The role of indoor allergens in chronic allergic disease

Platts-Mills, Thomas A.E.

doi:10.1016/j.jaci.2006.12.647

Cited by 42 publications

(30 citation statements)

References 50 publications

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“…Our study demonstrated that approximately 60% of the cat-allergic subjects had detectable titers of IgE to rFel d 1. Previously published values have ranged from 65 to 95% [5,6,7,8,9,10,11,28]. In our study, the percent of IgE binding increased to 83% if those cat-allergic individuals with a RAST <2 to cat dander extract were excluded (data not shown).…”

Section: Discussionsupporting

confidence: 54%

“…A comparison with HDM allergens showed this was associated with a lower amount of non-antigen-specific IgE antibody indicating the absence of a nonspecific stimulus for IgE found in other allergen sources [9]. The low titers have been especially found in adults presenting with rhinoconjunctivitis who constitute the bulk of the sample studied here [10].…”

Section: Discussionmentioning

confidence: 98%

“…They could have a significant impact on the efficacy of immunotherapy with Fel d 1 alone and may need to be considered for use in patient selection for therapy. This consideration has become increasingly relevant since it is now evident that most cat-allergic adults with rhinoconjunctivitis have low titers of anti-Fel d 1 antibody, so even small IgE responses to other specificities could constitute a significant proportion of their allergy [5,6,7,8,9,10,11]. This study describes two newly identified cat allergens of potential importance.…”

Section: Introductionmentioning

confidence: 99%

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Two Newly Identified Cat Allergens: The von Ebner Gland Protein Fel d 7 and the Latherin-Like Protein Fel d 8

Smith

O’Neil

Hales

et al. 2011

Int Arch Allergy Immunol

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Introduction: 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.

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Section: Discussionsupporting

confidence: 54%

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Two Newly Identified Cat Allergens: The von Ebner Gland Protein Fel d 7 and the Latherin-Like Protein Fel d 8

Smith

O’Neil

Hales

et al. 2011

Int Arch Allergy Immunol

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“…Mus m 1 belongs to the lipocalin superfamily and is one of the most important allergens for mouse allergic patients [7]. In recent years, Mus m 1 received considerable attention as a model system to unveil structural and energetic features of protein-ligand interaction and the mutation Y120F has been found to alter the protein binding activity [21,22,23,24].…”

Section: Discussionmentioning

confidence: 99%

“…Mouse allergy is both an occupational disease [1,2] and a disorder that can occur in homes [3,4,5], where it may negatively impact on the efficacious clinical control of asthmatic children: mouse urinary proteins (MUPs) represent the main etiologic agent of mouse allergy [6,7], being excreted into the environment where they are extremely stable and can easily reach the airways. The MUPs belong to the lipocalin superfamily which includes several allergenic proteins, such as the major rat allergen (Rat n 1), dog allergens (Can f 1 and Can f 2), cow allergen (Bos d 5), horse allergen (Equ c 1) and cockroach allergen (Bla g 4) [8].…”

Section: Introductionmentioning

confidence: 99%

In Search of a Vaccine for Mouse Allergy: Significant Reduction of Mus m 1 Allergenicity by Structure-Guided Single-Point Mutations

Ferrari

Breda

Longhi

et al. 2011

Int Arch Allergy Immunol

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Background: Mouse urinary proteins are relevant allergens from mice urine. We used the recombinant protein Mus m 1 as an allergen model to identify if, by altering Mus m 1 architecture via single-point mutations, we could effectively modify its allergenicity. Methods: Based on structural considerations, we synthesized two single-point mutants, Mus m 1-Y120A and Mus m 1-Y120F, which were expected to harbor large structural alterations. Circular dichroism and fluorescence analysis showed significant conformational rearrangements of the aromatic side chains in the internal cavity of Mus m 1-Y120A when compared to Mus m 1-Y120F and Mus m 1. Evaluation of the allergenic potential of the recombinant molecules was performed in vitro with both immunochemical approaches and assays based on the measurement of basophil degranulation. Moreover, to assess the integrity of the T cell epitopes and as an in vitro measure of immunogenicity, we tested the reactivity of T lymphocytes from subjects allergic to mouse urine against proteins and synthetic peptides encompassing the immunodominant linear epitope containing the mutation. Results: We found that the selected point mutation was able to modulate the protein allergenicity, and to severely impair the recognition of Mus m 1 by IgE, while T cell reactivity was fully maintained. Conclusions: In silico predicted, minimum selected structural modifications allowed to design one protein with reduced allergenicity and preserved immunogenicity. Structurally guided mutations can direct the design of proteins with reduced allergenicity which can be used as vaccines for a safer and more effective immunotherapy of allergic disorders.

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Molecular Biology of Allergens: Structure and Immune Recognition

Chapman

Pomés

Aalberse

Allergy Frontiers: Epigenetics, Allergens and Risk Factors

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The role of indoor allergens in chronic allergic disease

Cited by 42 publications

References 50 publications

Two Newly Identified Cat Allergens: The von Ebner Gland Protein Fel d 7 and the Latherin-Like Protein Fel d 8

Two Newly Identified Cat Allergens: The von Ebner Gland Protein Fel d 7 and the Latherin-Like Protein Fel d 8

In Search of a Vaccine for Mouse Allergy: Significant Reduction of Mus m 1 Allergenicity by Structure-Guided Single-Point Mutations

Molecular Biology of Allergens: Structure and Immune Recognition

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