Cockroach Allergens: Function, Structure and Allergenicity

Pomés, Anna; Wünschmann, Sabina; Hindley, James P.; Vailes, Lisa D.; Chapman, Martin D.

doi:10.2174/092986607782541178

Cited by 37 publications

(44 citation statements)

References 70 publications

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“…However, most B. germanica allergens present homologues in P. americana which could account for IgE cross-reactivity [5]. Another hypothesis would be that the pattern of environmental exposure to cockroach allergens leading to sensitization may be distinct.…”

Section: Discussionmentioning

confidence: 99%

“…Allergens from the two most common domiciliary cockroach species, Blattella germanica and Periplaneta americana , have been identified, with diverse structure and biological function. Cockroach allergens comprise at least 10 groups of distinct proteins, including Bla g 1 and Per a 1 (midgut microvilli protein homologues), Bla g 2 and Per a 2 (inactive aspartic proteases), Per a 3 (arylphorin/hemocyanin), Bla g 4 and Per a 4 (male pheromone transport lipocalins), Bla g 5 and Per a 5 (glutathione-S-transferases), Bla g 6 and Per a 6 (troponins), Bla g 7 and Per a 7 (tropomyosins), Bla g 8 (myosin light chain), Bla g 9 and Per a 9 (arginine kinases) and Per a 10 (serine protease) [5]. B. germanica enolase and vitellogenin have also been identified as novel cockroach allergens by proteomics approach [6].…”

Section: Introductionmentioning

confidence: 99%

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Efficacy of Recombinant Allergens for Diagnosis of Cockroach Allergy in Patients with Asthma and/or Rhinitis

Barbosa¹,

Santos²,

Ferriani

et al. 2013

Int Arch Allergy Immunol

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Background: Immunoglobulin E (IgE) reactivity to individual allergens among cockroach-allergic patients has revealed wide variability. The aim of this study was to assess the effectiveness of recombinant cockroach allergens for skin testing, and to determine sensitization profiles among cockroach-allergic patients living in Brazil. Methods: Fifty-seven cockroach-allergic patients with asthma and/or rhinitis were recruited. Skin testing with recombinant (r) allergens from Periplaneta americana (rPer a 1 and rPer a 7) and Blattella germanica (rBla g 2, rBla g 4 and rBla g 5) were performed at 10 μg/ml and 5 μg/ml (rPer a 1). IgE antibodies to rPer a 7 and rPer a 1 were quantitated by ELISA. Results: Of 57 patients tested, 3 (5.3%), 24 (42.1%), 4 (7%), 3 (5.3%) and 4 (7%) showed positive reactions to rPer a 1, rPer a 7, rBla g 2, rBla g 4 and rBla g 5, respectively. Twenty-eight patients (49.1%) had positive tests to at least one allergen. In keeping with skin test results, 31/57 patients (54.4%) and 5/55 patients (9%) had detectable IgE to rPer a 7 and rPer a 1, respectively. Levels of IgE to rPer a 7 were higher in patients with positive tests to rPer a 7 than those with negative tests (geometric mean 13.2 and 1.8 IU/ml, p < 0.05). There was good concordance of results of skin tests and measurements of serum IgE to rPer a 7. Conclusion: IgE reactivity to rPer a 7 (P. americana tropomyosin) was dominant among patients in Brazil. However, 50% of the patients did not present reactivity to any of the recombinant allergens tested.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Efficacy of Recombinant Allergens for Diagnosis of Cockroach Allergy in Patients with Asthma and/or Rhinitis

Barbosa¹,

Santos²,

Ferriani

et al. 2013

Int Arch Allergy Immunol

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“…Several allergens from Blattella germanica, or the German cockroach, have been described to date [1]. In a recent study, sensitization to cockroach allergens (Bla g 1, Bla g 2, Bla g 4, Bla g 5, and Per a 7) was assessed in 118 patients with known cockroach allergies [2].…”

Section: Introductionmentioning

confidence: 99%

Reactivity of German Cockroach Allergen, Bla g 2, Peptide Fragments to IgE Antibodies in Patients' Sera

et al. 2008

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Bla g 2 is a cockroach allergen of great importance. This study was conducted to identify IgE-binding epitope(s) of Bla g 2 using the recombinant protein technique. Approximately 50% of tested sera showed IgE reactivity to Pichiaexpressed Bla g 2 (PrBla g 2) and E. coli-expressed Bla g 2 (ErBla g 2). Only 5.3% of serum samples showed stronger reactivity to PrBla g 2 than ErBla g 2, indicating that serum was reactive to conformational or carbohydrate epitopes. The full-length and 5 peptide fragments of Bla g 2 were produced in E. coli. All fragments showed IgE-binding activity to the cockroach-allergy patients' sera. Specifically, peptide fragments of amino acid residue 1-75 and 146-225 appeared to be important for IgE-binding. The information about the IgE-binding epitope of Bla g 2 can aid in the diagnosis and treatment for cockroach allergies.

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“…The Allergen Nomenclature Subcommittee (www.allergen.org) has officially listed 10 different groups of proteins as cockroach allergens, and 6 allergens from German cockroaches have been described in the literature to elicit IgE responses in genetically predisposed individuals [1]. All 6 allergens (Bla g 1, 2, 4, 5, 6, and 7) that have been tested to date exhibit a low degree of IgE reactivity and frequency among Korean cockroach-sensitized subjects [2,3,4,5,6,7].…”

Section: Introductionmentioning

confidence: 99%

Identification of Novel Allergenic Components from German Cockroach Fecal Extract by a Proteomic Approach

Jeong

Kim

Park

et al. 2013

Int Arch Allergy Immunol

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Background: Cockroaches produce potent allergens, and cockroach feces are known to be especially rich in allergens. In this study, we analyze the allergenic components from cockroach feces and evaluate allergenicity of recombinant α-amylase identified from fecal extract. Methods: IgE-reactive proteins from German cockroach fecal extract were analyzed by proteomic analysis and immunoblotting. Recombinant α-amylase was produced and its allergenicity was evaluated by ELISA. Results: Analysis of German cockroach fecal extracts identified 12 IgE-reactive components. Most of these allergens were found to be digestive enzymes such as α-amylase, trypsin, chymotrypsin, metalloprotease, and midgut carboxypeptidase A, but the identity of 3 IgE-reactive proteins is still unknown. Glycinin-like proteins, which were likely derived from the cockroach diet, were also identified. German cockroach α-amylase shares the highest identity with pig α-amylase (55.8%), followed by mite group 4 allergens (Blo t 4, 50.4%; Der p 4, 49.8%; Eur m 4, 47.4%). In this study, recombinant α-amylase from German cockroach was expressed, and its allergenicity was examined by ELISA. Specific IgE against recombinant amylase was detected in 41.4% (12/29) of serum samples from German cockroach-sensitized subjects. Recombinant α-amylase was able to inhibit 55% of specific IgE to German cockroach whole-body extract. Conclusions: Amylase was found to be an important novel allergen in cockroach feces. It is hoped that recombinant α-amylase will be useful for further studies and clinical applications.

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Cockroach Allergens: Function, Structure and Allergenicity

Cited by 37 publications

References 70 publications

Efficacy of Recombinant Allergens for Diagnosis of Cockroach Allergy in Patients with Asthma and/or Rhinitis

Efficacy of Recombinant Allergens for Diagnosis of Cockroach Allergy in Patients with Asthma and/or Rhinitis

Reactivity of German Cockroach Allergen, Bla g 2, Peptide Fragments to IgE Antibodies in Patients' Sera

Identification of Novel Allergenic Components from German Cockroach Fecal Extract by a Proteomic Approach

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