Crystal structure and epitope analysis of house dust mite allergen Der f 21
Group 21 and 5 allergens are homologous house dust mite proteins known as mid-tier allergens. To reveal the biological function of group 21 allergens and to understand better the allergenicity of the rDer f 21 allergen, we determined the 1.5Å crystal structure of rDer f 21 allergen from Dermatophago...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2019
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| Online Access: | http://psasir.upm.edu.my/id/eprint/81057/1/ABSTRACT.pdf |
| _version_ | 1796980851782713344 |
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| author | Sze, Lei Pang Ho, Kok Lian Waterman, Jitka Rambo, Robert Paul Teh, Aik-Hon Mathavan, Indran Harris, Gemma Beis, Konstantinos Say, Yee How Anusha, Matta Sri Sio, Yang Yie Chew, Fook Tim Ng, Chyan Leong |
| author_facet | Sze, Lei Pang Ho, Kok Lian Waterman, Jitka Rambo, Robert Paul Teh, Aik-Hon Mathavan, Indran Harris, Gemma Beis, Konstantinos Say, Yee How Anusha, Matta Sri Sio, Yang Yie Chew, Fook Tim Ng, Chyan Leong |
| author_sort | Sze, Lei Pang |
| collection | UPM |
| description | Group 21 and 5 allergens are homologous house dust mite proteins known as mid-tier allergens. To reveal the biological function of group 21 allergens and to understand better the allergenicity of the rDer f 21 allergen, we determined the 1.5Å crystal structure of rDer f 21 allergen from Dermatophagoides farinae. The rDer f 21 protein consists of a three helical bundle, similar to available structures of group 21 and homologous group 5 allergens. The rDer f 21 dimer forms a hydrophobic binding pocket similar to the one in the Der p 5 allergen, which indicates that both of the homologous groups could share a similar function. By performing structure-guided mutagenesis, we mutated all 38 surface-exposed polar residues of the rDer f 21 allergen and carried out immuno-dot blot assays using 24 atopic sera. Six residues, K10, K26, K42, E43, K46, and K48, which are located in the region between the N-terminus and the loop 1 of rDer f 21 were identifed as the major IgE epitopes of rDer
f 21. Epitope mapping of all potential IgE epitopes on the surface of the rDer f 21 crystal structure revealed heterogeneity in the sIgE recognition of the allergen epitopes in atopic individuals. The higher the allergen-sIgE level of an individual, the higher the number of epitope residues that are found in the allergen. The results illustrate the clear correlation between the number of specifc major epitope residues in an allergen and the sIgE level of the atopic population. |
| first_indexed | 2024-03-06T10:29:08Z |
| format | Article |
| id | upm.eprints-81057 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T10:29:08Z |
| publishDate | 2019 |
| publisher | Nature Portfolio |
| record_format | dspace |
| spelling | upm.eprints-810572022-07-21T07:31:54Z http://psasir.upm.edu.my/id/eprint/81057/ Crystal structure and epitope analysis of house dust mite allergen Der f 21 Sze, Lei Pang Ho, Kok Lian Waterman, Jitka Rambo, Robert Paul Teh, Aik-Hon Mathavan, Indran Harris, Gemma Beis, Konstantinos Say, Yee How Anusha, Matta Sri Sio, Yang Yie Chew, Fook Tim Ng, Chyan Leong Group 21 and 5 allergens are homologous house dust mite proteins known as mid-tier allergens. To reveal the biological function of group 21 allergens and to understand better the allergenicity of the rDer f 21 allergen, we determined the 1.5Å crystal structure of rDer f 21 allergen from Dermatophagoides farinae. The rDer f 21 protein consists of a three helical bundle, similar to available structures of group 21 and homologous group 5 allergens. The rDer f 21 dimer forms a hydrophobic binding pocket similar to the one in the Der p 5 allergen, which indicates that both of the homologous groups could share a similar function. By performing structure-guided mutagenesis, we mutated all 38 surface-exposed polar residues of the rDer f 21 allergen and carried out immuno-dot blot assays using 24 atopic sera. Six residues, K10, K26, K42, E43, K46, and K48, which are located in the region between the N-terminus and the loop 1 of rDer f 21 were identifed as the major IgE epitopes of rDer f 21. Epitope mapping of all potential IgE epitopes on the surface of the rDer f 21 crystal structure revealed heterogeneity in the sIgE recognition of the allergen epitopes in atopic individuals. The higher the allergen-sIgE level of an individual, the higher the number of epitope residues that are found in the allergen. The results illustrate the clear correlation between the number of specifc major epitope residues in an allergen and the sIgE level of the atopic population. Nature Portfolio 2019 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/81057/1/ABSTRACT.pdf Sze, Lei Pang and Ho, Kok Lian and Waterman, Jitka and Rambo, Robert Paul and Teh, Aik-Hon and Mathavan, Indran and Harris, Gemma and Beis, Konstantinos and Say, Yee How and Anusha, Matta Sri and Sio, Yang Yie and Chew, Fook Tim and Ng, Chyan Leong (2019) Crystal structure and epitope analysis of house dust mite allergen Der f 21. Scientific Reports, 9. art. no. 4933. pp. 1-13. ISSN 2045-2322 https://www.nature.com/articles/s41598-019-40879-x 10.1038/s41598-019-40879-x |
| spellingShingle | Sze, Lei Pang Ho, Kok Lian Waterman, Jitka Rambo, Robert Paul Teh, Aik-Hon Mathavan, Indran Harris, Gemma Beis, Konstantinos Say, Yee How Anusha, Matta Sri Sio, Yang Yie Chew, Fook Tim Ng, Chyan Leong Crystal structure and epitope analysis of house dust mite allergen Der f 21 |
| title | Crystal structure and epitope analysis of house dust mite allergen Der f 21 |
| title_full | Crystal structure and epitope analysis of house dust mite allergen Der f 21 |
| title_fullStr | Crystal structure and epitope analysis of house dust mite allergen Der f 21 |
| title_full_unstemmed | Crystal structure and epitope analysis of house dust mite allergen Der f 21 |
| title_short | Crystal structure and epitope analysis of house dust mite allergen Der f 21 |
| title_sort | crystal structure and epitope analysis of house dust mite allergen der f 21 |
| url | http://psasir.upm.edu.my/id/eprint/81057/1/ABSTRACT.pdf |
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