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.


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


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,


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