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Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding.

Chruszcz M, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W, Pomés A
J Mol Biol 386 520-30 (2009)
Cited: 56 times
EuropePMC logo PMID: 19136006

Abstract

The group 1 mite allergens Der f 1 and Der p 1 are potent allergens excreted by Dermatophagoides farinae and Dermatophagoides pteronyssinus, respectively. The human immunoglobulin E antibody responses to the group 1 allergens show more cross-reactivity than the murine immunoglobulin G antibody responses, which are largely species specific. Here, we report the crystal structure of the mature form of Der f 1, which was isolated from its natural source, and a new high-resolution structure of mature recombinant Der p 1. Unlike Der p 1, Der f 1 is monomeric both in the crystalline state and in solution. Moreover, no metal binding is observed in the structure of Der f 1 despite the fact that all amino acids involved in Ca(2+) binding in Der p 1 are completely conserved in Der f 1. Although Der p 1 and Der f 1 share an extensive sequence identity, comparison of the crystal structures of both allergens revealed structural features that could explain the differences in murine IgG and human IgE antibody responses to these allergens. There are structural differences between Der f 1 and Der p 1 that are unevenly distributed on the allergens' surfaces. This uneven spatial arrangement of conserved versus altered residues could explain both the specificity and cross-reactivity of antibodies against Der f 1 and Der p 1.

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  1. Relevant B cell epitopes in allergic disease. Pomés A. Int Arch Allergy Immunol 152 1-11 (2010)
  2. Nanomaterials in the Context of Type 2 Immune Responses-Fears and Potentials. Himly M, Mills-Goodlet R, Geppert M, Duschl A. Front Immunol 8 471 (2017)

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  1. Molecular determinants for antibody binding on group 1 house dust mite allergens. Chruszcz M, Pomés A, Glesner J, Vailes LD, Osinski T, Porebski PJ, Majorek KA, Heymann PW, Platts-Mills TA, Minor W, Chapman MD. J Biol Chem 287 7388-7398 (2012)
  2. Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding. Chruszcz M, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W, Pomés A. J Mol Biol 386 520-530 (2009)
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  7. 100 Years later: Celebrating the contributions of x-ray crystallography to allergy and clinical immunology. Pomés A, Chruszcz M, Gustchina A, Minor W, Mueller GA, Pedersen LC, Wlodawer A, Chapman MD. J Allergy Clin Immunol 136 29-37.e10 (2015)
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  13. Allergen Delivery Inhibitors: A Rationale for Targeting Sentinel Innate Immune Signaling of Group 1 House Dust Mite Allergens through Structure-Based Protease Inhibitor Design. Zhang J, Chen J, Newton GK, Perrior TR, Robinson C. Mol Pharmacol 94 1007-1030 (2018)
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  2. Editorial Pro: The evidence for a causal role of dust mites in asthma. Platts-Mills TA, Erwin EA, Heymann PW, Woodfolk JA. Am J Respir Crit Care Med 180 109-13; discussion 120-1 (2009)
  3. Recombinant house dust mite allergens. Vrtala S, Huber H, Thomas WR. Methods 66 67-74 (2014)
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  7. MHC class II-restricted presentation of the major house dust mite allergen Der p 1 Is GILT-dependent: implications for allergic asthma. West LC, Grotzke JE, Cresswell P. PLoS One 8 e51343 (2013)
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  11. Sequence polymorphisms of Der f 1, Der p 1, Der f 2 and Der p 2 from Korean house dust mite isolates. Jeong KY, Lee IY, Yong TS, Lee JH, Kim EJ, Lee JS, Hong CS, Park JW. Exp Appl Acarol 58 35-42 (2012)
  12. Der f 34, a Novel Major House Dust Mite Allergen Belonging to a Highly Conserved Rid/YjgF/YER057c/UK114 Family of Imine Deaminases. ElRamlawy KG, Fujimura T, Baba K, Kim JW, Kawamoto C, Isobe T, Abe T, Hodge-Hanson K, Downs DM, Refaat IH, Beshr Al-Azhary D, Aki T, Asaoku Y, Hayashi T, Katsutani T, Tsuboi S, Ono K, Kawamoto S. J Biol Chem 291 21607-21615 (2016)
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  21. A genomic analysis and transcriptomic atlas of gene expression in Psoroptes ovis reveals feeding- and stage-specific patterns of allergen expression. Burgess STG, Marr EJ, Bartley K, Nunn FG, Down RE, Weaver RJ, Prickett JC, Dunn J, Rombauts S, Van Leeuwen T, Van de Peer Y, Nisbet AJ. BMC Genomics 20 756 (2019)
  22. Der f 35: An MD-2-like house dust mite allergen that cross-reacts with Der f 2 and Pso o 2. Fujimura T, Aki T, Isobe T, Matsuoka A, Hayashi T, Ono K, Kawamoto S. Allergy 72 1728-1736 (2017)
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  27. Structure and IgE Cross-Reactivity among Cashew, Pistachio, Walnut, and Peanut Vicilin-Buried Peptides. Foo ACY, Nesbit JB, Gipson SAY, DeRose EF, Cheng H, Hurlburt BK, Kulis MD, Kim EH, Dreskin SC, Mustafa S, Maleki SJ, Mueller GA. J Agric Food Chem 71 2990-2998 (2023)
  28. A recombinant Der p 1-specific allergen-toxin demonstrates superior killing of allergen-reactive IgG+ hybridomas in comparison to its recombinant allergen-drug conjugate. Daramola AK, Akinrinmade OA, Fajemisin EA, Naran K, Mthembu N, Hadebe S, Brombacher F, Huysamen AM, Fadeyi OE, Hunter R, Barth S. Immunother Adv 3 ltac023 (2023)
  29. Comparative Analysis of the Immune Response and the Clinical Allergic Reaction to Papain-like Cysteine Proteases from Fig, Kiwifruit, Papaya, Pineapple and Mites in an Italian Population. Giangrieco I, Ciardiello MA, Tamburrini M, Tuppo L, Rafaiani C, Mari A, Alessandri C. Foods 12 2852 (2023)
  30. Comparative analysis of cysteine proteases reveals gene family evolution of the group 1 allergens in astigmatic mites. Shi L, Xiong Q, Ao FK, Wan TY, Xiao X, Liu X, Sun B, Tungtrongchitr A, Leung TF, Tsui SKW. Clin Transl Allergy 13 e12324 (2023)
  31. Design of a ProDer f 1 vaccine delivered by the MHC class II pathway of antigen presentation and analysis of the effectiveness for specific immunotherapy. Liu Z, Jiang Y, Li C. Int J Clin Exp Pathol 7 4636-4644 (2014)
  32. Specific IgY anti-group 1 dust mite allergens induced by unglycosylated synthetic oligopeptides Egea E, Mendoza D, Garavito G, Espejo Á, Lizaraso LM, Navarro E, Barrera LA. Biomedica 38 232-243 (2018)


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