Dermatophagoides pteronyssinus

 

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Code: d1
Latin name: Dermatophagoides pteronyssinus
Source material: Whole body culture
Family: Pyroglyphidae
Common names: House dust mite, Dust mite

Allergen Exposure

Geographical distribution

See common geographical background in our Scientific Document (link to the right).

The most important House dust mites are Dermatophagoides pteronyssinus and (in drier areas) D. farinae. In subtropical and tropical regions the Storage mite Blomia tropicalis is also a major source of allergens, co-existing with D. pteronyssinus. Recent evidence shows that even these very general boundaries are blurring, and in many instances all 3 mite species may be highly relevant, causing widespread sensitisation. But D. pteronyssinus is especially important because its distribution is for all practical purposes worldwide.

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. pteronyssinus, though it has a worldwide distribution, seems to be more abundant in Europe than in America. It prefers more humid climates than D. farinae does. The duration of the life cycle from egg to adult is 31 days and the female longevity is approximately 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.

Environment

See common environmental background tomites in our Scientific Document (link to the right).

Allergens

The most important allergenic proteins in D. pteronyssinus are Der p 1 and Der p 2. Extracts of D. pteronyssinus contain high concentrations of the Group 1 and 2 allergens, usually between 20 and 100 μg/ml (1). 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. About 20% of patients, however, do not have IgE antibody to the Group 1 and 2 allergens, and even though this is a minority, it constitutes a large population. In further allergen groups, 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 level the Group 1 and 2 allergens (2).

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. Der p 7 is present at under 1 μg/ml. Der p 3 is present at less than 1 μg/ml (3). Experiments measuring the trypsin enzymatic activity of Der p 3 demonstrated a 200-fold higher concentration in spent mite media (1). Der p 5, 10, 11 and 14 appear to be present in low quantities (2-6). There is evidence that Der p 3, 7 and 14 are unstable in the extracts (2). Nonetheless, allergens present in low amount in extracts can induce high titres of IgE antibodies. Also, non-allergenic polypeptides, such as the ferritin heavy chain, may be highly immunogenic, and can induce a balanced Th1/Th2 cytokine response (7).

A study concludes that Der p 1 levels in German mattress dust samples have been reduced by a factor of approximately 3 to 4 by the consecutive cold winters of 1995/ 1996 and 1996/1997 (8).

The following recombinant allergens have been characterised:

  • rDer p 1 (13,46).
  • rDer p 2 (47-48).
  • rDer p 4 (25).
  • rDer p 5 (29,47-50).
  • rDer p 7 (32,47-48,51-52).
  • rDer p 8 (47).
  • rDer p 10 (47,53).
  • rDer p 11 (37).

Der p 1 and Der p 2 are both products of single genes but are highly polymorphic and exist as a number of isoforms (2). Thirteen of the 20 sequences reported for Der p 1 have been unique (54). Although the major Group 1 mite allergens Der p 1 and Der f 1 were first isolated as cysteine proteases, some studies reported that natural Der p 1 exhibits mixed cysteine and serine protease activity (46). Der p 1 and Der p 2 have been shown to be potent inducers of nitric oxide release from alveolar macrophages (55). Both allergens are major allergens and result in sensitisation in approximately 80% or more of D. pteronyssinus-sensitised patients (2, 6,30). Some studies have, however, reported lower levels of sensitisation. In a Thai study, skin reactivity to Der p 1, Der p 2 and Der p 5 was positive in 35% and 30% of 40 atopic children, respectively, and in 26.7% and 28.9% of 45 atopic adults, respectively (11).

Through the use of the recombinant allergens rDer p 2, rDer p 5 and rDer p 7 in skin tests, immediate hypersensitivity was demonstrated in 70, 60 and 52% respectively of a group of mite-sensitive allergic patients who were strongly positive to whole mite extract. Comparable results were obtained for allergen-specific IgE tests (48).

Der p 3 is a major allergen, sensitising approximately 50% of D. pteronyssinussensitised patients, but usually at low titres (2,19).

IgE sensitisation to Der p 4 has been reported to occur frequently, but usually at low titres (28). Children may be less sensitised to this allergen: in a study, 25% of mite-allergic children and 46% of miteallergic adults harboured serum-specific IgE to the mite amylase Der p 4 (26).

Recombinant Der p 4 appears to have comparable activity to that of the native form, binding specific IgE in 3 of 10 House dust mite-allergic patients tested (25). Der p 5 induces IgE antibodies in about 50% of subjects, but usually at low titres (19). Other studies have reported variability of sensitisation depending on the study group. Skin tests with rDer p 5 indicated sensitisation in about 60% of patients with asthma and 29% of those with allergic rhinitis alone (29). In a Thai study, sensitisation to Der p 5 was reported to range from 2.5% of atopic children to 11.1% of atopic adults (11). With recombinant rDer p5, sera of 21 of 38 miteallergic subjects were shown to be sensitised to this allergen; these results strongly correlated with observed IgE-binding to the native allergen (50).

Der p 6 has been reported to be 37% identical to the trypsin allergen Der p 3 (23). Der p 6 induces IgE antibodies in 40-50% of subjects but usually at low titres (19,30). Der p 9 manifested homology with the mite tryptic allergen Der p 3 and the chymotryptic allergen Der p 6. Allergenspecific IgE analyses showed that the frequencies of reactivity to Der p 9, Der p 1, Der p 2, Der p 3, and Der p 6 were 92%, 97%, 100%, 97%, and 65%, respectively (n = 35) (9).

The Group 7 mite allergen Der p 7 results in IgE sensitisation in 50% of allergic patients but usually at low titres (19,31). Sensitisation may occur at a lower prevalence in children (52). rDer p 7 reacted with about 50% of sera from mite-allergic patients (51). Although Der p 7 reacts with only 50% of allergic sera, it has been reported to often have a high level of IgE binding activity and may be more important than the major Der p 2 allergen in a high percentage of subjects. A competitive binding assay showed that rDer p 7 inhibited 91% of IgE binding to natural Der p 7 in sera from 2 patients and 73% in a further 2. The IgE binding of rDer p 2 and Der p 7 from 41 sera was then compared. Of the sera, 88% and 46% respectively showed positive binding. All of the 19 sera which bound Der p 7 also bound Der p 2, but 11 (58%) had bound IgE to Der p 7 at a high level or at least a higher one than that of the binding to Der p 2 (32). Further, the proliferative and cytokine response to the Group 1 and Group 7 allergens for D. pteronyssinus and D. farinae indicates that there is a high degree of T-cell crossreactivity between the whole purified allergens from each species (12). The allergen Der p 8 is reported to induce IgE in about 40 to 50% of subjects, usually at low titres (19). Recent work has found less IgE binding to Der p 8 than the original estimate (47,34). However, in a study of sera from Taiwanese asthmatics, IgE reactivity of 96% and 84% was demonstrated to native Der p 8 and recombinant Der p 8, respectively. Native Der p 8 showed 75% and 65% IgE reactivity with sera from similar subjects from Malaysia and Singapore, respectively. Although a high frequency of sensitisation to mite GST among allergic subjects was observed, the titres of IgE reactivity were low (35). Der p 9 manifested homology with the mite tryptic allergen Der p 3, and with the chymotryptic allergen Der p 6. IgE antibody analyses showed that the frequencies of reactivity to Der p 9, Der p 1, Der p 2, Der p 3, and Der p 6 were 92%, 97%, 100%, 97%, and 65%, respectively (n = 35). A study reported that Der p 9 is a serine protease different to the trypsin and chymotrypsin Group 3 and 6 allergens. It was shown to have very high IgE binding activity, but the same study also showed unusually high titres against the Group 3 allergens (9).

The Group 10 tropomyosin allergens are conserved by evolution and cross-react among organisms such as shellfish and parasites (56). The frequency of sensitisation to the tropomyosin allergen Der p 10 has varied from extremely high, in Japan (80%) and Zimbabwe (55%) (4), to low, in Europe (57). Paramyosin is a structural muscle protein of invertebrates (19). The Group 11 allergen Der p 11, a paramyosin allergen, binds IgE in 80% of allergic subjects (5), and the 98 and 60 kDa chitinase enzymes Der f 15 and 18 bind IgE from about 70% and 54% of allergic subjects (58-59). The recombinant allergen rDer p 11 showed positive IgE binding in 78% of mite-sensitised patients (37). A study reported that the prevalence of serum IgE reactivity to rDer p 11 on immunodot assays ranged from 41.7% to 66.7% in different allergic patient groups, whereas it was rare in non-atopic patients with urticaria (18.8%) and in normal individuals (8%) (38).

Group 14 mite allergens have sequence homology to a vitellogenin- or apo-lipophorinlike protein. These molecules are for lipid transport or lipid storage, which may explain their instability in aqueous extracts (19). Der p 14 binds IgE in 80% of subjects allergic to D. farinae (6,60) and D. pteronyssinus (2). The allergen degrades in extracts or is processed into smaller peptides (6).

The House dust mites D. pteronyssinus and D. farinae cause allergic disease in dogs as well as in humans. In geographical regions where the 2 mite species coexist, they both elicit IgE antibody 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 Group 1 and 2 allergens, as found for humans. 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. They are therefore potentially important allergens for humans as well as dogs (43).

Group 15 mite allergens are homologous to insect chitinases. In D. farinae, they have been shown to be located in the gut, suggesting they have a function in digestion rather than in moulting. The Group 15 allergens are therefore very significant because they are the major allergens recognised by dogs and cats, and because they are highly glycosylated, consisting of almost 50% carbohydrate (19).

Potential cross-reactivity

Allergens from mites have both common and species-specific determinants. In this case, allergenic determinants are shared with other mites belonging to the Pyroglyphidae family and are highly cross-reactive with other Dermatophagoides species (61-62). There seems to be a limited cross-reactivity with Storage (nonpyroglyphid) mites (62). Allergen cross-reactivity has been reported between House dust mites and other invertebrates (20).

In a study that investigated the individual allergens responsible for the cross-reactivity between D. siboney and other mite allergens, 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%). 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 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 for D. siboney (63).

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 (64). 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 (65-66). Recently, the Shrimp allergen rPen a 1 was shown to extensively and specifically compete for IgE binding to extracts of other crustacean species, House dust mite and German cockroach (67).

In general, as a number of specific allergens in D. pteronyssinus are homologous with other allergens, varying degrees of cross-reactivity can be expected. For example, a high homology of between 48 and 54% occurs between Blo t 3 and the Group 3 allergens from House dust mites, and this results in cross-reactivity between Blomia tropicalis and D. pteronyssinus (68). Der p 4 and Eur m 4 were calculated to be 90% identical, and were also calculated to be approximately 50% identical to insect and mammalian alpha-amylases (25).

A degree of cross-reactivity has been demonstrated between rBlo t 5 and rDer p 5 (49). Nonetheless, Group 5 allergens of D. pteronyssinus and B. tropicalis are speciesspecific (69). Through the use of a large panel of asthmatic sera and a combination of in vitro and in vivo assays, Blo t 5, the major allergen of B tropicalis, was shown to exhibit low levels of cross-reactivity with homologous Der p 5. These findings suggested that highly specific clinical reagents are necessary for precise diagnosis and immunotherapeutic treatment of sensitisation to Group 5 mite allergens (70). D. pteronyssinus glutathione Stransferase (Der p 8) has been shown to be cross-reactive with the homologous GST allergen from Sarcoptes scabiei (Scabies), an allergen which may play a role in the pathophysiology associated with crusted scabies (71). Cross-reactivity has also been demonstrated between mite GST and Cockroach GST, suggesting that GST is a panallergen (35).

Der p 9 has a degree of homology with Der p 3 (trypsin) and Der p 6 (chymotrypsin). IgE antibody inhibition studies demonstrated some cross-reactivity between this allergen and Der p 3 but not Der p 6 (9).

Some mite allergenic proteins such as tropomyosin (Der p 10) are widely crossreactive among invertebrates such as Shrimp, Snails, Cockroaches and chironomids (62,72-73). Mite tropomyosin has a high homology with tropomyosin from these other sources. P. americana (American cockroach) tropomyosin showed 80%, 81%, and 82% sequence identity to tropomyosins from D. pteronyssinus, D. farinae, and Shrimp, respectively, which are important allergens in their own right (74). rBlo t 10 has been reported to have a 96% amino acid identity to tropomyosin of other mites. Although Blo t 10 and Der p 10 are highly conserved and significantly crossreactive, unique IgE epitopes do exist (75).

Tropomyosin from Dermanyssus gallinae, a protein with 89% and 88% identity to tropomyosins from the ticks Boophilus microplus and Haemaphysalis longicornis, respectively, has been shown to have an 85% identity to the House dust mite tropomyosin Der p 10 (76).

Recombinant tropomyosin from the Sheep scab mite Psoroptes ovis appears to have a 98% and 97% identity to the House dust mite allergens Der f 10 and Der p 10 respectively. Similarly, the recombinant paramyosin had a predicted 97%, 95% and 89% identity to the paramyosins of D. pteronyssinus (Der p 11), Sarcoptes scabiei and Blomia tropicalis (Blo t 11) respectively (77).

One third of the children allergic to House dust mite were sensitised to Snails without any previous ingestion of Snails: this observation suggests that House dust mite was the sensitising agent and that the crossreaction could be clinically relevant in countries where eating Snails is common (78). Cross-reactivity has also been reported between IgE-binding proteins from Anisakis simplex and D. pteronyssinus (79). In 5 patients with asthma and allergic rhinoconjunctivitis to mites, and with IgEmediated allergy to barnacle, the allergens isolated from this crustacean were shown to be cross-reactive with D. pteronyssinus in 2 patients(80).

There is a high prevalence of sensitisation to C. arcuatus in northern Spain. Minimal cross-reactivity between C. arcuatus and D. pteronyssinus was reported (81).

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 (61,82-84). A large body of evidence suggests that exposure to the House dust mite allergens D. pteronyssinus and D. farinae is an important risk factor for allergic sensitisation, asthma development, and asthma symptom exacerbation (82,85-94)- Studies of House dust-allergic individuals around the world have shown that House dust mites cause symptoms such as perennialtype asthma, rhinitis and conjunctivitis, often with nocturnal or early morning episodes (95- 98). 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 hyperreactivity (99). In a Croatian study, asthmatic children with greater asthma severity were reported to have a higher serum concentration of both total IgE (>288.0 kU/L) and allergenspecific IgE to D. pteronyssinus (>44.1 kUA/L), respectively (100).

D. pteronyssinus has also been reported to play an important role as a trigger factor in patients with atopic dermatitis, including adult patients (101). Patients in whom the House dust mite-induced 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 domestic House dust mite (102). D. pteronyssinus may also result in allergic conjunctivitis but appear to have seasonal expression: in a Japanese study evaluating the relationship between IgE antibodies in the serum and allergic conjunctivitis in autumn, found that IgE antibody levels caused by house dust, D. pteronyssinus, and Orchard grass were higher in the autumn group than in the spring group (103).

House dust mite is also reported to have a prenatal influence on atopic expression. In a Korean study, House dust mite-positive asthmatics were more likely to have been born in August and September, times of high House dust mite exposure. This birth month pattern was evident in asthmatics who were sensitive only to House dust mites, but was not observed in those sensitive to House dust mites and other allergen(s) (104). The level of prenatal exposure to Der p 1 was also reported to influence the immune profile of cord blood T lymphocytes and the clinical outcome in early life, with the result that exposure to House dust mites during pregnancy tended to be higher in mothers of children with atopic dermatitis during the first year of life, when compared with those without atopic dermatitis (p = 0.08) (105). Various studies have reported that the rate of sensitisation is higher among atopic children, and that high mite infestation increases the rate of sensitisation (95). 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 (106). In a follow-up study, home visits with 3580 participants in the European Community Respiratory Health Survey II, involving 22 study centres, were conducted; mattress dust was sampled and analysed for Der p 1, Der f 1, and Der 2 allergen. Der 1 and Der 2 allergens were detectable (> 0.1 μg/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 (107).

D. pteronyssinus and D. farinae appear in studies 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 also 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 (108). 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 (109).

In a study assessing the specific allergen content in dust samples from the homes of 106 allergy clinic patients in Baltimore in the USA, Dust mite allergen was detected in 99% of homes. D. farinae was found in 95%, D. pteronyssinus in 88% and D. 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 (110).

In tropical Singapore, a prospective evaluation 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-specific IgE for D. pteronyssinus and D. farinae mix was detected in 85% (and 62% for B. tropicalis) (111). In Huelva, Spain, in the 136 dust samples studied, D. pteronyssinus was the most frequently identified mite species (94.8%). Tyrophagus putrescentiae was found in third position (41.1%), after Glycyphagus domesticus (54.4%) (112-113). 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 (114). Similar results emanated from another study in the same area, which reported a very high rate of D. pteronyssinus being found in August (115).

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%) (116). A number of studies in South America have documented the significance of D. pteronyssinus sensitisation. In Valdivia, Chile, 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 IgE 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 (117). In a study of patients with allergic respiratory disease who attended 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 (118).

D. pteronyssinus, D. siboney and Blomia tropicalis are the most important allergenic mites in Cuba. A total of 88.4% of patients were found to be positive to D. siboney, 87.1% to D. pteronyssinus, and 68.1% to B. tropicalis. Sensitisation to Dermatophagoides species was pre-dominant, demonstrated by the fact that 31.9% of patients had skin reactivity to either D. siboney or D. pteronyssinus only, whereas only 5.6% were sensitised solely to B. tropicalis. Most patients (58.6%) were polysensitised to the 3 species (119).

In a study of 579 asthmatic patients in Taiwan, it was shown through measuring 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 (120). In 93 Taiwanese asthmatic children aged from 3 to 15 years who were evaluated for sensitisation to 5 different 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% (121). 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 (122). In Xuzhou, China, 15.3% of a population of 222 students were shown to be sensitised to mites; and of 515 young patients with allergic symptoms, 82.3% were shown to be sensitised to mites. The prevalence of sensitisation declined with the age group evaluated (123).

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 allergen-specific IgE responses to House dust mites (124). Interestingly, in habitats where 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 (125). In Reykjavik, Iceland, studies have reported that 6 to 9% of young adults are sensitised to D. pteronyssinus; however, only negligible amounts of House dust mite and House dust mite allergens were detected in their homes. These patients are often men who spent time on farms in childhood and now have a high prevalence of IgE antibodies cross-reactive to D. pteronyssinus (126). Although most studies have focussed on immediate-type hypersensitivity, House dust mite may play a role in delayed reactions. Patch testing (APT) may help in evaluating these patients. It has been reported that APT with House dust mite assists in identifying mite-sensitive children with respiratory allergy. Positive APT results may imply that delayed hypersensitivity reactions affect children with asthma and rhinitis who are allergic to House dust mite (127).

A large body of studies from around the world has demonstrated the relevance of this allergen (128-129). 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 rhinorrhoea, and these started between 10 and 240 minutes after eating (130).

Compiled by Dr Harris Steinman, harris@zingsolutions.com

References

  1. 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
  2. Thomas WR, Smith WA, Hales BJ. The allergenic specificities of the house dust mite. Chang Gung Med J 2004;27(8):563-9.
  3. Li CS, Hsu CW, Chua KY, Hsieh KH, Lin RH. Environmental distribution of house dust mite allergen (Der p 5). J Allergy Clin Immunol 1996;97(3):857-9
  4. 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
  5. 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
  6. 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
  7. 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
  8. Gehring U, Brunekreef B, Fahlbusch B, Wichmann HE, Heinrich J; the INGA study group. Are house dust mite allergen levels influenced by cold winter weather? Allergy 2005;60(8):1079-82
  9. King C, Simpson RJ, Moritz RL, Reed GE, Thompson PJ, Stewart GA. The isolation and characterization of a novel collagenolytic serine protease allergen (Der p 9) from the dust mite Dermatophagoides pteronyssinus. J Allergy Clin Immunol 1996;98:739-47
  10. Li CS, Hsu CW, Lin RH. House dust mite allergens (Der p I and Der p V) within domestic environments of atopic and control children. Arch Environ Health 1997;52(3):208-12
  11. Trakultivakorn M, Nuglor T. Sensitization to Dermatophagoides pteronyssinus and Blomia tropicalis extracts and recombinant mite allergens in atopic Thai patients. Asian Pac J Allergy Immunol 2002;20(4):217-21
  12. Hales BJ, Shen HD, Thomas WR. Crossreactivity of T-cell responses to Dermatophagoides pteronyssinus and D. farinae. Studies with group 1 and 7 allergens. Clin Exp Allergy 2000;30(7):927-33
  13. 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
  14. Meno K, Thorsted PB, Ipsen H, Kristensen O, Larsen JN, Spangfort MD, Gajhede M, Lund K. The crystal structure of recombinant proDer p 1, a major house dust mite proteolytic allergen. J Immunol 2005;175(6):3835-45
  15. de HS, Stura E, VanderElst L, Carlier V, Jacquemin M, Saint-Remy JM. Threedimensional structure and IgE-binding properties of mature fully active Der p 1, a clinically relevant major allergen. J Allergy Clin Immunol 2006;117(3):571-576
  16. Sun BQ, Wu A, Chan A, Chik S, Wong D, Zhong NS. House dust mite allergen (Der p 1 and Blo t 5) levels in asthmatics’ home in Hongkong. Chin Med Sci J 2004;19(3):185-8
  17. Fernandez-Caldas E, Puerta L, Caraballo L, Lockey RF. Mite allergens. Clin Allergy Immunol 2004;18:251-70
  18. Ford SA, Tovey ER, Baldo BA. The spectrum of low molecular weight house dust mite (Dermatophagoides pteronyssinus) allergens with emphasis on Der p II. Clin Exp Allergy 1990;20(1):27-31
  19. 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
  20. Sidenius KE, Hallas TE, Poulsen LK, Mosbech H. Allergen cross-reactivity between house-dust mites and other invertebrates. Allergy 2001;56(8):723-33
  21. Thomas WR, Smith W. Towards defining the full spectrum of important house dust mite allergens. Clin Exp Allergy 1999;29(12):1583-7
  22. 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
  23. Bennett BJ, Thomas WR. Cloning and sequencing of the group 6 allergen of Dermatophagoides pteronyssinus. Clin Exp Allergy 1996;26(10):1150-4
  24. Stewart GA, Thompson PJ, Simpson RJ. Protease antigens from house dust mite. Lancet 1989;2(8655):154-5
  25. Mills KL, Hart BJ, Lynch NR, Thomas WR, Smith W. Molecular characterization of the group 4 house dust mite allergen from Dermatophagoides pteronyssinus and its amylase homologue from Euroglyphus maynei. Int Arch Allergy Immunol 1999;120(2):100-7
  26. Lake FR, Ward LD, Simpson RJ, Thompson PJ, Stewart GA. House dust mite-derived amylase: allergenicity and physicochemical characterization. J Allergy Clin Immunol 1991;87(6):1035-42
  27. Platts-Mills TA, Vervloet D, Thomas WR, Aalberse RC, Chapman MD. Indoor allergens and asthma: report of the Third International Workshop. J Allergy Clin Immunol 1997;100(6 Pt 1):S2-24
  28. Mills KL, Thomas WR, Smith W. Characterization of the group 4 allergens of the house dust mite. J Allergy Clin Immunol 2002;109:S180
  29. Lin KL, Hsieh KH, Thomas WR, Chiang BL, Chua KY. Characterization of Der p V allergen, cDNA analysis, and IgE-mediated reactivity to the recombinant protein. J Allergy Clin Immunol 1994;94(6 Pt 1):989-96
  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. 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
  32. Shen HD, Chua KY, Lin WL, Chen HL, Hsieh KH, Thomas WR. IgE and monoclonal antibody binding by the mite allergen Der p 7. Clin Exp Allergy 1996;26(3):308-15
  33. O’Neill GM, Donovan GR, Baldo BA Cloning and characterization of a major allergen of the house dust mite, Dermatophagoides pteronyssinus, homologous with glutathione S-transferase. Biochim Biophys Acta 1994;1219(2):521-8
  34. O’Neill GM, Donovan GR, Baldo BA Glutathione S-transferase a major allergen of the house dust mite, Dermatophagoides pteronyssinus. Immunol Lett 1995;48(2):103-7
  35. Huang CH, Liew LM, Mah KW, Kuo IC, Lee BW, Chua KY. Characterization of glutathione S-transferase from dust mite, Der p 8 and its immunoglobulin E cross-reactivity with cockroach glutathione S-transferase. Clin Exp Allergy 2006;36(3):369-376
  36. Huntley JF, Machell J, Nisbet AJ, Van den Broek A, Chua KY, Cheong N, Hales BJ, Thomas WR. Identification of tropomyosin, paramyosin and apolipophorin/vitellogenin as three major allergens of the sheep scab mite, Psoroptes ovis. Parasite Immunol 2004;26(8-9):335-42
  37. 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
  38. 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
  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. Epton MJ, Dilworth RJ, Smith W, Thomas WR. Sensitisation to the lipid-binding apolipophorin allergen Der p 14 and the peptide Mag-1. Int Arch Allergy Immunol 2001;124(1-3):57-60
  41. O’Neil SE, Heinrich TK, Thomas WR. Der p 15 0102-An isoform of the gene for Der p15 encoding a chitinase allergen from Dermatophagoides pteronyssinus www.ncbi.nlm.nih.gov/entrez/ viewer.fcgi?db=protein&val=67975089 2006;30 May
  42. O’Neil SE, Heinrich TK, Thomas WR. Der p 15-A chitinase allergen from Dermatophagoides pteronyssinus. www.ncbi.nlm.nih.gov/entrez/ viewer.fcgi?db=protein&val=67975087 2005;25 June
  43. 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
  44. O’Neil SE, Heinrich TK, Thomas WR. Der p 18-A chitinase allergen from Dermatophagoides pteronyssinus www.ncbi.nlm.nih.gov/entrez/ viewer.fcgi?db=protein&val=67975085 2006;30 May
  45. Allergome http://www.allergome.org 2007
  46. 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
  47. Pittner G, Vrtala S, Thomas WR, Weghofer M, Kundi M, Horak F, Kraft D, Valenta R. Component-resolved diagnosis of house-dust mite allergy with purified natural and recombinant mite allergens. Clin Exp Allergy 2004;34(4):597-603
  48. Lynch NR, Thomas WR, Garcia NM, Di Prisco MC, Puccio FA, L’opez RI, et al. Biological activity of recombinant Der p 2, Der p 5 and Der p 7 allergens of the housedust mite Dermatophagoides pteronyssinus. Int Arch Allergy Immunol 1997;114(1):59-67
  49. Caraballo L, Mercado D, Jimenez S, Moreno L, Puerta L, Chua KY. Analysis of the crossreactivity between BtM and Der p 5, two group 5 recombinant allergens from Blomia tropicalis and Dermatophagoides pteronyssinus. Int Arch Allergy Immunol 1998;117(1):38-45
  50. Tovey, E. R., M. C. Johnson, A. L. Roche, G. S. Cobon, B. A. Baldo. Cloning and sequencing of a cDNA expressing a recombinant house dust mite protein that binds human IgE and corresponds to an important low molecular weight allergen. J Exp Med 1989;170:1457-1462
  51. Shen HD, Chua KY, Lin WL, Hsieh KH, Thomas WR. Characterization of the house dust mite allergen Der p 7 by monoclonal antibodies. Clin Exp Allergy 1995;25(5):416-22
  52. Shen, H.-D., K.-Y. Chua, K.-.L. Lin, K.-H. Hsieh, and W.R. Thomas. Molecular cloning of a house dust mite allergen with common antibody binding specificities with multiple components in mite extracts. Clin Exp Allergy 1993;23:934-40
  53. Asturias JA, Arilla MC, Gomez-Bayon N, Martinez A, Martinez J, Palacios R. Sequencing and high level expression in Escherichia coli of the tropomyosin allergen (Der p 10) from Dermatophagoides pteronyssinus. Biochim Biophys Acta 1998;1397(1):27-30
  54. Smith WA, Hales BJ, Jarnicki AG, Thomas WR. Allergens of wild house dust mites: Environmental Der p 1 and Der p 2 sequence polymorphisms. J Allergy Clin Immunol 2001;107(6):985-92
  55. Peake HL, Currie AJ, Stewart GA, McWilliam AS. Nitric oxide production by alveolar macrophages in response to house dust mite fecal pellets and the mite allergens, Der p 1 and Der p 2. J Allergy Clin Immunol 2003;112(3):531-7
  56. Reese G, Ayuso R, Lehrer SB. Tropomyosin: an invertebrate pan-allergen. Int Arch Allergy Immunol 1999;119(4):247-58
  57. Westritschnig K, Sibanda E, Thomas W, Auer H, Aspock H, Pittner G, Vrtala S, Spitzauer S, Kraft D, Valenta R. Analysis of the sensitization profile towards allergens in central Africa. Clin Exp Allergy 2003;33(1):22-7
  58. 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
  59. 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
  60. 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
  61. 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
  62. Thomas WR, Smith W. House-dust-mite allergens. Allergy 1998;53(9):821-32
  63. 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
  64. 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
  65. 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
  66. Nisbet AJ, MacKellar A, McLean K, Brennan GP, Huntley JF. Eukaryotic expression of recombinant Pso o 1, an allergen from Psoroptes ovis, and its localization in the mite. Parasitology 2007;134(Pt 1):83-9
  67. DeWitt AM, Mattsson L, Lauer I, Reese G, Lidholm J. Recombinant tropomyosin from Penaeus aztecus (rPen a 1) for measurement of specific immunoglobulin E antibodies relevant in food allergy to crustaceans and other invertebrates. Mol Nutr Food Res 2004;48(5):370-9
  68. Flores I, Mora C, Rivera E, Donnelly R, Montealegre F. Cloning and molecular characterization of a cDNA from Blomia tropicalis homologous to dust mite group 3 allergens (trypsin-like proteases). Int Arch Allergy Immunol 2003;130(1):12-6
  69. Simpson A, Green R, Custovic A, Woodcock A, Arruda LK, Chapman MD. Skin test reactivity to natural and recombinant Blomia and Dermatophagoides spp. allergens among mite allergic patients in the UK. Allergy 2003;58(1):53-6
  70. Kuo IC, Cheong N, Trakultivakorn M, Lee BW, Chua KY. An extensive study of human IgE cross-reactivity of Blo t 5 and Der p 5. J Allergy Clin Immunol 2003;111(3):603-9
  71. Dougall A, Holt DC, Fischer K, Currie BJ, Kemp DJ, Walton SF. Identification and characterization of Sarcoptes scabiei and Dermatophagoides pteronyssinus glutathione S-transferases: implication as a potential major allergen in crusted scabies. Am J Trop Med Hyg 2005;73(5):977-84
  72. 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
  73. van Ree R, Antonicelli L, et al. Possible induction of food allergy during mite immunotherapy. Allergy 1996;51(2):108-13
  74. 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
  75. Yi FC, Cheong N, Shek PC, Wang DY, Chua KY, Lee BW. Identification of shared and unique immunoglobulin E epitopes of the highly conserved tropomyosins in Blomia tropicalis and Dermatophagoides pteronyssinus. Clin Exp Allergy 2002;32(8):1203-10
  76. Nisbet AJ, Huntley JF, Mackellar A, Sparks N, McDevitt R. A house dust mite allergen homologue from poultry red mite Dermanyssus gallinae (De Geer). Parasite Immunol 2006;28(8):401-5
  77. Nisbet AJ, MacKellar A, Wright HW, Brennan GP, Chua KY, Cheong N, Thomas JE, Huntley JF. Molecular characterization, expression and localization of tropomyosin and paramyosin immunodominant allergens from sheep scab mites (Psoroptes ovis). Parasitology 2006;133(Pt 4):515-23
  78. Vuitton DA, Ranc e F, Paquin ML, Adessi B, et al. Cross-reactivity between terrestrial snails (Helix species) and house-dust mite (Dermatophagoides pteronyssinus). I. In vivo study. Allergy 1998;53(2):144-50
  79. Bernardini R, Mistrello G, Novembre E, Roncarolo D, Zanotta S, Lombardi E, Cianferoni A, Pucci N, De Martino M, Vierucci A. Cross-reactivity between IgEbinding proteins from Anisakis simplex and Dermatophagoides pteronyssinus. Int J Immunopathol Pharmacol 2005;18(4):671-5
  80. Marinho S, Morais-Almeida M, Gaspar A, Santa-Marta C, Pires G, Postigo I, Guisantes J, Martinez J, Rosado-Pinto J. Barnacle allergy: allergen characterization and cross-reactivity with mites. J Investig Allergol Clin Immunol 2006;16(2):117-22
  81. Boquete M, Carballas C, Carballada F, Iraola V, Carnes J, Fernandez-Caldas E. In vivo and in vitro allergenicity of the domestic mite Chortoglyphus arcuatus. Ann Allergy Asthma Immunol 2006;97(2):203-208
  82. Pope AM, Patterson R, Burge H: Indoor allergens. Assessing and Controlling Adverse Health Effects. National Academy Press, Washington 1993
  83. Voorhorst R, Spieksma FTM, Varekamp H. House-dust atopy and the House-dust mite. Stafleu’s Scientific Publishing Co, Leiden 1969
  84. Wharton GW: House dust mites. J Med Entom 1976, 12, 577-621
  85. Arlian LG. House-dust-mite allergens. Exp Appl Acarol 1991;10(3-4):167-86
  86. 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
  87. 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
  88. 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
  89. 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
  90. 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
  91. 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
  92. 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
  93. Zlobina ZhM, Pron’kina OV, Khlgatian SV, Berzhets AI, Berzhets VM. Mites allergy in children from Tula region. [Russian] Zh Mikrobiol Epidemiol Immunobiol 2006;(7):85-8
  94. Valdivieso R, Iraola V, Estupinan M, Fernandez-Caldas E. Sensitization and exposure to house dust and storage mites in high-altitude areas of Ecuador. Ann Allergy Asthma Immunol 2006;97(4):532-538
  95. 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
  96. 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
  97. 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
  98. 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
  99. 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.
  100. Clin Exp Allergy 2001;31(5):705-14 100. Kovac K, Dodig S, Tjesic-Drinkovic D, Raos M. Correlation between asthma severity and serum IgE in asthmatic children sensitized to Dermatophagoides pteronyssinus. Arch Med Res 2007;38(1):99-105
  101. Kuljanac I. The role of Dermatophagoides pteronyssinus in atopic dermatitis. Acta Dermatovenerol Croat 2006;14(2):86-9
  102. 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
  103. Mimura T, Yamagami S, Amano S, Funatsu H, Arimoto A, Usui T, Ono K, Araie M, Okamoto S. Allergens in Japanese patients with allergic conjunctivitis in autumn. Eye 2005;19(9):995-9
  104. Yoo Y, Yu J, Kang H, Kim DK, Koh YY, Kim CK. Birth month and sensitization to house dust mites in asthmatic children. Allergy 2005; 60(10):1327-1330
  105. Hagendorens MM, Ebo DG, Bridts CH, Van de Water L, De Clerck LS, Stevens WJ. Prenatal exposure to house dust mite allergen (Der p 1), cord blood T cell phenotype and cytokine production and atopic dermatitis during the first year of life. Pediatr Allergy Immunol 2004;15(4):308-15
  106. 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
  107. 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
  108. 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
  109. 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
  110. 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
  111. 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;35(4):434-40
  112. Arias J, Lombardero M, Arteaga C, Barber D. Exposition and sensitization to Tyrophagus putrescentiae in a allergic population to Dermatophagoides pteronyssinus in Huelva, Spain. [Spanish] Allergol Immunopathol (Madr ) 2005;33(4):4-220
  113. Arias-Irigoyen J, Lombardero M, Arteaga C, Carpizo JA, Barber D. Limited IgE crossreactivity between Dermatophagoides pteronyssinus and Glycyphagus domesticus in patients naturally exposed to both mite species. J Allergy Clin Immunol 2007 Apr 3
  114. 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
  115. Akdemir C, Gurdal H. House dust mite in Kutahya, Turkey. [Turkish] Turkiye Parazitol Derg 2005;29(2):110-115
  116. 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
  117. 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
  118. 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
  119. Castro Almarales RL, Mateo MM, Naranjo Robalino RM, Navarro Viltre BI, Alvarez CM, et al. Correlation between skin tests to Dermatophagoides pteronyssinus, Dermatophagoides siboney and Blomia tropicalis in Cuban asthmatics. Allergol Immunopathol (Madr ) 2006;34(1):23-26
  120. 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
  121. 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
  122. 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
  123. Xing DR, Wen TH. Prevalence of anaphylaxis to dust mite in human population in Xuzhou. [Chinese] Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi 2004;22(5):287-9
  124. 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
  125. 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
  126. Adalsteinsdottir B, Sigurdardottir ST, Gislason T, Kristensen B, Gislason D. What characterizes house dust mite sensitive individuals in a house dust mite free community in reykjavik, iceland? Allergol Int 2007;56(1):51-6
  127. Guler N, Kirerleri E, Tamay Z, Ones U. Atopy patch testing in children with asthma and rhinitis symptoms allergic to house dust mite. Pediatr Allergy Immunol 2006;17(5):346-50
  128. 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
  129. Tsai JJ, Chen WC. Different age of asthmatic patients affected by different aeroallergens. [Chinese] J Microbiol Immunol Infect 1999;32(4):283-8
  130. 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.