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J Biol Chem. 2014 Aug 22;289(34):23382-8. doi: 10.1074/jbc.M114.579060. Epub 2014 Jul 3.

Molecular and immunological characterization of the first allergenic lipocalin in hamster: the major allergen from Siberian hamster (Phodopus sungorus).

Author information

1
From the Allergy Department, Hospital Fundación Jiménez Díaz, 28040 Madrid.
2
the Department of Immunology, Instituto de Investigaciones Sanitarias Fundación Jiménez Díaz, Universidad Autónoma de Madrid, 28040 Madrid.
3
the Department of Immunology, Instituto de Investigaciones Sanitarias Fundación Jiménez Díaz, Universidad Autónoma de Madrid, 28040 Madrid, the Department of Biochemistry and Molecular Biology I, Universidad Complutense de Madrid, 28040 Madrid, and.
4
From the Allergy Department, Hospital Fundación Jiménez Díaz, 28040 Madrid, the Centro de Investigación Biomédica en Red de Enfermedades Respiratorias (CIBERES), Instituto de Salud Carlos III, 28029 Madrid, Spain.
5
the Department of Immunology, Instituto de Investigaciones Sanitarias Fundación Jiménez Díaz, Universidad Autónoma de Madrid, 28040 Madrid, cpastor@fjd.es.

Abstract

The most frequent pet allergy is to cat and dog, but in recent years, it has become increasingly popular to have other pets, and the risk of exposure to new allergens is more prevalent. The list of new pets includes hamsters, and one of the most popular hamsters is the Siberian hamster (Phodopus sungorus). The aim of this study was the characterization and cloning of the major allergen from this hamster. The study of its allergenicity and cross-reactivity could improve the specific diagnosis and treatment for hamster-allergic patients. Thirteen Siberian hamster-allergic patients were recruited at the outpatient clinic. Protein extracts were prepared from the hair, urine, and salivary glands of four hamster species (European, golden, Siberian, and Roborovski). IgE-binding proteins were detected by immunoblotting and identified by mass spectrometry. The recombinant protein was produced in Escherichia coli and then purified by metal chelate affinity chromatography. The allergenic properties of the recombinant protein were tested by ELISA and immunoblotting, and biological activity was tested according to capacity for basophil activation. Three IgE-binding proteins were identified in extracts obtained from Siberian hamster hair, urine, and salivary glands. All proteins corresponded to the same protein, which was identified as a lipocalin. This lipocalin had no cross-reactivity with common and golden hamsters. The recombinant allergen was cloned and purified, showing similar IgE reactivity in vitro to Siberian hamster protein extracts. Also, the recombinant allergen was capable of producing biological activation in vivo. The major Siberian hamster allergen was cloned, and allergenic properties were characterized, providing a new tool for specific diagnosis of allergy to Siberian hamster.

KEYWORDS:

Allergen; Allergy; Asthma; Hamster; Immunoglobulin E (IgE); Inflammation; Lipocalin; Pet Allergy

PMID:
24993820
PMCID:
PMC4156070
DOI:
10.1074/jbc.M114.579060
[Indexed for MEDLINE]
Free PMC Article

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