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Peptidase 1 (mite)
Crystal structure of Der p 1 allergen[1] from pdb entry 3F5V​
Identifiers
EC no.3.4.22.65
Databases
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BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
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Peptidase 1 (mite) (EC 3.4.22.65), also known as endopeptidase 1 (mite), is an enzyme found in various species of mites.[2][3] This enzyme exhibits cysteine protease activity with broad endopeptidase specificity.[4]

The various forms of peptidase 1 pertaining to individual mite species comprise the group 1 mite allergens.[5] Following the naming conventions of allergens, these peptidase 1 variants include Der p 1 of the European house dust mite Dermatophagoides pteronyssinus;[6] Der f 1 of the American house dust mite Dermatophagoides farinae;[1] Eur m 1 of the Mayne's house dust mite Euroglyphus maynei;[7] and Pso o 1 of the sheep scab mite Psoroptes ovis.[8] The group 1 mite allergens, especially Der p 1 and Der f 1, are major sources of house dust mite (HDM) allergies in temperate climates.[6][9][10]

History

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The first allergen to be purified and characterized was Der p 1, in a 1980 study by Martin D. Chapman and Thomas Platts-Mills.[10][11] By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that of actinidin and papain.[12] In the mid-1990s, Hewitt et al., Shakib et al., and King et al. proposed methods of Der p 1 promoting allergic responses through its protease activities.[12]

In 2002, Pso o 1 was identified and characterized by Lee et al., who determined its amino acid sequence and found it to be homologous to the other group 1 mite allergens.[10]

In 2009, Der f 1 was the first observed instance of a natural allergen in the form of a monomer.[1][13]

Structure

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Peptidase 1 is a cysteine protease belonging to the C1 protein family, with a structure similar to that of papain.[4][13][14][15][16] Initially, peptidase 1 is synthesized as a inactive zymogen, which is activated by enzymatic cleavage.[10][12][15]

Structurally, peptidase 1 enzymes are nearly identical; for example, a two-domain structure and an approximate 81% sequence identity are retained between Der p 1 and Der f 1.[1][12][14] Due to the conserved structures, a single allergen may be used as a model in the development of drugs intended to target group 1 mite allergens, with Der p 1 usually considered the archetype.[14][17] Specificity and cross-reactivity between multiple group 1 allergens is thought to stem from the differences and homologies in structure, particularly regarding the positions of epitopes.[1][18]

Der p 1

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Peptidase 1
Identifiers
OrganismDermatophagoides pteronyssinus
SymbolDERP1
PDB1XKG
UniProtP08176
Search for
StructuresSwiss-model
DomainsInterPro

Der p 1 is a 25 kDa glycoprotein composed of a 222-amino acid sequence encoded by the gene DERP1.[4][19][20] Der p 1 is synthesized as an inactive 80-amino acid protein precursor known as proDer p 1, which is then cleaved and activated by mature Der p 1.[12][15][17]

Due to its cysteine protease structure, Der p 1 may be irreversibly inhibited by E-64 or iodoacetamide, which bind to the cysteine active site and block substrate access.[12][14][21] The major kiwifruit cysteine proteinase inhibitor KCPI1 has also been shown to able to inhibit Der p 1.[3]

Der f 1

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Peptidase 1
Identifiers
OrganismDermatophagoides farinae
SymbolDERF1
PDB3RVV
UniProtP16311
Search for
StructuresSwiss-model
DomainsInterPro

Der f 1 is a 25 kDa protease composed of a 223-amino acid sequence.[20][22] In its inactive precursor state, proDer f 1 has an 80-amino acid prodomain.[17][22]

Unlike Der p 1, Der f 1 lacks binding sites for metals such as magnesium and calcium.[13] Through secretion by Pichia pastoris, Der f 1 is easier to produce in a recombinant form than Der p 1 due to the removal of an N-glycosylation site.[16] In solution or crystal, Der f 1 is a monomer.[1][13] Der f 1 has been shown to express polymorphism, with at least two haplotypes observed in different regions.[18]

Der f 1 can be inhibited by chestnut cystatin, which is thought to stem from the presence of the amino acid Gln152 (instead of Der p 1's Arg151) near the enzyme's active site.[1][3]

Eur m 1

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Peptidase 1
Identifiers
OrganismEuroglyphus maynei
SymbolEURM1
UniProtP25780
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StructuresSwiss-model
DomainsInterPro

Eur m 1 is composed of a 223-amino acid sequence.[7] In its inactive precursor state, Eur m 1 has an 80-amino acid prodomain.[7][17]

Eur m 1 shares 88% identity with Der f 1, which has led to the proposal that Euroglyphus maynei may be more closely related to Dermatophagoides farinae than Dermatophagoides pteronyssinus.[9]

Pso o 1

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Peptidase 1
Identifiers
OrganismPsoroptes ovis
SymbolPSOO1
UniProtQ1EIQ3
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StructuresSwiss-model
DomainsInterPro

Pso o 1 is a 36 kDa protease composed of a 223-amino acid sequence sequence.[10][23] Pso o 1's precursor form is thought to be comprised of an 81-amino acid sequence.[23]

Compared to other forms of peptidase 1, Pso o 1 shares 54% identity with Der f 1, 53% identity with Der p 1, and 53% identity with Eur m 1.[10] A number of amino acid sequences from other peptidase 1 enzymes are shown to be conserved in Pso o 1, including enzymatic amino acids, a N-glycosylation site, and the Der p 1 epitope Leu147-Gln160.[10]

Biological function

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Peptidase 1 enzymes are found in the fecal pellets of mites. Some of these enzymes have also been located in the mite gut, suggesting that these enyzmes play a role in digestion.[8][15][24] As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the activation of other allergens.[14][15]

Mite fecal pellets carrying peptidase 1 enter the respiratory tract through inhalation.[25] There, as group 1 mite allergens, peptidase 1 enzymes promote allergic sensitization, usually either by causing epithelial leakage in the respiratory tract through cleavage of the cells' tight junctions or by triggering innate chemokine release through activation of signal transduction pathways.[12][14][26]

Der p 1

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Der p 1 is located in the mid-gut and fecal pellets of the European house dust mite Dermatophagoides pteronyssinus.[15][27][28] It has been suggested that the mite's gastrointestinal cells produce Der p 1.[24] In the mite, Der p 1 is responsible for the activation of zymogens located in the mite digestive tract, including itself and the serine proteases Der p 3, Der p 6, and Der p 9, which are then secreted as potent allergens and thereby increase the pathogenesis of the allergy.[15]

Der p 1 is a major source of HDM allergies, triggering immunoglobulin E binding levels of 80-90% and, combined with the group 2 allergen Der p 2, accounting for over 50% of all HDM-related IgE binding.[15][16][25][27][29] CD23 and CD25 are targets of Der p 1, which cleaves these receptors from the surfaces of active B cells and T cells, respectively, and thereby triggers the release of more IgE.[12][21] Because of the prevalence of Der p 1 in mite allergies, developers of HDM allergy vaccines consider it necessary to factor in Der p 1.[29] As a result, Der p 1 is a major component of mite allergen crude extracts and is frequently used as the basis of numerous hypoallergenic derivatives created in the refinement of specific immunotherapy.[16][29] Even by inhibiting only Der p 1, allergic responses may be noticeably alleviated.[14]

Der f 1

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Der f 1 is found in the fecal pellets of the American house dust mite Dermatophagoides farinae.[1] Der f 1 is considered a major mite allergen and has been shown to promote allergic reactions in the lungs and skin.[1][30][31] Der f 1 shows over 80% cross-reactivity with Der p 1.[32] Like Der p 1, Der f 1 functions by cleaving CD23 to trigger an IgE response.[20] Der f 1 also triggers an immune response through eosinophil degranulation.[33]

Eur m 1

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Eur m 1 is secreted by the Mayne's house dust mite Euroglyphus maynei.[7] Eur m 1 provokes allergic responses from T cells.[34] Der p 1 and Der f 1 show only low levels of cross-reactivity with Eur m 1.[34]

Pso o 1

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Pso o 1 is found in the gut and fecal pellets of the sheep scab mite Psoroptes ovis.[8][24] Psoroptic mange in sheep is promoted by the cysteine protease activity of Pso o 1, which targets connective tissues and the molecules of the extracellular matrix.[24] Although Psoroptes belongs to a different order from the house dust mite species, Pso o 1 is classified as a group 1 mite allergen alongside Der p 1, Der f 1, and Eur m 1.[10][23]

References

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  1. ^ a b c d e f g h i Chruszcz M1, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W, Pomés A. (2009). "Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding". J. Mol. Biol. 386 (2): 520-30. doi:10.1016/j.jmb.2008.12.049. PMID 19136006.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: numeric names: authors list (link)
  2. ^ Meighan, P. and Pirzad, R. (2004). "Mite endopeptidase 1". In Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (ed.). Handbook of Proteolytic Enzymes (2nd ed.). London: Elsevier. pp. 1187–1189.{{cite book}}: CS1 maint: multiple names: authors list (link)
  3. ^ a b c Rassam, M; Laing, WA (January 2004). "Purification and characterization of phytocystatins from kiwifruit cortex and seeds". PHYTOCHEMISTRY. 65 (1): 19–30. doi:10.1016/j.phytochem.2003.09.019. PMID 14697268. {{cite journal}}: |access-date= requires |url= (help)
  4. ^ a b c Harris, J., Mason, D.E., Li, J., Burdick, K.W., Backes, B.J., Chen, T., Shipway, A., Van Heeke, G., Gough, L., Ghaemmaghami, A., Shakib, F., Debaene, F. and Winssinger, N. (2004). "Activity profile of dust mite allergen extract using substrate libraries and functional proteomic microarrays". Chem. Biol. 11: 1361–1372. doi:10.1016/j.chembiol.2004.08.008. PMID 15489163.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ "Information on EC 3.4.22.65 - peptidase 1 (mite)". Enzyme Database - BRENDA. January 2015. Retrieved 11 April 2015.
  6. ^ a b Schulz, O., Sewell, H.F. and Shakib, F. (1998). "A sensitive fluorescent assay for measuring the cysteine protease activity of Der p 1, a major allergen from the dust mite Dermatophagoides pteronyssinus". Mol. Pathol. 51: 222–224. doi:10.1136/mp.51.4.222. PMID 9893750.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  7. ^ a b c d "EURM1 - Peptidase 1 precursor - Euroglyphus maynei (Mayne's house dust mite)". UniProt. Retrieved 27 March 2015.
  8. ^ a b c McNair, Carol M.; Billingsley, Peter F.; Nisbet, Alasdair J.; Knox, Dave P. (27 October 2009). "Feeding-associated gene expression in sheep scab mites (Psoroptes ovis)". Veterinary Research. 41 (2): 16. doi:10.1051/vetres/2009064. {{cite journal}}: |access-date= requires |url= (help)
  9. ^ a b Cui, Y.; Zhou, P.; Peng, J.; Peng, M.; Zhou, Y.; Lin, Y.; Liu, L. (May 2008). "Cloning, sequence analysis, and expression of cDNA coding for the major house dust mite allergen, Der f 1, in Escherichia coli". BRAZILIAN JOURNAL OF MEDICAL AND BIOLOGICAL RESEARCH. 41 (5): 380–388. doi:10.1590/S0100-879X2008000500006. PMID 18545812. {{cite journal}}: |access-date= requires |url= (help)
  10. ^ a b c d e f g h Lee, AJ; Machell, J; Van Den Broek, AH; Nisbet, AJ; Miller, HR; Isaac, RE; Huntley, JF (August 2002). "Identification of an antigen from the sheep scab mite, Psoroptes ovis, homologous with house dust mite group I allergens". Parasite immunology. 24 (8): 413–22. PMID 12406195.
  11. ^ Chapman, MD; Platts-Mills, TA (August 1980). "Purification and characterization of the major allergen from Dermatophagoides pteronyssinus-antigen P1". Journal of immunology (Baltimore, Md. : 1950). 125 (2): 587–92. PMID 6771329.
  12. ^ a b c d e f g h Chapman, Martin D.; Wuenschmann, Sabina; Pomes, Anna (September 2007). "Proteases as Th2 adjuvants". CURRENT ALLERGY AND ASTHMA REPORTS. 7 (5): 363–367. doi:10.1007/s11882-007-0055-6. PMID 17697645. {{cite journal}}: |access-date= requires |url= (help)
  13. ^ a b c d Thomas, WR; Hales, BJ; Smith, WA (July 2010). "House dust mite allergens in asthma and allergy". Trends in molecular medicine. 16 (7): 321–8. PMID 20605742.
  14. ^ a b c d e f g Newton, Gary K.; Perrior, Trevor R.; Jenkins, Kerry; Major, Meriel R.; Key, Rebekah E.; Stewart, Mark R.; Firth-Clark, Stuart; Lloyd, Steven M.; Zhang, Jihui; Francis-Newton, Nicola J.; Richardson, Jonathan P.; Chen, Jie; Lai, Pei; Garrod, David R.; Robinson, Clive (26 November 2014). "The Discovery of Potent, Selective, and Reversible Inhibitors of the House Dust Mite Peptidase Allergen Der p 1: An Innovative Approach to the Treatment of Allergic Asthma". Journal of Medicinal Chemistry. 57 (22): 9447–9462. doi:10.1021/jm501102h.
  15. ^ a b c d e f g h Herman, J; Thelen, N; Smargiasso, N; Mailleux, AC; Luxen, A; Cloes, M; De Pauw, E; Chevigné, A; Galleni, M; Dumez, ME (March 2014). "Der p 1 is the primary activator of Der p 3, Der p 6 and Der p 9 the proteolytic allergens produced by the house dust mite Dermatophagoides pteronyssinus". Biochimica et biophysica acta. 1840 (3): 1117–24. PMID 24291687.
  16. ^ a b c d Vrtala, S; Huber, H; Thomas, WR (1 March 2014). "Recombinant house dust mite allergens". Methods (San Diego, Calif.). 66 (1): 67–74. PMID 23911838.
  17. ^ a b c d Zhang, J.; Hamilton, J. M.; Garrod, D. R.; Robinson, C. (November 2007). "Interactions between mature Der p 1 and its free prodomain indicate membership of a new family of C1 peptidases". ALLERGY. 62 (11): 1302–1309. doi:10.1111/j.1397-9995.2007.01492.x. PMID 17919146. {{cite journal}}: |access-date= requires |url= (help)
  18. ^ a b Shafique, Rubaba Hamid; Klimov, Pavel B.; Inam, Muhammad; Chaudhary, Farhana Riaz; OConnor, Barry M. (10 December 2014). "Group 1 Allergen Genes in Two Species of House Dust Mites, Dermatophagoides farinae and D-pteronyssinus (Acari: Pyroglyphidae): Direct Sequencing, Characterization and Polymorphism". PLOS ONE. 9 (12). doi:10.1371/journal.pone.0114636. {{cite journal}}: |access-date= requires |url= (help)CS1 maint: unflagged free DOI (link)
  19. ^ "Dermatophagoides pteronyssinus antigen p 1". US National Library of Medicine Medical Subject Headings. Retrieved 3 April 2015.
  20. ^ a b c Cruz, Luz Mary; Lopez-Malpica, Fernando; Diaz, Ana Maria (June 2008). "Analysis of cross-reactivity between group 1 allergens from mites". PUERTO RICO HEALTH SCIENCES JOURNAL. 27 (2): 163–170. {{cite journal}}: |access-date= requires |url= (help)
  21. ^ a b Thomas, WR; Hales, BJ; Smith, WA (September 2005). "Structural biology of allergens". CURRENT ALLERGY AND ASTHMA REPORTS. 5 (5): 388–393. doi:10.1007/s11882-005-0012-1. PMID 16091212. {{cite journal}}: |access-date= requires |url= (help)
  22. ^ a b "DERF1 - Peptidase 1 precursor - Dermatophagoides farinae (American house dust mite)". UniProt. Retrieved 12 April 2015.
  23. ^ a b c "Peptidase 1 precursor - Psoroptes ovis (Sheep scab mite)". UniProt. Retrieved 12 April 2015.
  24. ^ a b c d NISBET, A. J.; MacKELLAR, A.; McLEAN, K.; BRENNAN, G. P.; HUNTLEY, J. F. (18 September 2006). "Eukaryotic expression of recombinant Pso o 1, an allergen from Psoroptes ovis, and its localization in the mite". Parasitology. 134 (01): 83. doi:10.1017/S0031182006001235. {{cite journal}}: |access-date= requires |url= (help)
  25. ^ a b Kalsheker, N.A., Deam, S., Chambers, L., Sreedharan, S., Brocklehurst, K. and Lomas, D.A. (1996). "The house dust mite allergen Der p1 catalytically inactivates α1-antitrypsin by specific reactive centre loop cleavage: a mechanism that promotes airway inflammation and asthma". Biochem. Biophys. Res. Commun. 221: 59–61. doi:10.1006/bbrc.1996.0544. PMID 8660343.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  26. ^ Wan, Hong; Winton, Helen L.; Soeller, Christian; Tovey, Euan R.; Gruenert, Dieter C.; Thompson, Philip J.; Stewart, Geoffrey A.; Taylor, Graham W.; Garrod, David R.; Cannell, Mark B.; Robinson, Clive (1 July 1999). "Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions". Journal of Clinical Investigation. 104 (1): 123–133. doi:10.1172/JCI5844.
  27. ^ a b Schulz, O., Sewell, H.F. and Shakib, F. (1998). "Proteolytic cleavage of CD25, the α subunit of the human T cell interleukin 2 receptor, by Der p 1, a major mite allergen with cysteine protease activity". J. Exp. Med. 187: 271–275. doi:10.1084/jem.187.2.271. PMID 9432986.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  28. ^ Thomas, B; Heap, P; Carswell, F (1991). "Ultrastructural localization of the allergen Der p I in the gut of the house dust mite Dermatophagoides pteronyssinus". International archives of allergy and applied immunology. 94 (1–4): 365–7. PMID 1937901.
  29. ^ a b c Banerjee, S; Weber, M; Blatt, K; Swoboda, I; Focke-Tejkl, M; Valent, P; Valenta, R; Vrtala, S (15 May 2014). "Conversion of Der p 23, a new major house dust mite allergen, into a hypoallergenic vaccine". Journal of immunology (Baltimore, Md. : 1950). 192 (10): 4867–75. PMID 24733847.
  30. ^ "Dermatophagoides farinae antigen f 1". US National Library of Medicine Medical Subject Headings. Retrieved 3 April 2015.
  31. ^ Takai, T., Kato, T., Sakata, Y., Yasueda, H., Izuhara, K., Okumura, K. and Ogawa, H. (2005). "Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine protease activity". Biochem. Biophys. Res. Commun. 328: 944–952. doi:10.1016/j.bbrc.2005.01.051. PMID 15707969.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  32. ^ Prester, Ljerka (April 2012). "ARTHROPOD ALLERGENS IN URBAN HOMES". ARHIV ZA HIGIJENU RADA I TOKSIKOLOGIJU-ARCHIVES OF INDUSTRIAL HYGIENE AND TOXICOLOGY. 63: 47–51. doi:10.2478/10004-1254-63-2012-2125. PMID 22548852. {{cite journal}}: |access-date= requires |url= (help)
  33. ^ Kato, T.; Takai, T.; Fujimura, T.; Matsuoka, H.; Ogawa, T.; Murayama, K.; Ishii, A.; Ikeda, S.; Okumura, K.; Ogawa, H. (September 2009). "Mite serine protease activates protease-activated receptor-2 and induces cytokine release in human keratinocytes". ALLERGY. 64 (9): 1366–1374. doi:10.1111/j.1398-9995.2009.02023.x. PMID 19416145. {{cite journal}}: |access-date= requires |url= (help)
  34. ^ a b Hales, BJ; Thomas, WR (August 1997). "T-cell sensitization to epitopes from the house dust mites Dermatophagoides pteronyssinus and Euroglyphus maynei". CLINICAL AND EXPERIMENTAL ALLERGY. 27 (8): 868–875. PMID 9291282. {{cite journal}}: |access-date= requires |url= (help)
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