Abstract
Arthropods are important in human health, which can transmit pathogens to humans, parasitize, or produce important allergens. Allergy prevalence becomes higher in Korea recently as well as other developed countries in contrast to a decrease of infectious diseases. Allergic diseases caused by household arthropods have increased dramatically during the last few decades since human beings spend more their time for indoor activities in modernized life style. Household arthropods are one of the most common causes of allergic diseases. Biological characterization of household arthropods and researches on their allergens will provide better understanding of the pathogenesis of allergic diseases and suggest new therapeutic ways. Therefore, studies on arthropods of allergenic importance can be considered one of the major research areas in medical arthropodology and parasitology. Here, the biology of several household arthropods, including house dust mites and cockroaches, the 2 most well known arthropods living indoor together with humans worldwide, and characteristics of their allergens, especially the research activities on these allergens performed in Korea, are summarized.
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Key words: allergen, allergy, arthropod, cockroach, insect, mite
INTRODUCTION
More than million species of arthropods have been reported to be present in nature. These are very important in the ecosystem, and some species of which are closely related with human health. Arthropod-borne infectious diseases are of great importance, especially in developing countries. Important human parasitic diseases transmitted by arthropods include malaria, trypanosomiasis, leishmaniasis, and filariasis. They also transmit viral diseases, such as yellow fever, dengue fever, and Japanese encephalitis [
1]. Arthropods are also associated with allergic diseases. They are easily found outdoors, however, a limited number of arthropod species co-exists with human beings in our homes. Household arthropods are one of the most common causes of allergic diseases. House dust mites (HDMs) and cockroaches are the most well-known household arthropods, which produce allergenic materials to humans. People are sensitized more with HDM-derived allergens than any others [
2]. In addition to these, several other household arthropods of medical importance, especially in terms of producing allergens are also found in homes. Allergy prevalence is higher in developed countries in contrast to a decrease of infectious diseases. Allergic diseases caused by household arthropods have increased dramatically during the last few decades since humans spend more their time for indoor activities in modernized life style [
3,
4].
Usually IgE-reactive materials are considered allergens. Parasites, especially helminths, produce excretory or secretory materials, which induce IgE responses similar to allergens. A certain kind of parasite-derived materials are true allergens, such as an
Anisakis simplex antigen, Ani s 1 [
5]. However, we do not consider all these parasite-derived materials as allergens. Allergens should increase the IgE level, and should also induce allergic symptoms in atopic individuals. To date, several hundred allergens have been identified from various sources of our environment, including arthropods [
6]. Even though the characteristics of allergens are not possible to be determined completely, allergens can be classified into several groups based on their molecular structures or biological functions. One of the most important groups of allergens is calycins which include lipid-binding proteins, fatty acid binding proteins, and lipocalins. More than 50% of major allergens are known to be calycins. They are normally present in body fluids and secretions in arthropods, and some are known as pheromone-binding proteins [
7,
8]. The protease activity is considered important to be allergenic [
9]. It is believed that protease allergens can directly damage the epitheliumand increase the IgE production. They also have been shown to activate protease activated receptors and subsequently lead to pro-inflammatory responses. None of the known cockroach allergens, however, are active proteases [
10,
11]. But serine proteases in cockroach extract can influence allergic inflammation [
12]. Chitinases are reported to be allergens in HDMs [
13]. Actually, chitin is found in the exoskeletons of arthropods, and seems to contribute to the development of allergic diseases. Recently, mammalian chitinases are known to play an important role in mediating Th2 cell-driven inflammation in asthma [
14]. Tropomyosin was found to be a major allergenic component accounting for the cross-reactivity between insects, mites, nematodes, and crustaceans, which is also an important heat-stable food allergen [
15].
INDOOR ARTHROPOD ALLERGENS
Perennial allergy rather than seasonal type is more likely to be related with indoor arthropod allergy, since indoor arthropods are always found in homes only with some fluctuation of the population density.
House dust mites
More than 40 species of mites have been found in house dust. Of these,
Dermatophagoides farinae and
Dermatophagoides pteronyssinus belonging to the family Pyroglyphidae and class Arachnida are found most frequently. In a narrow sense dust mites are limited to mites belonging to Pyroglyphidae, but other mites found in house dust are also medically important since they can also elicit allergic symptoms with cross-reactive or their own specific molecules. It takes approximately a month from hatching of eggs to the adult stage. Adult mites have 4 pair of legs, but the larvae have 3 pairs. An adult
Dermatophagoides can survive for a few weeks to several months. The HDM feeds on various protein sources, especially shed human skin scales. HDMs take water from their daily food or absorb it from the air. One g of dust may contain several hundred to thousand HDMs. They are found mostly in mattresses, blankets, pillows, and nearby environment in man-dwelling spaces. The most favorable conditions for HDMs are 80-90% relative humidity and a temperature of 23-30℃ [
1]. In Korea,
D. farinae has been more frequently found than
D. pteronyssinus with few exceptions [
16,
17].
D. farinae is supposed to be found in the environment showing lower humidity, such as apartments in the city than
D. pteronyssinus. The number of mites/g dust or the group 1 allergen concentration was the highest in August or in October according to different reports. There was no difference in the HDM inhabitation density among housing, such as a public housing (apartment) and a detached house. That also showed no difference between patients' houses and healthy control people's houses. Approximately one third to a half (31.2-56.9%) of house dust contained more than 2 µg/g of dust of group 1 allergen, which was thought to be high enough to sensitize the people. Ten % of dust samples contained more than 10 µg/g of dust of group 1 allergen, which was supposed to be very high enough to provoke allergy symptoms [
18]. To remove HDMs, frequent washing, cleaning, and drying are recommended. Mechanical laundry is an effective tool for the environmental control of allergens, water temperature, and number of rinsing is a critical factor for the removal of HDMs [
19].
More than 20 groups of dust mite allergenic proteins have been identified and characterized to date [
20]. Dust mite allergens and their biological characteristics and functions are summarized in
Table 1. Several studies performed using HDM crude extract were reported. Production of IL-5 and IL-10 in peripheral blood mononuclear cells was significantly higher in atopic asthmatics than those of non-atopic controls by stimulation of
D. farinae antigen, but IFN-γ production was not [
21]. It was also reported that
D. pteronyssinus extract can increase expression of MCP-1, IL-6, and IL-8 in human monocytic THP-1 cells independent on protease activity [
22]. The group 1 allergen is the most important one, which is a cysteine protease. The protease enzyme activity would be important to induce allergic inflammation [
23]. The patterns of IL-4 and IFN-γ production after Der p 1 stimulation and the effect on the cytokine production from T cells were evaluated, and it was found that there was a significant difference on stimulation index of IFN-γ production as well as IL-4 after Der p 1 stimulation between atopic and non-atopic individuals [
24]. The function of group 2 allergen has not been completely revealed, which was suspected to be related with a male reproductive organ. However, the group 2 allergen was localized in the intestinal epithelium and its content. It was revealed by immunofluorescent antibody technique using monoclonal antibodies [
25-
27]. The ELISA using monoclonal antibody was set up to measure the concentration of group 2 allergen in dust [
28,
29]. Isoallergens of Der p 2 showed different IgE immune responses. Quantification of Der p 2 with 2-site ELISA kits might be affected by the prevalence of the isoallergens in reservoir dust [
30]. Recently, Der f 2 was described to induce phospholipase D1 activation and expression of IL-13 through activation of activating transcription factor-2 in human bronchial epithelial cells [
31]. The group 3, 6, and 9 allergens have serine protease activities, respectively [
20]. Positive association with human leukocyte antigen class II genes and specific IgE responses to Der p 1 and Der p 2 was described in Korean adolescents [
32].
Cross-reactivity between different organisms is believed to occur due to identical or similar IgE-binding epitopes. Tropomyosin derived from
D. farinae was named Der f 10, and was described as a major allergen initially [
33]. However, tropomyosin (Der p 10) from
D. pteronyssinus was cloned thereafter, and the IgE binding frequency of Der p 10 was reported as low as 5.6% [
34].
Storage mites are found in our foods, such as flours, nuts, cakes or rice, and feed on plants and microorganisms. Occupational allergic diseases caused by storage mites have been reported [
35]. Allergic symptoms can be also induced by ingestion of the food contaminated with storage mites. There are a number of reports that storage mite allergens are cross-reactive with HDM allergens [
36]. However, storage mites are recognized as specific inhalant allergens recently [
37]. A bronchial asthma case due to sensitization with
Tyrophagus putrescentiae was reported in Korea [
38].
Blomia spp., especially
Blomia tropicalis, is the most commonly distributed in homes in tropical and subtropical regions, such as Southeast Asia [
39,
40]. The 2 most abundant species of storage mites in Europe are
Lepidoglyphus destructor and
Euroglyphus maynei [
41,
42]. Recently,
L. destructor and
T. putrescentiae were described as the leading causes of allergic sensitization in a general population from warm and humid climates [
37].
T. putrescentiae and
Acarus siro occur worldwide and also could contribute to significant allergen levels in house dust [
43]. There are many other kinds of storage mites reported worldwide which could cause an allergy [
44,
45]. In Korea,
T. putrescentiae is the third most common species of dust mites and the most commonly found species of storage mites in home. They are found especially in the kitchen area nearby the areas where the rice is stored, which is a main food for Koreans [
17]. Although the storage mite specific allergy patient has been reported rarely in Korea, sensitization to storage mites was commonly found [
46]. The sensitization rate to
T. putrescentiae was investigated to be 30.8% of 196 inhabitants in Daejeon as similar as those to
D. farinae (31.2%) and
D. pteronyssinus (29.9%). Of these, 2.6% of patients with perennial asthma showed sensitization to
T. putrescentiae only. Mass rearing technique on
T. putrescentiae was established for the research purpose [
47].
T. putrescentiae extract showed strong cross-reactivity with
D. pteronyssinus extract [
48].
T. putrescentiae specific allergens have been investigated. Expressed sequence tags analysis was performed to identify possible new storage mite allergens, and the cDNA sequence encoding a protein homologous to fatty acid binding protein, a mite group 13 allergen, was identified and named Tyr p 13 [
49]. Cloning and expression of α-tubulin, which sequence was also obtained from
T. putrescentiae expressed sequence tags, was performed. The deduced amino acid sequence of the α-tubulin from the storage mite showed as much as 97.3% identity to the α-tubulin sequences from other organisms. The highly conserved amino acid sequences of α-tubulins across different species of mites may indicate that cross-reactivity for this potential allergen exists [
50]. A cDNA encoding troponin C, homologous to cockroach allergen Bla g 6, was also identified and named Tyr p 24 from
T. putrescentiae expressed sequence tags. It shares 62.7 to 85.5% sequence identity with troponin C from various arthropods. Interestingly, the intensity of IgE binding to troponin C was increased approximately 2-fold by the addition of 10 mM CaCl
2 [
51]. However, Tyr p 24 and Bla g 6 was not shown to be cross-reactive significantly. A partial cDNA sequence encoding tropomyosin was isolated from the cDNA library by immunoscreening using antimouse IgG1 sera raised against
T. putrescentiae whole body extract. Full-length information of
T. putrescentiae tropomyosin was obtained by reverse transcriptase-PCR (RT-PCR). The deduced amino acid sequence shares 64-94% identity with previously known allergenic tropomyosins. Recombinant Tyr p 10 showed 12.5% (5/40) IgE-binding reactivity [
52]. Biological characteristics of storage mite allergens are summarized in
Table 1.
Cockroaches are frequently found in homes worldwide. They had been cave-dwellers with our ancestors, nowadays which are also well adapted to modern human residential areas. Over 3,500 cockroach species exist worldwide. Most of the species live outdoors, but about 50 species live in or around human houses. Reproduction occurs year-round, but do not proliferate fast compared with other insects, such as flies and midges. Their flattened body shape is rather efficient to hide in a narrow space so they can survive easily in our homes. Cockroaches feed on various plants and animal products, including human food, sewage, and garbage. Cockroaches live in kitchens, bathrooms, and other sites close to water sources, since they consume water frequently [
53]. Excreta, regurgitated food, excreted body fluid, dead body, and castovers contain allergenic molecules and elicit strong allergic symptoms in genetically predisposed individuals. Major IgE-binding components of cockroach were found to be concentrated in the feces [
54]. Cockroach-induced asthma is a severe form which would need intensive attention and investigation [
55]. It has been reported that a cockroach allergy is an important risk factor for asthma-related emergency room visits and hospitalization [
56].
Four cockroach species, the German (
Blattella germanica) (36.2%), the American (
Periplaneta americana) (33.3%), the Japanese (
Periplaneta japonica) (1.1%), and the dusky brown (
Periplaneta fuliginosa) (1.7%) cockroach, have been found to infest homes in Seoul, Korea [
57]. The German cockroach,
B. germanica, is the most commonly encountered species in our homes [
58]. The detached house showed higher trapping rates than the apartment. At the same time sensitization rate was investigated so that the positive skin test rates were 46.2% in the healthy control group and 43.8% in the allergy patients. The positive rate of specific IgE to crude German cockroach extract in children with atopic asthma was 18.7%. Of those children, the elevated specific IgE levels both to Bla g 1 and Bla g 2 were 58.3%, respectively [
59]. Very recently, the sensitization rate to cockroach allergens would have decreased in city dwellers since the garbage disposal system is improved and insecticides are supposed to be more commonly used in homes in Korea (personal communication).
The allergenicity of cockroach extract has been demonstrated in human subjects by means of skin tests, bronchial provocation tests, and RASTs [
59]. Immunoblot analysis identified several allergenic components in German cockroach extract with molecular weights of 12.5 to 110 kDa [
60,
61]. It is generally accepted that the major German cockroach allergens are Bla g 1 and Bla g 2. Subsequently, several additional allergens, such as Bla g 4 (lipocalin or calycin), Bla g 5 (glutathione
S-transferase), and Bla g 6 (troponin c) have been cloned, and their allergenicities were studied [
62-
65]. Compared with HDM allergens, cockroach allergens have not been studied in details relatively. Cockroach allergens and their characteristics are summarized in
Table 2. German cockroach extract contains effector molecules to various human cells, which induces activation of human eosinophils to release cytotoxic inflammatory mediators, such as superoxide and granular proteins [
66]. That also has a direct effect on human airway epithelial cells, in particular generating [Ca
++] oscillations through Ca
++ release from thapsigargin-sensitive Ca
++ stores through activation of PAR-2 [
67]. German cockroach extract with protease activity-induced IL-8 expression is regulated by transcriptional activation of NF-κB and NF-IL6 coordinating with the ERK pathway in human airway epithelial cells [
68].
Bla g 1 gene is exclusively expressed by midgut cells, up to 7 amino acid repeats were identified by dotplot matrix analysis [
69]. It shows 37% sequence identity with midgut villi membrane protein from
Tenebrio molitor [
70], but the biological function of cockroach group 1 allergen still remains to be elucidated. Bla g 1 shows high IgE-binding frequency but weak intensity among Korean cockroach-sensitized subjects [
71]. Measurement of Bla g 1 levels has been used to estimate the exposure to cockroach allergens and exposure above 2 U/g dust is thought to be a strong risk factor for sensitization [
72]. Bla g 2 was found to be the most important cockroach allergen, showing the highest prevalence of sensitization (54 to 71%) [
73]. It shows primary sequence homology to aspartic proteinases. However, amino acid substitutions in the catalytic triads of the molecule suggested that Bla g 2 is inactive. High concentrations of Bla g 2 were found to be expressed in digestive organs (esophagus, gut, and proventriculus) and feces [
74]. Cockroach allergens appeared to be particularly effective at sensitizing atopic individuals, considering the finding that the proposed threshold value of Bla g 2 for sensitizing is 0.08 µg/g dust (2 U/g), whereas those of mite group 1 and cat allergens are 2 µg/g dust and 8 µg/g dust, respectively [
75]. Bla g 4 is one of the most important German cockroach allergens, and a major IgE epitope of Bla g 4 was revealed to be located at amino acid sequences 118-152 of C-terminal. Bla g 4 has a sequence diversity [
76]. A study was undertaken to compare the IgE reactivity of German cockroach GSTs, Bla g 5 (sigma class) and delta class GST (BgGSTD1). A certain serum sample with highest IgE reactivity showed a limited cross-reactivity. IgE-binding frequency to the cockroach GSTs was low, but the titer of IgE reactivity was strong in some sera [
64]. Tropomyosin was cloned from the American cockroach (
P. americana), Per a 7, and the purified tropomyosin could recognize 41% (12/29) of IgE-reacting sera [
77,
78]. A cDNA sequence encoding for the German cockroach tropomyosin, Bla g 7, was obtained, and its recombinant protein was produced [
79]. Its recombinant or native protein showed 16-18% IgE reactivity to the sera tested to be a minor allergen. German cockroach tropomyosin has only minor sequence variations that did not seem to affect its allergenicity significantly [
80]. Recombinant German cockroach tropomyosin expressed in
Pichia pastoris showed higher allergenicity than that expressed in
Escherichia coli [
81]. Other factors in addition to the structural differences of native and recombinant proteins may also influence the IgE reactivity of tropomyosin. To investigate the cross-reactive allergenic components of the dusky brown cockroach,
P. fuliginosa, enzyme-linked immunosorbent assay inhibition and immunoblot analyses for the dusky brown cockroach were performed with
B. germanica and
D. farinae allergic sera.
P. fuliginosa appears to possess allergens that are highly cross-reactive with allergens of
B. germanica and
D. farinae [
82]. Tropomyosin was found to be a major allergenic component accounting for the cross-reactivity between cockroaches and dust mites [
83]. Trypsin from German cockroach was found to be a putative allergen [
84], and a serine protease from American cockroach was identified as a major allergen [
85].
Silverfish live in houses, and feed on the starch in human possessions, such as books, clothes, or beddings. Specific IgE reactivity was reported [
86,
87]. There are silverfish in Korean home, but no study has been performed so far. Mosquito bites can elicit allergic reactions; IgE-mediated immediate type responses and delayed type local skin responses [
88]. Rarely systemic anaphylactic reactions may occur [
89], but so far no report has been available in Korea. Various species of non-biting midges, i.e. chironomids cause allergic diseases. Hemoglobin of chironomid larvae has been identified as the most important allergen found in midge-asthmatic patients [
90]. Recently, analysis of adult midge
Chironomus kiiensis has identified tropomyosin (Chi k 10) as an important allergen in Korea [
91,
92]. Cross-reactivity of allergens is an important issue. Tropomyosin from various arthropods is the most well characterized example [
82]. Paramyosin, arginine kinase, and glutathione
S-transferase are also considered pan-allergens [
93,
94]. The mayfly, caddisfly, housefly, and fruit fly were reported to be the source of allergens [
95,
96]. However, no report is available in Korea. It is also well known that fire ants (
Pachycondyla chinensis) contain potent allergens in their venom [
97-
99]. The fire ant stings and injects venomous components similar to those of wasps, which can cause systemic allergic reactions. Major allergens from
P. chinensis belonging to the antigen 5 family were characterized [
100]. The Pharaoh ant,
Monomorium pharaonis, often infests homes and can cause respiratory allergy, which was initially reported in Korea [
101]. Various kinds of arthropods, such as lady bugs, beetles, rice weevils, bedbugs, crickets, spiders, booklice (
Fig. 1), pill bugs, earwigs, and flour beetles in our homes may cause allergies, but little is known about their respective allergens [
102,
103].
CONCLUSIONS
Human beings live together with small creatures, especially several kinds of arthropods, in homes with or without recognition. These arthropods rarely transmit infectious organisms to humans, but they produce excreta, secretions, and leave dead bodies containing allergenic molecules. Allergic diseases have increased worldwide recently and information on household arthropod allergens also has been accumulated. Household arthropods and their allergenic products, however, need more investigation in Korea and worldwide. Studies on the characteristics, biological functions, and molecular structures of allergens, and their interactions with host cells can provide us with valuable scientific information to understand the basic mechanism for development of allergic diseases, and facilitate practical development of new therapeutic drugs in the future.
References
- 1. Guerrant RL, Walker DH, Weller PF. Tropical infectious diseases; principles, pathogenesis, & practice. 2006, 2nd ed. Philadelphia, USA. Elsevier Churchill Livingston. pp 77-81.
- 2. Ree HI. Medical Entomology. 2005, 4th ed. Seoul, Korea. Komunsa. pp 362-366.
- 3. Jeong KY, Hong CS, Yong TS. Domestic arthropods and their allergens. Protein Pept Lett 2007;14:934-942.
- 4. Linneberg A. Are we getting enough allergens? Int Arch Allergy Immunol 2008;147:93-100.
- 5. Ibarrola I, Arilla MC, Herrero MD, Esteban MI, Martinez A, Asturias JA. Expression of a recombinant protein immunochemically equivalent to the major Anisakis simplex allergen Ani s 1. J Investig Allergol Clin Immunol 2008;18:78-83.
- 6. Gaffin JM, Phipatanakul W. The role of indoor allergens in the development of asthma. Curr Opin Allergy Clin Immunol 2009;9:128-135.
- 7. Mantyjarvi R, Rautiainen J, Virtanen T. Lipocalins as allergens. Biochim Biophys Acta 2000;1482:308-317.
- 8. Trompette A, Divanovic S, Visintin A, Blanchard C, Hedge RS, Madan R, Thorne PS, Wills-Karp M, Giovannini TL, Weiss JP, Karp CL. Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein. Nature 2009;457:585-588.
- 9. Chapman MD, Wunschmann S, Pomes A. Proteases as Th2 adjuvants. Curr Allergy Asthma Rep 2007;7:363-367.
- 10. Jeong KY, Hong CS, Yong TS. Recombinant allergens for diagnosis and immunotherapy of allergic disorders, with emphasis on cockroach allergy. Curr Protein Pept Sci 2006;7:57-71.
- 11. Pomes A, Wunschmann S, Hindley J, Vailes LD, Chapman MD. Cockroach allergens: function, structure and allergenicity. Protein Pept Lett 2007;14:960-969.
- 12. Jeong SK, Kim HJ, Youm JK, Ahn SK, Choi EH, Sohn MH, Kim KE, Hong JH, Shin DM, Lee SH. Mite and cockroach allergens activate protease-activated receptor 2 and delay epidermal permeability barrier recovery. J Invest Dermatol 2008;128:1930-1939.
- 13. 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;36:831-839.
- 14. Shuhui L, Mok YK, Wong WS. Role of mammalian chitinases in asthma. Int Arch Allergy Immunol 2009;149:369-377.
- 15. Taylor SL, Lehrer SB. Principles and characteristics of food allergens. Crit Rev Food Sci Nutr 1996;36:S91-S118.
- 16. Lee WK, Cho BK. An ecological study on the house dust mite. Korean J Dermatol 1984;22:286-294.
- 17. Ree HI, Jeon SH, Lee IY, Hong CS, Lee DK. Fauna and geographical distribution of house dust mites in Korea. Korean J Parasitol 1997;35:9-17.
- 18. Hong CS. House dust mites and clinical allergy. J Korean Soc Allergol 1991;11:297-308.
- 19. Park JW, Kim CW, Kang DB, Lee IY, Choi SY, Yong TS, Shin DC, Kim KE, Hong CS. Low-flow, long-term air sampling under normal domestic activity to measure house dust mite and cockroach allergens. J Investig Allergol Clin Immunol 2002;12:293-298.
- 20. Thomas WR, Heinrich TK, Smith WA, Hales BJ. Pyroglyphid house dust mite allergens. Protein Pept Lett 2007;14:943-953.
- 21. Park JW, Hong CS, Ko SH, Kim CW. IL-5 and IL-10 production of peripheral blood mononuclear cells by stimulation of D. farinae antigen in atopic asthmatics. J Asthma Allergy Clin Immunol 1999;19:557-565.
- 22. Lee JS, Kim IS, Ryu JS, Yun CY. House dust mite, Dermatophagoides pteronyssinus increases expression of MCP-1, IL-6, and IL-8 in human monocytic THP-1 cells. Cytokine 2008;42:365-371.
- 23. Ghaemmaghami AM, Robins A, Gough L, Sewell HF, Shakib F. Human T cell subset commitment determined by the intrinsic property of antigen: the proteolytic activity of the major mite allergen Der p 1 conditions T cells to produce more IL-4 and less IFN-γ. Eur J Immunol 2001;31:1211-1216.
- 24. Oh JW, Lee HB, Chung YH, Choi Y, Song MK. The difference of interleukin-4 and interferon-γ production of Der p 1 stimulated T cells and effects of immunomodulator in house dust mite sensitive atopic and non-atopic individuals. J Asthma Allergy Clin Immunol 1999;19:548-556.
- 25. Park GM, Lee SM, Lee IY, Ree HI, Kim KS, Hong CS, Yong TS. Localization of a major allergen, Der p 2, in the gut and faecal pellets of Dermatophagoides pteronyssinus. Clin Exp Allergy 2000;30:1293-1297.
- 26. 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;57:729-731.
- 27. 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;13:36-42.
- 28. Jeong KY, Jin HS, Oh SH, Hong CS, Lee IY, Ree HI, Yong TS. Monoclonal antibodies to recombinant Der f 2 and development of a two-site ELISA sensitive to major Der f 2 isoallergen in Korea. Allergy 2002;57:29-34.
- 29. Yong TS, Lee SM, Park GM, Lee IY, Ree HI, Kim KS, Oh SH, Park JW, Hong CS. Monoclonal antibodies to recombinant Der p 2, a major house dust mite allergen: specificity, epitope analysis and development of two-site capture ELISA. Korean J Parasitol 1999;37:163-169.
- 30. Park JW, Kim KS, Jin HS, Kim CW, Kang DB, Choi SY, Yong TS, Oh SH, Hong CS. Der p 2 isoallergens have different allergenicity, and quantification with 2-site ELISA using monoclonal antibodies is influenced by the isoallergens. Clin Exp Allergy 2002;32:1042-1047.
- 31. Park SY, Cho JH, Oh DY, Park JW, Ahn MJ, Han JS, Oh JW. House dust mite allergen Der f 2-induced phospholipase D1 activation is critical for the production of interleukin-13 through activating transcription factor-2 activation in human bronchial epithelial cells. J Biol Chem 2009;284:20099-20110.
- 32. Kim YK, Oh SY, Oh HB, Lee BJ, Son JW, Cho SH, Kim YY, Min KU. Positive association between HLA-DRB1*07 and specific IgE responses to purified major allergens of D. pteronyssinus (Der p 1 and Der p 2). Ann Allergy Asthma Immunol 2002;88:170-174.
- 33. 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, Dermatophagoides farinae. J Allergy Clin Immunol 1995;96:74-83.
- 34. Asturias JA, Arilla MC, Gómez-Bayón N, Martínez A, Martínez 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;1397:27-30.
- 35. Revsbech P, Dueholm M. Storage mite allergy among bakers. Allergy 1990;45:204-208.
- 36. Park JW, Ko SH, Yong TS, Ree HI, Jeoung BJ, Hong CS. Cross-reactivity of Tyrophagus putrescentiae with Dermatophagoides farinae and Dermatophagoides pteronyssinus in urban areas. Ann Allergy Asthma Immunol 1999;83:533-539.
- 37. Vidal C, Boquete O, Gude F, Rey J, Meijide LM, Fernandez-Merino MC, Gonzalez-Quintela A. High prevalence of storage mite sensitization in a general adult population. Allergy 2004;59:401-405.
- 38. Choi DR, Kim HS, Koh CO, Kim HS, Yoon HS, Park YB, Kim SH, Lee JY. A case of bronchial asthma due to Tyrophagus putrescentiae in a non occupational setting. J Asthma Allergy Clin Immunol 2004;24:141-145.
- 39. Fernandez-Caldas E, Lockey RF. Blomia tropicalis, a mite whose time has come. Allergy 2004;59:1161-1164.
- 40. Chua KY, Cheong N, Kuo IC, Lee BW, Yi FC, Huang CH, Liew LN. The Blomia tropicalis allergens. Protein Pept Lett 2007;14:325-333.
- 41. Hart BJ, Whitehead L. Ecology of house dust mites in Oxfordshire. Clin Exp Allergy 1990;20:203-209.
- 42. Franz JT, Masuch G, Musken H, Bergmann KC. Mite fauna of German farms. Allergy 1997;52:1233-1237.
- 43. Musken H, Franz JT, Wahl R, Paap A, Cromwell O, Masuch G, Bergmann KC. Sensitization to different mite species in German farmers: clinical aspects. J Investig Allergol Clin Immunol 2000;10:346-351.
- 44. Krol A, Krafchik B. The differential diagnosis of atopic dermatitis in childhood. Dermatol Ther 2006;19:73-82.
- 45. Groenewoud GC, de Graafin't Veld C, vVan Oorschot-van Nes AJ, de Jong NW, Vermeulen AM, van Toorenenbergen AW, Burdorf A, de Groot H, Gerth van Wijk R. Prevalence of sensitization to the predatory mite Amblyseius cucumeris as a new occupational allergen in horticulture. Allergy 2002;57:614-619.
- 46. Lee JY. Tyrophagus putrescentiae: an important allergen in Daejeon. J Asthma Allergy Clin Immunol 2002;22:703-710.
- 47. Ree HI, Lee IY. Development of mass rearing technique of Tyrophagus putrescentiae (Acari: Acaridae) found in house dust. Korean J Parasitol 1997;35:149-154.
- 48. Munhbayarlah S, Park JW, Ko SH, Ree HI, Hong CS. Identification of Tyrophagus putrescentiae allergens and evaluation of cross-reactivity with Dermatophagoides pteronyssinus. Yonsei Med J 1998;39:109-115.
- 49. Jeong KY, Kim WK, Lee JS, Lee J, Lee IY, Kim KE, Park JW, Hong CS, Ree HI, Yong TS. Immunoglobulin E reactivity of recombinant allergen Tyr p 13 from Tyrophagus putrescentiae homologous to fatty acid binding protein. Clin Diagn Lab Immunol 2005;12:581-585.
- 50. Jeong KY, Lee H, Lee JS, Lee J, Lee IY, Ree HI, Hong CS, Park JW, Yong TS. Immunoglobulin E binding reactivity of a recombinant allergen homologous to α-tubulin from Tyrophagus putrescentiae. Clin Diagn Lab Immunol 2005;12:1451-1454.
- 51. Jeong KY, Kim CR, Un S, Yi MH, Lee IY, Park JW, Hong CS, Yong TS. Allergenicity of recombinant troponin C from Tyrophagus putrescentiae. Int Arch Allergy Immunol 2010;151:207-213.
- 52. Jeong KY, Lee H, Lee JS, Lee J, Lee IY, Ree HI, Hong CS, Yong TS. Molecular cloning and the allergenic characterization of tropomyosin from Tyrophagus putrescentiae. Protein Pept Lett 2007;14:431-436.
- 53. Arruda LK. Cockroach allergens. Curr Allergy Asthma Rep 2005;5:411-416.
- 54. Yun YY, Ko SH, Park JW, Lee IY, Ree HI, Hong CS. Comparison of allergenic components between German cockroach whole body and fecal extracts. Ann Allergy Asthma Immunol 2001;86:551-556.
- 55. Kang BC, Wu CW, Johnson J. Characteristics and diagnoses of cockroach-sensitive bronchial asthma. Ann Allergy 1992;68:237-244.
- 56. Litonjua AA, Carey VJ, Burge HA, Weiss ST, Gold DR. Exposure to cockroach allergen in the home is associated with incident doctor-diagnosed asthma and recurrent wheezing. J Allergy Clin Immunol 2001;107:41-47.
- 57. Jeong KY, Lee IY, Lee J, Ree HI, Hong CS, Yong TS. Effectiveness of education for control of house dust mites and cockroaches in Seoul, Korea. Korean J Parasitol 2006;44:73-79.
- 58. Kim WK, Kim CH, Lee KE, Shon MH, Jang GC, Kim KE, Lee IY, Jeong KY, Lee JW, Yong TS, Kim CW, Park JW, Hong CS. Seasonal distribution of cockroaches, a major source of indoor allergens, in Seoul metropolitan area. J Asthma Allergy Clin Immunol 2002;22:728-735.
- 59. Lee SY, Kim KE, Kim DS, Kim DH, Lee KY. A study of antigen provocation test with German cockroach in atopic asthmatic children. Ped Allergy Respir Dis 1993;3:83-93.
- 60. Jeoung BJ, Ryu JW, Yum HY, Park JW, Hong CS, Lee HB, Yong TS, Kim KE, Lee KY. Identification and characterization of German cockroach allergen. Ped Allergy Respir Dis 1998;8:221-228.
- 61. Yong TS, Lee JS, Lee J, Park SJ, Jeon SH, Ree HI, Park JW. Identification and purification of IgE-reactive proteins in German cockroach extract. Yonsei Med J 1999;40:283-289.
- 62. Lee H, Jeong KY, Shin KH, Yi MH, Gantulaga D, Hong CS, Yong TS. Reactivity of German cockroach allergen, Bla g 2, peptide fragments to IgE antibodies in patients' sera. Korean J Parasitol 2008;46:243-246.
- 63. Shin KH, Jeong KY, Hong CS, Yong TS. IgE binding reactivity of peptide fragments of Bla g 4, a major German cockroach allergen. Korean J Parasitol 2009;47:31-36.
- 64. Jeong KY, Jeong KJ, Yi MH, Lee H, Hong CS, Yong TS. Allergenicity of sigma and delta class glutathione S-transferases from the German cockroach. Int Arch Allergy Immunol 2009;148:59-64.
- 65. Jeong KY, Lee H, Shin KH, Yi MH, Jeong KJ, Hong CS, Yong TS. Sequence polymorphisms of major German cockroach allergens Bla g 1, Bla g 2, Bla g 4, and Bla g 5. Int Arch Allergy Immunol 2009;145:1-8.
- 66. Sohn MH, Lee YA, Jeong KY, Sim S, Kim KE, Yong TS, Shin MH. German cockroach extract induces activation of human eosinophils to release cytotoxic inflammatory mediators. Int Arch Allergy Immunol 2004;134:141-149.
- 67. Hong JH, Lee SI, Kim KE, Yong TS, Seo JT, Sohn MH, Shin DM. German cockroach extract activates protease-activated receptor 2 in human airway epithelial cells. J Allergy Clin Immunol 2004;113:315-319.
- 68. Lee KE, Kim JW, Jeong KY, Kim KE, Yong TS, Sohn MH. Regulation of German cockroach extract-induced IL-8 expression in human airway epithelial cells. Clin Exp Allergy 2007;37:1364-1373.
- 69. Pomés A, Melén E, Vailes LD, Retief JD, Arruda LK, Chapman MD. Novel allergen structures with tandem amino acid repeats derived from German and American cockroach. J Biol Chem 1998;273:30801-30807.
- 70. Shao L, Devenport M, Fujioka H, Ghosh A, Jacobs-Lorena M. Identification and characterization of a novel peritrophic matrix protein, Ae-Aper50, and the microvillar membrane protein, AEG 12, from the mosquito, Aedes aegypti. Insect Biochem Mol Biol 2005;35:947-959.
- 71. Yi MH, Jeong KY, Kim CR, Yong TS. IgE-binding reactivity of peptide fragments of Bla g 1.02, a major German cockroach allergen. Asian Pac J Allergy Immunol 2009;27:121-129.
- 72. Eggleston PA, Rosenstreich D, Lynn H, Gergen P, Baker D, Kattan M, Mortimer KM, Mitchell H, Ownby D, Slavin R, Malveaux F. Relationship of indoor allergen exposure to skin test sensitivity in inner-city children with asthma. J Allergy Clin Immunol 1998;102:563-570.
- 73. Satinover SM, Reefer AJ, Pomes A, Chapman MD, Platts-Mills TA, Woodfolk JA. Specific IgE and IgG antibody-binding patterns to recombinant cockroach allergens. J Allergy Clin Immunol 2005;115:803-809.
- 74. Arruda LK, Vailes LD, Mann BJ, Shannon J, Fox JW, Vedvick TS, Hayden ML, Chapman MD. Molecular cloning of a major cockroach (Blattella germanica) allergen, Bla g 2. Sequence homology to the aspartic proteases. J Biol Chem 1995;270:19563-19568.
- 75. 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:S2-S24.
- 76. Jeong KY, Yi MH, Jeong KJ, Lee H, Hong CS, Yong TS. Sequence diversity of the Bla g 4 cockroach allergen, homologous to lipocalins, from Blattella germanica. Int Arch Allergy Immunol 2009;148:339-345.
- 77. Asturias JA, Gómez-Bayón N, Arilla MC, Martínez A, Palacios R, Sánchez-Gascón F, Martínez J. Molecular characterization of American cockroach tropomyosin (Periplaneta americana allergen 7), a cross-reactive allergen. J Immunol 1999;162:4342-4348.
- 78. Sookrung N, Indrawattana N, Tungtrongchitr A, Bunnag C, Tantilipikorn P, Kwangsri S, Chaicump W. Allergenicity of native/recombinant tropomyosin, Per a 7, of American cockroach (CR), Periplaneta americana, among CR allergic Thais. Asian Pac J Allergy Immunol 2009;27:9-17.
- 79. Jeong KY, Lee J, Lee IY, Ree HI, Hong CS, Yong TS. Allergenicity of recombinant Bla g 7, German cockroach tropomyosin. Allergy 2003;58:1059-1063.
- 80. Jeong KY, Lee J, Lee IY, Ree HI, Hong CS, Yong TS. Analysis of amino acid sequence variations and immunoglobulin E-binding epitopes of German cockroach tropomyosin. Clin Diagn Lab Immunol 2004;11:874-878.
- 81. Jeong KY, Lee J, Lee IY, Hong CS, Ree HI, Yong TS. Expression of tropomyosin from Blattella germanica as a recombinant nonfusion protein in Pichia pastoris and comparison of its IgE reactivity with its native counterpart. Protein Expr Purif 2004;37:273-278.
- 82. Jeong KY, Hong CS, Yong TS. Allergenic tropomyosins and their cross-reactivities. Protein Pept Lett 2006;13:835-845.
- 83. 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;11:680-685.
- 84. Ock MS, Kim BJ, Kim SM, Byun KH. Cloning and expression of trypsin-encoding cDNA from Blattella germanica and its possibility as an allergen. Korean J Parasitol 2005;43:101-110.
- 85. Sudha VT, Arora N, Gaur SN, Pasha S, Singh BP. Identification of a serine protease as a major allergen (Per a 10) of Periplaneta americana. Allergy 2008;63:768-776.
- 86. Barletta B, Puggioni EM, Afferni C, Butteroni C, Iacovacci P, Tinghino R, Ariano R, Panzani RC, Di Felice G, Pini C. Preparation and characterization of silverfish (Lepisma saccharina) extract and identification of allergenic components. Int Arch Allergy Immunol 2002;128:179-186.
- 87. Barletta B, Di Felice G, Pini C. Biochemical and molecular biological aspects of silverfish allergens. Protein Pept Lett 2007;14:970-974.
- 88. Peng Z, Estelle F, Simons R. Mosquito allergy and mosquito salivary allergens. Protein Pept Lett 2007;14:975-981.
- 89. McCormack DR, Salata KF, Hershey JN, Carpenter GB, Engler RJ. Mosquito bite anaphylaxis: immunotherapy with whole body extracts. Ann Allergy Asthma Immunol 1995;74:39-44.
- 90. Baur X, Dewair M, Fruhmann G, Aschauer H, Pfletschinger J, Braunitzer G. Hypersensitivity to chironomids (non-biting midges): localization of the antigenic determinants within certain polypeptide sequences of hemoglobins (erythrocruorins) of Chironomus thummi thummi (Diptera). J Allergy Clin Immunol 1982;69:66-76.
- 91. Yong TS, Lee JS, Lee IY, Park SJ, Park GM, Ree HI, Park JW, Hong CS, Park HS. Identification of Chironomus kiiensis allergens, a dominant species of non-biting midges in Korea. Korean J Parasitol 1999;37:171-179.
- 92. Jeong KY, Yum HY, Lee IY, Ree HI, Hong CS, Kim DS, Yong TS. Molecular cloning and characterization of tropomyosin, a major allergen of Chironomus kiienesis, a dominant species of nonbiting midges in Korea. Clin Diagn Lab Immunol 2004;11:320-324.
- 93. Aalberse RC, Akkerdaas J, van Ree R. Cross-reactivity of IgE antibodies to allergens. Allergy 2001;56:478-490.
- 94. Binder M, Mahler V, Hayek B, Sperr WR, Scholler M, Prozell S, Wiedermann G, Valent P, Valenta R, Duchene M. Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen. J Immunol 2001;167:5470-5477.
- 95. Smith TS, Hogan MB, Welch JE, Corder WT, Wilson NW. Modern prevalence of insect sensitization in rural asthma and allergic rhinitis patients. Allergy Asthma Proc 2005;26:356-360.
- 96. Kino T, Chihara J, Fukuda K, Sasaki Y, Shogaki Y, Oshima S. Allergy to insects in Japan. III. High frequency of IgE antibody responses to insects (moth, butterfly, caddis fly, and chironomid) in patients with bronchial asthma and immunochemical quantitation of the insect-related airborne particles smaller than 10 microns in diameter. J Allergy Clin Immunol 1987;79:857-866.
- 97. Yun YY, Ko SH, Park JW, Hong CS. Anaphylaxis to venom of the Pachycondyla species ant. J Allergy Clin Immunol 1999;104:879-882.
- 98. Kim SS, Park HS, Kim HY, Lee SK, Nahm DH. Anaphylaxis caused by the new ant, Pachycondyla chinensis: demonstration of specific IgE and IgE-binding components. J Allergy Clin Immunol 2001;107:1095-1099.
- 99. Cho YS, Lee YM, Lee CK, Yoo B, Park HS, Moon HB. Prevalence of Pachycondyla chinensis venom allergy in ant-infested area in Korea. J Allergy Clin Immuol 2002;110:54-57.
- 100. Lee EK, Jeong KY, Lyu DP, Lee YW, Sohn JH, Lim KJ, Hong CS, Park JW. Characterization of the major allergens of Pachycondyla chinensis in ant sting anaphylaxis patients. Clin Exp Allergy 2009;39:602-607.
- 101. Kim CW, Choi SY, Park JW, Hong CS. Respiratory allergy to the indoor ant (Monomorium pharaonis) not related to sting allergy. Ann Allergy Asthma Immunol 2005;94:301-306.
- 102. Bagenstose AH 3rd, Mathews KP, Homburger HA, Saaveard-Delgado AP. Inhalant allergy due to crickets. J Allergy Clin Immunol 1980;65:71-74.
- 103. Alanko K, Tuomi T, Vanhanen M, Pajari-Backas M, Kanerva L, Havu K, Saarinen K, Bruynzeel DP. Occupational IgE-mediated allergy to Tribolium confusum (confused flour beetle). Allergy 2000;55:879-882.
Fig. 1Booklouse (Lipocelis sp.) isolated from a dust bag of a house-hold vacuum cleaner.
Table 1.Characteristics of house dust mite allergens
Table 1.
|
Group |
Biochemical identity |
Molecular weight (kDa) |
Allergen |
Species |
|
1 |
Cysteine protease |
25 |
Der p 1 |
Dermatophagoides pteronyssinus
|
|
|
|
Der f 1 |
Dermatophagoides farinae
|
|
|
|
Blo t 1 |
Blomia tropicalis
|
|
|
|
Pso o 1 |
Psoroptes ovis
|
|
2 |
Niemann-Pick C2 homologue |
14 |
Der p 2 |
D. pteronyssinus
|
|
|
|
Der f 2 |
D. farinae
|
|
|
|
Blo t 2 |
B. tropicalis
|
|
|
|
Tyr p 2 |
Tyrophagus putrescentiae
|
|
|
|
Lep d 2 |
Lepidoglyphus destructor
|
|
|
|
Gly d 2 |
Glycyphagus domesticus
|
|
|
|
Aca s 2 |
Acarus siro
|
|
|
|
Sui m 2 |
Suidasia medanensis
|
|
|
|
Pso o 2 |
P. ovis
|
|
3 |
Trypsin |
25 |
Der p 3 |
D. pteronyssinus
|
|
|
|
Der f 3 |
D. farinae
|
|
|
|
Der s 3 |
Dermatophagoides siboney
|
|
|
|
Blo t 3 |
B. tropicalis
|
|
|
|
Tyr p 3 |
T. putrescentiae
|
|
|
|
Eur m 3 |
Euroglyphus maynei
|
|
|
|
Lep d 3 |
L. destructor
|
|
|
|
Gly d 3 |
G. domesticus
|
|
|
|
Sar s 3 |
Sarcoptes scabiei
|
|
4 |
Alpha-amylase |
56 |
Der p 4 |
D. pteronyssinus
|
|
|
|
Blo t 4 |
B. tropicalis
|
|
5 |
Unknown |
15 |
Der p 5 |
D. pteronyssinus
|
|
|
|
Blo t 5 |
B. tropicalis
|
|
|
|
Lep d 5 |
L. destructor
|
|
|
|
Gly d 5 |
G. domesticus
|
|
6 |
Chymotrypsin |
25 |
Der p 6 |
D. pteronyssinus
|
|
|
|
Der f 6 |
D. farinae
|
|
7 |
Unknown |
24 |
Der p 7 |
D. pteronyssinus
|
|
|
|
Der f 7 |
D. farinae
|
|
|
|
Lep d 7 |
L. destructor
|
|
|
|
Gly d 7 |
G. domesticus
|
|
8 |
Glutathione S-transferase |
26 |
Der p 8 |
D. pteronyssinus
|
|
|
|
Lep d 8 |
L. destructor
|
|
|
|
Gly d 8 |
G. domesticus
|
|
9 |
Collagenolytic serine protease |
29 |
Der p 9 |
D. pteronyssinus
|
|
10 |
Tropomyosin |
35 |
Der p 10 |
D. pteronyssinus
|
|
|
|
Der f 10 |
D. farinae
|
|
|
|
Blo t 10 |
B. tropicalis
|
|
|
|
Tyr p 10 |
T. putrescentiae
|
|
|
|
Lep d 10 |
L. destructor
|
|
|
|
Gly d 10 |
G. domesticus
|
|
|
|
Cho a 10 |
Chortoglyphus arcuatus
|
|
|
|
Pso o 10 |
P. ovis
|
|
11 |
Paramyosin |
100 |
Der p 11 |
D. pteronyssinus
|
|
|
|
Der f 11 |
D. farinae
|
|
|
|
Blo t 11 |
B. tropicalis
|
|
|
|
Pso o 11 |
P. ovis
|
|
|
|
Sar s 11 |
S. scabiei
|
|
12 |
Unknown |
14 |
Blo t 12 |
B. tropicalis
|
|
|
|
Lep d 12 |
L. destructor
|
|
13 |
Fatty acid binding protein |
15 |
Blo t 13 |
B. tropicalis
|
|
|
|
Tyr p 13 |
T. putrescentiae
|
|
|
|
Lep d 13 |
L. destructor
|
|
|
|
Gly d 13 |
G. domesticus
|
|
|
|
Aca s 13 |
A. siro
|
|
14 |
Vitellogenin-apolipophorin like |
177 |
Der p 14 |
D. pteronyssinus
|
|
|
|
Der f 14 |
D. farinae
|
|
|
|
Pso o 14 |
P. ovis
|
|
15 |
Chitinase |
63 |
Der f 15 |
D. farinae
|
|
16 |
Gelsolin |
55 |
Der f 16 |
D. farinae
|
|
17 |
Calcium binding EF protein |
30 |
Der f 17 |
D. farinae
|
|
18 |
Chitinase-like |
60 |
Der f 18 |
D. farinae
|
|
19 |
Antimicrobial peptide |
7 |
Blo t 19 |
B. tropicalis
|
|
20 |
Arginine kinase |
20 |
Der p 20 |
D. pteronyssinus
|
|
21 |
Unknown |
|
Der p 21 |
D. pteronyssinus
|
|
|
|
Blo t 21 |
B. tropicalis
|
|
22 |
Unknown |
|
Der p 22 |
D. pteronyssinus
|
|
23 |
Unknown |
14 |
Der p 23 |
D. pteronyssinus
|
|
24 |
Troponin C |
18 |
Tyr p 24 |
T. putrescentiae
|
|
α-tubulin |
51 |
|
L. destructor
|
|
|
|
|
T. putrescentiae
|
|
Heat shock protein 70 |
70 |
|
D. farinae
|
|
|
|
|
B. tropicalis
|
Table 2.Characteristics of cockroach allergens
Table 2.
|
Group |
Biochemical identity |
Molecular weight (MW) |
Allergen |
Species |
|
1 |
Midgut microvilli protein homologue |
25-90 |
Bla g 1 |
Blattella germanica
|
|
|
|
Per a 1 |
Periplaneta americana
|
|
2 |
Aspartic protease homologue (inactive) |
36 |
Bla g 2 |
B. germanica
|
|
|
|
Per a 2 |
P. americana
|
|
3 |
Arylphorin/hemocyanin |
46-79 |
Per a 3 |
P. americana
|
|
4 |
Lipocalin |
21 |
Bla g 4 |
B. germanica
|
|
|
|
Per a 4 |
P. americana
|
|
5 |
Glutathione S-transferase (Sigma class) |
23 |
Bla g 5 |
B. germanica
|
|
6 |
Troponin C |
17 |
Bla g 6 |
B. germanica
|
|
|
|
Per a 6 |
P. americana
|
|
7 |
Tropomyosin |
33 |
Bla g 7 |
B. germanica
|
|
|
|
Per a 7 |
P. americana
|
|
|
|
Per f 7 |
Periplaneta fuliginosa
|
|
8 |
Myosin light chain |
|
Bla g 8 |
B. germanica
|
|
9 |
Arginine kinase |
40 |
Per a 9 |
P. americana
|
|
10 |
Serine protease |
28 |
Per a 10 |
P. americana
|
|
Trypsin |
28 |
|
B. germanica
|
|
Glutathione S-transferase (Delta class) |
25.7 |
|
B. germanica
|
