Peptidase 1 (mite)

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Peptidase 1 (mite)
Der P-1-3F5V.png
Crystal structure of Der p 1 allergen [1] from pdb entry 3F5V ​
Identifiers
EC no. 3.4.22.65
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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]

Contents

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

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

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 an 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

Peptidase 1
Identifiers
Organism Dermatophagoides pteronyssinus
SymbolDERP1
PDB 1XKG
UniProt P08176
Search for
Structures Swiss-model
Domains InterPro

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 be able to inhibit Der p 1. [3]

Der f 1

Peptidase 1
Identifiers
Organism Dermatophagoides farinae
SymbolDERF1
PDB 3RVV
UniProt P16311
Search for
Structures Swiss-model
Domains InterPro

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

Peptidase 1
Identifiers
Organism Euroglyphus maynei
SymbolEURM1
UniProt P25780
Search for
Structures Swiss-model
Domains InterPro

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

Peptidase 1
Identifiers
Organism Psoroptes ovis
SymbolPSOO1
UniProt Q1EIQ3
Search for
Structures Swiss-model
Domains InterPro

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

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 enzymes 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

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

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

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

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]

Related Research Articles

<span class="mw-page-title-main">Protease</span> Enzyme that cleaves other proteins into smaller peptides

A protease is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in numerous biological pathways, including digestion of ingested proteins, protein catabolism, and cell signaling.

<span class="mw-page-title-main">House dust mite</span> Common name for several species of mite

House dust mites are various species of acariform mites belonging to the family Pyroglyphidae that are found in association with dust in dwellings. They are known for causing allergies.

In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.

<span class="mw-page-title-main">Serine protease</span> Class of enzymes

Serine proteases are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.

A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis.

<span class="mw-page-title-main">Papain</span> Widely used enzyme extracted from papayas

Papain, also known as papaya proteinase I, is a cysteine protease enzyme present in papaya and mountain papaya. It is the namesake member of the papain-like protease family.

<span class="mw-page-title-main">Catalytic triad</span> Set of three coordinated amino acids

A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes. An acid-base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine or even selenocysteine. The 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence.

<span class="mw-page-title-main">Cysteine protease</span> Class of enzymes

Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad.

<span class="mw-page-title-main">Aspartic protease</span>

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<span class="mw-page-title-main">Actinidain</span> Class of enzymes

Actinidain is a type of cysteine protease enzyme found in fruits including kiwifruit, pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases.

<span class="mw-page-title-main">Cathepsin L1</span> Protein-coding gene in the species Homo sapiens

Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal cysteine protease that plays a major role in intracellular protein catabolism.

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<span class="mw-page-title-main">Pyroglyphidae</span> Family of mites

Pyroglyphidae is a family of non-parasitic mites. It includes the house dust mite that live in human dwellings, many species that live in the burrows and nests of other animals, and some pests of dried products stored in humid conditions.

<span class="mw-page-title-main">E-64</span> Chemical compound

E-64 is an epoxide which can irreversibly inhibit a wide range of cysteine peptidases.

<span class="mw-page-title-main">ML domain</span>

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<span class="mw-page-title-main">Zingibain</span>

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Aspergillus penicillioides is a species of fungus in the genus Aspergillus, and is among the most xerophilic fungi.

Oral mite anaphylaxis (OMA), also known as pancake syndrome, is a disease in which a person gets symptoms after eating food contaminated with particular mites. The disease name comes from reports of people becoming ill after eating pancakes made from contaminated wheat or corn (maize) flour.

<span class="mw-page-title-main">Dust mite allergy</span> Medical condition

Dust mite allergy, also known as house dust allergy, is a sensitization and allergic reaction to the droppings of house dust mites. The allergy is common and can trigger allergic reactions such as asthma, eczema or itching. The mite's gut contains potent digestive enzymes that persist in their feces and are major inducers of allergic reactions such as wheezing. The mite's exoskeleton can also contribute to allergic reactions. Unlike scabies mites or skin follicle mites, house dust mites do not burrow under the skin and are not parasitic.

<span class="mw-page-title-main">Papain-like protease</span>

Papain-like proteases are a large protein family of cysteine protease enzymes that share structural and enzymatic properties with the group's namesake member, papain. They are found in all domains of life. In animals, the group is often known as cysteine cathepsins or, in older literature, lysosomal peptidases. In the MEROPS protease enzyme classification system, papain-like proteases form Clan CA. Papain-like proteases share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a nucleophile.

References

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  2. ↑ Meighan, P.; Pirzad, R. (2004). "Mite endopeptidase 1". In Barrett, A.J.; Rawlings, N.D.; Woessner, J.F. (eds.). Handbook of Proteolytic Enzymes (2nd ed.). London: Elsevier. pp. 1187–1189.
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  5. ↑ "Information on EC 3.4.22.65 - peptidase 1 (mite)". Enzyme Database - BRENDA. January 2015. Retrieved 11 April 2015.
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  15. 1 2 3 4 5 6 7 8 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 (BBA) - General Subjects. 1840 (3): 1117–24. doi:10.1016/j.bbagen.2013.11.017. hdl: 2268/163997 . PMID   24291687.
  16. 1 2 3 4 Vrtala, S; Huber, H; Thomas, WR (1 March 2014). "Recombinant house dust mite allergens". Methods. 66 (1): 67–74. doi:10.1016/j.ymeth.2013.07.034. PMC   4582397 . PMID   23911838.
  17. 1 2 3 4 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.1398-9995.2007.01492.x. PMID   17919146. S2CID   11144482.
  18. 1 2 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): e114636. doi: 10.1371/journal.pone.0114636 . PMC   4262422 . PMID   25494056.
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  22. 1 2 "DERF1 - Peptidase 1 precursor - Dermatophagoides farinae (American house dust mite)". UniProt. Retrieved 12 April 2015.
  23. 1 2 3 "Peptidase 1 precursor - Psoroptes ovis (Sheep scab mite)". UniProt. Retrieved 12 April 2015.
  24. 1 2 3 4 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 (1): 83–9. doi:10.1017/S0031182006001235. PMID   16978441. S2CID   46361359.
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  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. PMC   408401 . PMID   10393706.
  27. 1 2 Schulz, O.; Sewell, H.F.; 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 (2): 271–275. doi:10.1084/jem.187.2.271. PMC   2212095 . PMID   9432986.
  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. doi:10.1159/000235405. PMID   1937901.
  29. 1 2 3 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. 192 (10): 4867–75. doi:10.4049/jimmunol.1400064. PMC   4582415 . 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.; 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 (4): 944–952. doi:10.1016/j.bbrc.2005.01.051. PMID   15707969.
  32. ↑ Prester, Ljerka (April 2012). "Arthropod allergens in urban homes". Arhiv Za Higijenu Rada I Toksikologiju. 63 (Supplement-1): 47–51. doi: 10.2478/10004-1254-63-2012-2125 . PMID   22548852.
  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. S2CID   20947793.
  34. 1 2 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. doi:10.1046/j.1365-2222.1997.840895.x. PMID   9291282.
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