Two newly identified cat allergens: The von Ebner gland protein Fel d 7 and the latherin-like protein Fel d 8

Characterization of the complete IgE binding spectrum of cat allergens is important for the development of improved diagnosis and effective immunotherapeutics. While Fel d 1 remains unchallenged as the major cat allergen, we now report the isolation of two new allergens capable of binding similar co...

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Main Authors: W. Smith, S. E. O'Neil, B. J. Hales, T. L.Y. Chai, L. A. Hazell, S. Tanyaratsrisakul, S. Piboonpocanum, W. R. Thomas
Other Authors: Telethon Institute for Child Health Research
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Published: 2018
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Online Access:https://repository.li.mahidol.ac.th/handle/123456789/12003
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spelling th-mahidol.120032018-05-03T15:27:00Z Two newly identified cat allergens: The von Ebner gland protein Fel d 7 and the latherin-like protein Fel d 8 W. Smith S. E. O'Neil B. J. Hales T. L.Y. Chai L. A. Hazell S. Tanyaratsrisakul S. Piboonpocanum W. R. Thomas Telethon Institute for Child Health Research Mahidol University Immunology and Microbiology Medicine Characterization of the complete IgE binding spectrum of cat allergens is important for the development of improved diagnosis and effective immunotherapeutics. While Fel d 1 remains unchallenged as the major cat allergen, we now report the isolation of two new allergens capable of binding similar concentrations of IgE in the allergic sera of some individuals. Materials and Methods: Cat tongue and submandibular salivary gland cDNA libraries were screened by DNA hybridisation and IgE immunoassay. The isolated DNA fragments were sub-cloned into an E. coli expression system and the IgE reactivity was examined with human cat-allergic sera using a DELFIA IgE quantitation assay. Results: Fel d 7, an 18 kDa von Ebner gland protein Can f 1 homologue, was isolated from the tongue library. Fel d 8, a 24-kDa latherin-like protein with homology to Equ c 5, was isolated from the submandibular library. The frequency of IgE binding of cat-allergic sera to recombinant Fel d 1, 7 and 8 was 60.5, 37.6 and 19.3%, respectively. Inhibition studies indicated some IgE binding cross-reactivity between Fel d 7 and dog dander extracts. Discussion: The study reports the isolation and characterization of two new cat allergens. The isolation of these allergens provides the opportunity to determine the role that IgE binding proteins other than Fel d 1 play in cat-allergic disease. For cat-allergic individuals with moderate to mild rhinoconjunctivitis these allergens may play a more important role in the manifestation of their allergic disease. Copyright © 2011 S. Karger AG, Basel. 2018-05-03T08:15:18Z 2018-05-03T08:15:18Z 2011-09-01 Article International Archives of Allergy and Immunology. Vol.156, No.2 (2011), 159-170 10.1159/000322879 14230097 10182438 2-s2.0-79955910838 https://repository.li.mahidol.ac.th/handle/123456789/12003 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79955910838&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Immunology and Microbiology
Medicine
spellingShingle Immunology and Microbiology
Medicine
W. Smith
S. E. O'Neil
B. J. Hales
T. L.Y. Chai
L. A. Hazell
S. Tanyaratsrisakul
S. Piboonpocanum
W. R. Thomas
Two newly identified cat allergens: The von Ebner gland protein Fel d 7 and the latherin-like protein Fel d 8
description Characterization of the complete IgE binding spectrum of cat allergens is important for the development of improved diagnosis and effective immunotherapeutics. While Fel d 1 remains unchallenged as the major cat allergen, we now report the isolation of two new allergens capable of binding similar concentrations of IgE in the allergic sera of some individuals. Materials and Methods: Cat tongue and submandibular salivary gland cDNA libraries were screened by DNA hybridisation and IgE immunoassay. The isolated DNA fragments were sub-cloned into an E. coli expression system and the IgE reactivity was examined with human cat-allergic sera using a DELFIA IgE quantitation assay. Results: Fel d 7, an 18 kDa von Ebner gland protein Can f 1 homologue, was isolated from the tongue library. Fel d 8, a 24-kDa latherin-like protein with homology to Equ c 5, was isolated from the submandibular library. The frequency of IgE binding of cat-allergic sera to recombinant Fel d 1, 7 and 8 was 60.5, 37.6 and 19.3%, respectively. Inhibition studies indicated some IgE binding cross-reactivity between Fel d 7 and dog dander extracts. Discussion: The study reports the isolation and characterization of two new cat allergens. The isolation of these allergens provides the opportunity to determine the role that IgE binding proteins other than Fel d 1 play in cat-allergic disease. For cat-allergic individuals with moderate to mild rhinoconjunctivitis these allergens may play a more important role in the manifestation of their allergic disease. Copyright © 2011 S. Karger AG, Basel.
author2 Telethon Institute for Child Health Research
author_facet Telethon Institute for Child Health Research
W. Smith
S. E. O'Neil
B. J. Hales
T. L.Y. Chai
L. A. Hazell
S. Tanyaratsrisakul
S. Piboonpocanum
W. R. Thomas
format Article
author W. Smith
S. E. O'Neil
B. J. Hales
T. L.Y. Chai
L. A. Hazell
S. Tanyaratsrisakul
S. Piboonpocanum
W. R. Thomas
author_sort W. Smith
title Two newly identified cat allergens: The von Ebner gland protein Fel d 7 and the latherin-like protein Fel d 8
title_short Two newly identified cat allergens: The von Ebner gland protein Fel d 7 and the latherin-like protein Fel d 8
title_full Two newly identified cat allergens: The von Ebner gland protein Fel d 7 and the latherin-like protein Fel d 8
title_fullStr Two newly identified cat allergens: The von Ebner gland protein Fel d 7 and the latherin-like protein Fel d 8
title_full_unstemmed Two newly identified cat allergens: The von Ebner gland protein Fel d 7 and the latherin-like protein Fel d 8
title_sort two newly identified cat allergens: the von ebner gland protein fel d 7 and the latherin-like protein fel d 8
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/12003
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