, Krska KD, Colloff MJ, Thompson PJ. A comparative study of allergenic and potentially allergenic enzymes from Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei. Exp Appl Acarol 1992;16(1-2):165-80
  29. Kawamoto S, Mizuguchi Y, Morimoto K, Aki T, Shigeta S, Yasueda H, Wada T, Suzuki O, Jyo T, Ono K. Cloning and expression of Der f 6, a serine protease allergen from the house dust mite, Dermatophagoides farinae. Biochim Biophys Acta 1999;1454(2):201-7
  30. Yasueda H, Mita H, Akiyama K, Shida T, Ando T, Sugiyama S, Yamakawa H. Allergens from Dermatophagoides mites with chymotryptic activity. Clin Exp Allergy 1993;23(5):384-90
  31. Zhu YF, Liu ZG, Gao B. Cloning, expression, purification and identification of Der f6 gene and its immunological characteristics from the dust house mite, [Chinese] Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi 2006;24(4):241-6
  32. Shen HD, Lin WL, Tsai LC, Tam MF, Chua KY, Chen HL, Hsieh KH, et al. Characterization of the allergen Der f 7 from house dust mite extracts by species-specific and crossreactive monoclonal antibodies. Clin Exp Allergy 1997;27(7):824-32
  33. Shen HD, Chua KY, Lin WL, Hsieh KH, Thomas WR. Molecular cloning and immunological characterization of the house dust mite allergen Der f 7. Clin Exp Allergy 1995;25(10):1000-6
  34. Allergome 2005
  35. Tsai LC, Peng HJ, Lee CS, Chao PL, Tang RB, Tsai JJ, Shen HD, Hung MW, Han SH. Molecular cloning and characterization of full-length cDNAs encoding a novel highmolecular- weight Dermatophagoides pteronyssinus mite allergen, Der p 11. Allergy 2005;60(7):927-37
  36. Lee C, Tsai L, Chao P, Lin C, Hung M, Chien A, Chiang Y, Han S. Protein sequence analysis of a novel 103-kDa Dermatophagoides pteronyssinus mite allergen and prevalence of serum immunoglobulin E reactivity to rDer p 11 in allergic adult patients. Clin Exp Allergy 2004;34(3):354-362
  37. Tsai L, Sun Y, Chao P, Ng H, Hung M, Hsieh K, Liaw S, Chua K. Sequence analysis and expression of a cDNA clone encoding a 98- kDa allergen in Dermatophagoides farinae. Clin Exp Allergy 1999;29(12):1606-13
  38. Ramos JD, Nge C, Wah LB, Yan CK. cDNA Cloning and Expression of Blo t 11, the Blomia tropicalis Allergen Homologous to Paramyosin. Int Arch Allergy Immunol 2001;126(4):286-293
  39. Epton MJ, Dilworth RJ, Smith W, Hart BJ, Thomas WR. High-molecular-weight allergens of the house dust mite: an apolipophorin-like cDNA has sequence identity with the major M-177 allergen and the IgE-binding peptide fragments Mag1 and Mag3. Int Arch Allergy Immunol 1999;120(3):185-91
  40. Fujikawa A, Ishimaru N, Seto A, Yamada H, Aki T, Shigeta S, et al. Cloning and characterization of a new allergen, Mag 3, from the house dust mite, Dermatophagoides farinae: cross-reactivity with high-molecularweight allergen. Mol Immunol 1996;33(3):311-9
  41. McCall C, Hunter S, Stedman K, Weber E, Hillier A, Bozic C, Rivoire B, Olivry T. Characterization and cloning of a major high molecular weight house dust mite allergen (Der f 15) for dogs. Vet Immunol Immunopathol 2001;78(3-4):231-47
  42. O’neil SE, Heinrich TK, Hales BJ, Hazell LA, Holt DC, Fischer K, Thomas WR. The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus. Clin Exp Allergy 2006;36(6):831-839
  43. Tategaki A, Kawamoto S, Aki T, Jyo T, Suzuki O, Shigeta S, Ono K. Newly described house dust mite allergens. ACI International suppl 2000;1:74-76
  44. Kawamoto S, Suzuki T, Aki T, Katsutani T, Tsuboi S, Shigeta S, Ono K. Der f 16: a novel gelsolin-related molecule identified as an allergen from the house dust mite, Dermatophagoides farinae. FEBS Lett 2002;516(1-3):234-8
  45. Weber E, Hunter S, Stedman K, Dreitz S, Olivry T, Hillier A, McCall C. Identification, characterization, and cloning of a complementary DNA encoding a 60-kd house dust mite allergen (Der f 18) for human beings and dogs. J Allergy Clin Immunol 2003;112(1):79-86
  46. International Union of Immunological Societies Allergen Nomenclature: IUIS official list 2006
  47. Aki T, Fujikawa A, Wada T, Jyo T, Shigeta S, Murooka Y, Oka S, Ono K. Cloning and expression of cDNA coding for a new allergen from the house dust mite, Dermatophagoides farinae: homology with human heat shock cognate proteins in the heat shock protein 70 family. J Biochem (Tokyo) 1994;115(3):435-40
  48. Tsai LC, Chao PL, Hung MW, Sun YC, Kuo IC, Chua KY, Liaw SH, Chua KY, Kuo IC. Protein sequence analysis and mapping of IgE and IgG epitopes of an allergenic 98-kDa Dermatophagoides farinae paramyosin, Der f 11. Allergy 2000;55(2):141-7
  49. Chao PL, Peng HJ, Tang RB, Hung MW, Tsai LC. Serum specific IgE reactivity to recombinant Der f 11 in asthmatic children. J Asthma 2001;38(5):391-8
  50. Spieksma FT. Biological aspects of the house dust mite (Dermatophagoides pteronyssinus) in relation to house dust atopy. Clin Exp Immunol 1970;6(1):61-70
  51. Thomas WR, Smith W. House-dust-mite allergens. Allergy 1998;53(9):821-32.
  52. Sidenius KE, Hallas TE, Poulsen LK, Mosbech H. Allergen cross-reactivity between house-dust mites and other invertebrates. Allergy 2001;56(8):723-33
  53. Ferrandiz R, Casas R, Dreborg S. Crossreactivity between Dermatophagoides siboney and other domestic mites. II. Analysis of individual cross-reacting allergens after SDSPAGE and Western blotting inhibition. Int Arch Allergy Immunol 1998;116(3):206-14
  54. Cheong N, Soon SC, Ramos JD, Kuo IC, Kolortkar PR, Lee BW, Chua KY. Lack of human IgE cross-reactivity between mite allergens Blo t 1 and Der p 1. Allergy 2003;58(9):912-920
  55. Lee AJ, Machell J, Van Den Broek AH, Nisbet AJ, Miller HR, Isaac RE, Huntley JF. Identification of an antigen from the sheep scab mite, Psoroptes ovis, homologous with house dust mite group I allergens. Parasite Immunol 2002;24(8):413-22
  56. Santos AB, Chapman MD, Aalberse RC, Vailes LD, Ferriani VP, et al. Cockroach allergens and asthma in Brazil: identification of tropomyosin as a major allergen with potential cross-reactivity with mite and shrimp allergens. J Allergy Clin Immunol 1999;104(2 Pt 1):329-37
  57. 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
  58. Jeong KY, Hwang H, Lee J, Lee IY, Kim DS, Hong CS, Ree HI, Yong TS. Allergenic characterization of tropomyosin from the dusky brown cockroach, Periplaneta fuliginosa. Clin Diagn Lab Immunol 2004;11(4):680-5
  59. Pope AM, Patterson R, Burge H: Indoor allergens. Assessing and Controlling Adverse Health Effects. National Academy Press, Washington 1993
  60. Voorhorst R, Spieksma FTM, Varekamp H. House-dust atopy and the House-dust mite. Stafleu’s Scientific Publishing Co, Leiden 1969
  61. Wharton GW: House dust mites. J Med Entom 1976, 12, 577-621
  62. Arlian LG. House-dust-mite allergens. Exp Appl Acarol 1991;10(3-4):167-86
  63. Colloff MJ, Ayres J, Carswell F, Howarth PH, Merrett TG, Mitchell EB, Walshaw MJ, Warner JO, Warner JA, Woodcock AA. The control of allergens of dust mites and domestic pets: a position paper. Clin Exp Allergy. 1992;22 Suppl 2:1-28
  64. Platts-Mills TA, Thomas WR, Aalberse RC, Vervloet D, Champman MD. Dust mite allergens and asthma: report of a second international workshop. J Allergy Clin Immunol 1992;89(5):1046-60
  65. Sporik R, Holgate ST, Platts-Mills TA, Cogswell JJ. Exposure to house-dust mite allergen (Der p I) and the development of asthma in childhood. A prospective study. N Engl J Med 1990;323(8):502-7
  66. Hide DW, Matthews S, et al. Effect of allergen avoidance in infancy on allergic manifestations at age two years. J Allergy Clin Immunol 1994;93:842-6
  67. Chan-Yeung M, Manfreda J, Dimich-Ward H, Lam J, Ferguson A, Warren P, Simons E, Broder I, Chapman M, Platts-Mills T, et al. Mite and cat allergen levels in homes and severity of asthma. Am J Respir Crit Care Med 1995;152(6 Pt 1):1805-11
  68. Henderson FW, Henry MM, Ivins SS, Morris R, Neebe EC, Leu SY, Stewart PW. Correlates of recurrent wheezing in school-age children. The Physicians of Raleigh Pediatric Associates. Am J Respir Crit Care Med 1995;151(6):1786-93
  69. Custovic A, Taggart SC, Francis HC, Chapman MD, Woodcock A. Exposure to house dust mite allergens and the clinical activity of asthma. J Allergy Clin Immunol 1996;98(1):64-72
  70. The house-dust mite: its biology and role in allergy. Proceedings of an international scientific workshop. Oslo, Norway, 4-7 September 1997. Allergy 1998;53(48 Suppl):1-135
  71. Kuo IC, Yi FC, Cheong N, Shek LP, Chew FT, Lee BW, Chua KY. Sensitization to Blomia tropicalis and Dermatophagoides pteronyssinus – a comparative study between Singapore and Taiwan. Asian Pac J Allergy Immunol 1999;17(3):179-88
  72. Lynch NR, Puccio FA, Di Prisco MC, Lopez RI, Hazell LA, Smith WA, Thomas WR. Reactivity to recombinant house-dust-mite allergens in asthma and rhinitis in a tropical environment. Allergy 1998;53(8):808-11
  73. Platts-Mills TA, Rakes G, Heymann PW. The relevance of allergen exposure to the development of asthma in childhood. J Allergy Clin Immunol 2000;105(2 Pt 2):S503-8
  74. Van Der Veen MJ, Jansen HM, Aalberse RC, van der Zee JS. Der p 1 and Der p 2 induce less severe late asthmatic responses than native Dermatophagoides pteronyssinus extract after a similar early asthmatic response. Clin Exp Allergy 2001;31(5):705-14
  75. Kuljanac I. The role of Dermatophagoides pteronyssinus in atopic dermatitis. Acta Dermatovenerol Croat 2006;14(2):86-9
  76. Kramer U, Lemmen C, Bartusel E, Link E, Ring J, Behrendt H. Current eczema in children is related to Der f 1 exposure but not to Der p 1 exposure. Br J Dermatol. 2006; 154(1):99-105
  77. Katoh N, Hirano S, Suehiro M, Masuda K, Kishimoto S. The characteristics of patients with atopic dermatitis demonstrating a positive reaction in a scratch test after 48 hours against house dust mite antigen. J Dermatol 2004;31(9):720-6
  78. Burney P, Malmberg E, Chinn S, Jarvis D, Luczynska C, Lai E. The distribution of total and specific serum IgE in the European Community Respiratory Health Survey. J Allergy Clin Immunol 1997;99(3):314-22
  79. Zock JP, Heinrich J, Jarvis D, Verlato G, Norback D, Plana E, Sunyer J, Chinn S, et al. Distribution and determinants of house dust mite allergens in Europe: The European Community Respiratory Health Survey II. J Allergy Clin Immunol 2006;118(3):682-690
  80. Warner A, Boström S, Munir AKM, Möller C, Schou C, Kjellman N-IM. Environmental assessment of Dermatophagoides mite-allergen levels in Sweden should include Der m 1. Allergy 1998;53(7):698-70
  81. Sidenius KE, Hallas TE, Poulsen LK, Mosbech H. House dust mites and their allergens in Danish mattresses – results from a population based study. Ann Agric Environ Med 2002;9(1):33-9
  82. Wood RA, Eggleston PA, Lind P, Ingemann L, Schwartz B, Graveson S, Terry D, Wheeler B, Adkinson NF Jr. Antigenic analysis of household dust samples. Am Rev Respir Dis 1988;137(2):358-63
  83. Kidon MI, Chiang WC, Liew WK, Lim SH, See Y, Goh A, Tan JP, Chay OM, Balakrishnan A. Sensitization to dust mites in children with allergic rhinitis in Singapore: does it matter if you scratch while you sneeze? Clin Exp Allergy 2005 Apr;35(4):434-40
  84. Gulegen E, Girisgin O, Kutukoglu F, Girisgin AO, Coskun SZ. Mite species found in house dust in houses in Bursa. [Turkish] Turkiye Parazitol Derg 2005;29(3):185-187
  85. Solarz K, Senczuk L, Maniurka H, Cichecka E, Peszke M. Comparisons of the allergenic mite prevalence in dwellings and certain outdoor environments of the Upper Silesia (southwest Poland). Int J Hyg Environ Health 2007 Jan 10
  86. Calvo M, Fernandez-Caldas E, Arellano P, Marin F, Carnes J, Hormaechea A. Mite allergen exposure, sensitisation and clinical symptoms in Valdivia, Chile. J Investig Allergol Clin Immunol. 2005; 15(3):189-196
  87. Soares FA, Segundo GR, Alves R, Ynoue LH, Resende RO, Sopelete MC, Silva DA, Sung SS, Taketomi EA. Indoor allergen sensitization profile in allergic patients of the allergy clinic in the University Hospital in Uberlandia, Brazil. [Portuguese] Rev Assoc Med Bras 2007;53(1):25-8
  88. Chiang CH, Wu KM, Wu CP, Yan HC, Perng WC. Evaluation of risk factors for asthma in Taipei City. J Chin Med Assoc 2005;68(5):204-9
  89. Lai CL, Shyur SD, Wu CY, Chang CL, Chu SH. Specific IgE to 5 different major house dust mites among asthmatic children. Acta Paediatr Taiwan 2002;43(5):265-70
  90. Huang HW, Lue KH, Wong RH, Sun HL, Sheu JN, Lu KH. Distribution of allergens in children with different atopic disorders in central Taiwan. Acta Paediatr Taiwan 2006;47(3):127-34
  91. Young RP, Hart BJ, Faux JA, Hopkin JM. House dust mite sensitivity: a comparison of immune response with exposure to four species of Pyroglyphidae. Clin Exp Allergy 1990;20(3):319-25
  92. El-Shazly AM, El-Beshbishi SN, Azab MS, El- Nahas HA, Soliman ME, Fouad MA, Monib Mel. Present situation of house dust mites in Dakahlia Governorate, Egypt. J Egypt Soc Parasitol. 2006; 36(1):113-126
  93. Garcia-Gonzalez JJ, Vega-Chicote JM, Rico P, del Prado JM, et al. Prevalence of atopy in students from Malaga, Spain. Ann Allergy Asthma Immunol 1998;80(3):237-44
  94. Tsai JJ, Chen WC. Different age of asthmatic patients affected by different aeroallergens. [Chinese] J Microbiol Immunol Infect 1999;32(4):283-8
  95. Sanchez-Borges M, Capriles-Hulett A, Fernandez-Caldas E, et al. Mitecontaminated foods as a cause of anaphylaxis. J Allergy Clin Immunol 1997;99(6 Pt 1):738-43

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