Evaluation of two new recombinant guinea‐pig lipocalins, Cav p 2 and Cav p 3, in the diagnosis of guinea‐pig allergy

Hilger, Christiane; Swiontek, Kyra; Kler, Stéphanie; Diederich, Claire; Lehners, Christiane; Vogel, Lothar; Vieths, Stefan; Hentges, François

doi:10.1111/j.1365-2222.2011.03726.x

Cited by 29 publications

(19 citation statements)

References 24 publications

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“…Immunoblotting was performed, as previously described. 15 Briefly, polyvinylidene difluoride membranes were incubated overnight with patients' sera diluted 1:10 in blocking buffer (0.05% TRIS-buffered saline/Tween 20 and 3% BSA; Sigma-Aldrich, Bornem, Belgium). Specific bands were detected by adding anti-human IgE antibodies labeled with alkaline phosphatase (Sigma), followed by color development with nitroblue tetrazolium/5-bromo-4-chloro-3-indolyl-phosphate (NBT/BCIP; Promega, Leiden, The Netherlands).…”

Section: Sds-page and Immunoblottingmentioning

confidence: 99%

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Identification and isolation of a Fel d 1–like molecule as a major rabbit allergen

Hilger¹,

Kler²,

Arumugam³

et al. 2014

Journal of Allergy and Clinical Immunology

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Section: Sds-page and Immunoblottingmentioning

confidence: 99%

“…Specific IgE were quantified by means of ELISA, as previously described, 15 with purified native or deglycosylated Ory c 3. Blocking buffer was 3% BSA in PBS.…”

Section: Quantification Of Ige Antibodies With Elisamentioning

confidence: 99%

Identification and isolation of a Fel d 1–like molecule as a major rabbit allergen

Hilger¹,

Kler²,

Arumugam³

et al. 2014

Journal of Allergy and Clinical Immunology

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“…These include Fel d 1-like allergens from dogs and rabbits [15, 16], a major dog allergen Can f 5 which is a prostatic kallikrein [17], and two guinea pig lipocalins, Cav p 2 and Cav p 3. The latter are major allergens, proven to be valuable for diagnosis of guinea pig allergy when combined with serum albumin Cav p 4 [18]. Several new allergens, classified in up to 33 groups, have been identified in mite.…”

Section: Update Of Allergen Nomenclature and Recently Identified Allementioning

confidence: 99%

Interfaces Between Allergen Structure and Diagnosis: Know Your Epitopes

Pomés

Chruszcz

Gustchina

et al. 2015

Curr Allergy Asthma Rep

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Allergy diagnosis is based on the patient’s clinical history and can be strengthened by tests that confirm the origin of sensitization. In the past 25 years, these tests have evolved from the exclusive in vivo or in vitro use of allergen extracts, to complementary molecular-based diagnostics that rely on in vitro measurements of IgE reactivity to individual allergens. For this to occur, an increase in our understanding of the molecular structure of allergens, largely due to the development of technologies such as molecular cloning and expression of recombinant allergens, X-ray crystallography, or nuclear magnetic resonance (NMR), has been essential. New in vitro microarray or multiplex systems are now available to measure IgE against a selected panel of purified natural or recombinant allergens. The determination of the three-dimensional structure of allergens has facilitated detailed molecular studies, including the analysis of antigenic determinants for diagnostic purposes.

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“…The major dog allergen Can f 6, with 57% amino acid identity to Equ c 1 and highly cross-reactive with Fel d 4 (67% amino acid identity) has recently been identified in a population of cat- and dog-sensitized patients [99]. Three lipocalins from guinea pig Cavia porcellus (Cav p 1, Cav p 2 and Cav p 3) have also been described as major allergens [100, 101]. The degree of homology between Bla g 4 and the mammalian allergens is low (approximately 15–18%) and small cross-reactivity with mammalian allergens would be expected.…”

Section: Groups Of Cockroach Allergensmentioning

confidence: 99%

Investigating cockroach allergens: Aiming to improve diagnosis and treatment of cockroach allergic patients

Pomés

Arruda

2014

Methods

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Cockroach allergy is an important health problem associated with the development of asthma, as a consequence of chronic exposure to low levels of allergens in susceptible individuals. In the last 20 years, progress in understanding the disease has been possible, thanks to the identification and molecular cloning of cockroach allergens and their expression as recombinant proteins. Assays for assessment of environmental allergen exposure have been developed and used to measure Bla g 1 and Bla g 2, as markers of cockroach exposure. IgE antibodies to cockroach extracts and to specific purified allergens have been measured to assess sensitization and analyze association with exposure and disease. With the development of the field of structural biology and the expression of recombinant cockroach allergens, insights into allergen structure, function, epitope mapping and allergen-antibody interactions have provided further understanding of mechanisms of cockroach allergic disease at the molecular level. This information will contribute to develop new approaches to allergen avoidance and to improve diagnosis and therapy of cockroach allergy.

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Evaluation of two new recombinant guinea‐pig lipocalins, Cav p 2 and Cav p 3, in the diagnosis of guinea‐pig allergy

Abstract: Two major guinea-pig allergens, Cav p 2 and Cav p 3, have been characterized and produced as recombinant proteins. Combined to guinea-pig serum albumin, the new allergens proved to be valuable in the component-resolved diagnosis of guinea-pig allergy.

Cited by 29 publications

References 24 publications

Identification and isolation of a Fel d 1–like molecule as a major rabbit allergen

Identification and isolation of a Fel d 1–like molecule as a major rabbit allergen

Interfaces Between Allergen Structure and Diagnosis: Know Your Epitopes

Investigating cockroach allergens: Aiming to improve diagnosis and treatment of cockroach allergic patients

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