On the potential significance of the enzymatic activity of mite allergens to immunogenicity. Clues to structure and function revealed by molecular characterization

Clinical and Experimental Allergy

Volumn 27, Issue 1, 1997, Pages 10-21

  Robinson, C ^a   Kalsheker, N A ^b   Srinivasan, N ^c   King, C M ^d,e   Garrod, D R ^f   Thompson, P J ^e   Stewart, G A ^g  

^a ST GEORGE'S UNIVERSITY OF LONDON   (United Kingdom)

^b QUEEN S MEDICAL CENTRE   (United Kingdom)

^c UNIVERSITY OF LONDON   (United Kingdom)

^d UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

^e UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

^f UNIVERSITY OF MANCHESTER   (United Kingdom)

^g NONE

Author keywords

[No Author keywords available]

Indexed keywords

ALLERGEN; IMMUNOGLOBULIN E;

ALLERGY; AMINO ACID SEQUENCE; DERMATOPHAGOIDES; ENZYME ACTIVITY; HUMAN; IMMUNOGENICITY; NONHUMAN; PRIORITY JOURNAL; REVIEW;

ALLERGENS; AMINO ACID SEQUENCE; ANIMALS; ANTIGENS; ANTIGENS, DERMATOPHAGOIDES; CYSTEINE ENDOPEPTIDASES; GLYCOPROTEINS; HUMANS; MITES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0031026372     PISSN: 09547894     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2222.1997.tb00667.x     Document Type: Review

References (58)

1. Aas K. What makes an allergen an allergen? Allergy 1978; 33:3-14.
2. Robinson C. The airway epithelium: the origin and target of inflammatory airways disease and injury. In Holgate S, ed. Immunopharmacology of the respiratory system. London: Academic Press 1995, 187-207.
3. 99mTc-DTPA in asthma. Am Rev Respir Dis 1989; 139:1139-43.
4. Elia C, Bucca C, Rolla G, Scappaticci E, Cantino D. Freeze-fracture study of human bronchial epithelium in normal, bronchitic and asthmatic subjects. J Submicrosc Cytol 1988; 20:509-17.
5. Schroeckenstein W, Busse WW. Viral bronchitis in childhood: relationship to asthma and obstructive lung disease. Sem Resp Infect 1988; 3:40-48.
6. Herbert CA, Arthur MJP, Robinson C. Eosinophils augment gelatinase activity in the airway mucosa. Comparative effects as a putative mediator of epithelial injury. Br J Pharmacol 1996; 117:667-74.
7. Herbert CA, Edwards D, Boot JR, Robinson C. Stimulated eosinophils and proteinases augment the transepithelial flux of albumin in bovine bronchial mucosa. Br J Pharmacol 1993; 110:840-6.
8. Hahn DL. Infectious asthma: a re-emerging clinical entity? J Fam Prac 1995; 41:153-7.
9. Herbert CA, King CM, Ring PC et al. Augmentation of permeability in the bronchial epithelium by the house dust mite allergen Der p 1. Am J Respir Cell Mol Biol 1995; 12:369-78.
10. Travis J, Potempa J, Maeda H. Are bacterial proteinases pathogenic factors? Trends in Microbiol 1995; 3:405-7.
11. Stewart, GA. Molecular biology of allergens. In: Busse WW, Holgate ST, eds: Asthma and rhinitis. Oxford: Blackwell Science, 1994: 898-932.
12. Chu KY, Stewart GA, Thomas WR et al. Sequence analysis of cDNA coding for a major house dust mite allergen. Der p I. Homology with cysteine proteases. J Exp Med 1988; 167:175-82.
13. Dilworth RJ, Chua KY, Thomas WR. Sequence analysis of cDNA coding for a major house dust mite allergen, Der f I. Clin Exp Allergy 1991; 21:25-32.
14. Kent NA, Hill MR, Keen JN, Holland PWH, Hart BJ. Molecular characterization of group I allergen Eur m I from house dust mite Euroglyphus maynei. Int Archs Allergy Immunol 1992; 99:150-2.
15. Stewart GA, Thompson PJ, Simpson RJ. Protease antigens from house dust mite. Lancet 1989; 2:154-5; and correction: Lancet 1989; 2:462.
16. Topham CM, Srinivasan N, Thorpe CJ, Overington JP, Kalsheker NA. Comparative modelling of major house dust mite allergen Der p I: structure validation using an extended environmental amino acid propensity table. Protein Engng 1994; 7:869-94.
17. Chua KY, Kehal PK, Thomas WR. Sequence polymorphisms of cDNA clones encoding the mite allergen Der p I. Int Arch Allergy Immunol 1993; 101:364-8.
18. Hewitt CRA, Brown AP, Hart BJ, Pritchard DI. A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: innate protection by antiproteases. J Exp Med 1995; 182:1537-44.
19. Heymann PW, Chapman MD, Aalberse RC, Fox JW, Platts-Mills TAE. Antigenic and structural analysis of group II allergens (Der f II and Der p II) from house dust mites (Dermatophagoides spp). J Allergy Clin Immunol 1989; 83:1055-67.
20. Lind P. Purification and partial characterization of two major allergens from the house dust mite Dermatophagoides pteronyssinus. J Allergy Clin Immunol 1985; 76:753-61.
21. Lombardero M, Heymann PW, Platts MT, Fox JW, Chapman MD. Conformational stability of B cell epitopes on group I and group II Dermatophagoides spp. allergens. Effect of thermal and chemical denaturation on the binding of murine IgG and human IgE antibodies. J Immunol 1990; 144:1353-60.
22. Yuuki T, Okumura Y, Ando T et al. Cloning and sequencing of cDNAs corresponding to major mite allergen Der f II. Jpn J Allergol 1990; 39:557-61.
23. Chua KY, Doyle CR, Simpson RJ et al. Isolation of cDNA coding for the major mite allergen Der p II by IgE plaque immunoassay. Int Arch Allergy Appl Immunol 1990; 91:118-23.
24. Trudinger M, Chua KY, Thomas WR. cDNA encoding the major mite allergen Der f II. Clin Exp Allergy 1991; 21:33-7.
25. Stewart GA, Ward LD, Simpson RJ, Thompson PJ. The group III allergen from the house dust mite Dermatophagoides pteronyssinus is a trypsin-like enzyme. Immunology 1992; 75:29-35.
26. Smith W-A, Chua K-Y, Kuo MC, Rogers BL, Thomas WR. Cloning and sequencing of the Dermatophagoides pteronyssinus group III allergen, Der p III. Clin Exp Allergy 1994; 24:220-8.
27. Lake FR, Ward LD, Simpson RJ, Thompson PJ, Stewart GA. House dust mite derived amylase: allergenicity and physicochemical characterisation. J Allergy Clin Immunol 1991; 87:1035-42.
28. Tovey ER, Johnson MC, Roche AL, Cabon GS, Saldo BA. 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; 170:1457-62. Published erratum appears in J Exp Med 1990; 171:1387.
29. Yasueda H, Mita H, Akiyama K et al. Allergens from Dermatophagoides mites with chymotryptic activity. Clin Exp Allergy 1993; 23:384-90.
30. Shen H-D, Chua K-Y, Lin K-L, Hsieh K-H, Thomas WR. 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.
31. 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: 521-8.
32. King CM, Simpson RJ, Thompson PJ, Stewart GA. Characterization of a novel serine protease allergen from the dust mite, Dermatophagoides pteronyssinus. J Allergy Clin Immunology. In press.
33. Aki T, Fujikawa A, Wada T et al. Cloning and expression of cDNA coding for a new allergen from the house dust mite, Dermatophagoides farinae: homology with human heat shock cognate proteins in the heat shock protein 70 family. J Biochem 1994; 115:435-40.
34. Stewart GA, Simpson RJ, Moritz RL, Thomas WR, Turner KJ. Physiochemical characterization of allergens Der p I (Dpt 12), Dpt 22 and Dpt 36 from the house dust mite. In de Weck Al, Todt A, eds. International Workshop Proceedings, Mite Allergy, A World Wide Problem. Brussels: The UCB Institute for Allergy, 1988; 35-8.
35. Holt PG. Macrophage and dendritic cell populations in the respiratory tract. In: Holgate ST, ed. Immunopharmacology of the respiratory system. London: Academic Press, 1995: 1-12.
36. Bienenstock J, Johnston N, Perey DYE. Bronchial lymphoid tissue. 1. Morphologic characteristics. Lab Invest 1973; 28:686-92.
37. Bienenstock J, Johnston N, Perey DYE. Bronchial lymphoid tissue. 2. Functional characteristics. Lab Invest 1973; 28:693-8.
38. Pabst R, Gehrke I. Is the bronchus-associated lymphoid tissue (BALT) an integral structure of the lung in normal mammals, including humans? Am J Respir Cell Mol Biol 1990; 3:131-5.
39. Tschernig T, Kleeman WJ, Pabst R. Bronchus-associated lymphoid tissue (BALT) in the lungs of children who had died from sudden infant death syndrome and other causes. Thorax 1995; 50:658-60.
40. Delventhal S, Brandis A, Ostertag H, Pabst R. Low incidence of bronchus-associated lymphoid tissue (BALT) in chronically inflamed lungs. Virchows Archiv B, Cell Pathol incl Mol Pathol 1992; 62:271-4.
41. Sato A, Chida K, Iwata M, Hayakawa H. Study of bronchus-associated lymphoid tissue in patients with diffuse panbronchiolitis. Am Rev Respir Dis 1992; 146: 473-8.
42. Bienenstock J, Befus D. Gut- and bronchus-associated lymphoid tissue. Am J Anat 1984; 170:437-45.
43. Sandström T, Bjermer L, Rylander R. Lipopolysaccharide (LPS) inhalation in healthy subjects increases neutrophils, lymphocytes and fibronectin levels in bronchoalveolar lavage fluid. Eur Respir J 1992; 5:992-6.
44. Gerblich AA, Campbell AE, Schuyler MR. Changes in T-lymphocytes subpopulations after antigenic bronchial provocation in asthmatics. N Eng J Med 1984; 310:1349-52.
45. Herbert CA, Edwards D, Boot JR, Robinson C. In vitro modulation of the eosinophil-dependent enhancement of the permeability of the bronchial mucosa. Br J Pharmacol 1991; 104:391-8.
46. Maruo K, Akaike T, Inada Y et al. Effect of microbial and mite proteases on low and high molecular weight kininogens. J Biol Chem 1993; 268:17711-15.
47. Takahashi K, Aoki T, Kohmoto S et al. Activation of kallikrein system in human plasma with purified serine protease from Dermatophagoides farinae. Int Arch Allergy Appl Immunol 1990; 91:80-5.
48. Maeda H, Molla A. Pathogenic potentials of bacterial proteases. Clin Chim Acta 1989; 185:357-68.
49. Schulz O, Laing P, Sewell H, Shakib F. Der p I, a major allergen of the house dust mite, proteolytically cleaves the low-affinity receptor for human IgE (CD23). Eur J Immunol 1995; 25: 3191-4.
50. Overton J. The fate of desmosomes in trypsinized tissue. J Exp Zool 1968; 168:203-14.
51. Parrish EP, Marston JE, Mattey DL et al. Size heterogeneity, phosphorylation and transmembrane organization of desmosomal glycoproteins 2 and 3 (desmocollins) in MDCK cells. J Cell Sci 1990; 96:239-48.
52. Kawamura K, Watanabe K, Suzuki T et al. cDNA cloning and expression of a novel human desmocollin. J Biol Chem 1994; 269:26295-302.
53. Cantin AM, North SL, Hubbard RC, Crystal RG. Normal alveolar epithelial lining fluid contains high levels of glutathione. J Appl Physiol 1987; 163:152-7.
54. Scobie G, Ravindran V, Deam SM, Thomas M, Sreeedharan SK, Brocklehurst K, Kalsheker N. Expression cloning of a dust mite cysteine proteinase, Der p 1, a major allergen associated with asthma and hypersensitivity reactions. Biochem Soc Trans 1994; 22:448S.
55. Higgins JA, Thorpe CJ, Hayball JD, O'Hehir RE, Lamb JR. Overlapping T-cell epitopes in the group I allergen of Dermatophagoides species restricted by HLA-DP and HLA-DR class II molecules. J Allergy Clin Immunol 1994; 93:891-9.
56. Overington JP, Johnson MS, Sali A, Blundell TL. Tertiary structural constraints on protein evolutionary diversity: templates, key residues and structure prediction. Proc R. Soc London 1990; B241:132-45.
57. Pepys J, Hargreave F, Longbottom L, Faux J. Allergic reaction of the lungs to enzyme of Bacillus subtilis. Lancet 1969; i:1181-4.
58. Baur X, Fruhmann G. Allergic reaction, including asthma, to the pineapple protease bromelain following occupational exposure. Clin Allergy 1979; 9:443-50.