Characterization of the 33‐kilodalton major allergen of Penicillium citrinum by using MoAbs and N‐terminal amino acid sequencing

Shen, Horng-Der; Lin, Wei; Liaw, S.-F.; Tam, Ming F.; Han, Shou‐Hwa

doi:10.1111/j.1365-2222.1997.tb00676.x

Cited by 33 publications

(60 citation statements)

References 22 publications

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“…Crude allergenic extracts of P. citrinum and A. fumigatus were prepared essentially as previously described [12, 16]. The P. citrinum strain 52-5 [12]was isolated from the air in the Taipei area and verified by the American Type Culture Collection.…”

Section: Methodsmentioning

confidence: 99%

“…The P. citrinum strain 52-5 [12]was isolated from the air in the Taipei area and verified by the American Type Culture Collection. The A. fumigatus strain used was CCRC33476 [16].…”

Section: Methodsmentioning

confidence: 99%

“…Protein components in the crude fungal extracts were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) or by 2D gel electrophoresis and transferred electrophoretically onto polyvinylidene difluoride (PVDF) membrane (0.45 µm, Millipore, Bedford, Mass., USA) as described [12, 13, 14, 15, 16]. The membrane was blocked with 1% skim milk, then incubated with diluted human serum samples (1:5 dilution in Tris-buffered saline, pH 7.5, 0.05% Tween 20 and 1% skim milk) for 16 h at 4°C.…”

Section: Methodsmentioning

confidence: 99%

“…We have shown previously that the alkaline/vacuolar serine proteases are major allergens in eight prevalent Penicillium and Aspergillus species (Penicillium citrinum, Penicillium brevicompactum, Penicillium notatum, Penicillium oxalicum, Aspergillus oryzae, Aspergillus flavus, Aspergillus fumigatus, Aspergillus niger) [12, 13, 14, 15, 16, 17]. IgE cross-reactivity among these serine protease allergens was also detected [13, 14, 15, 16].…”

Section: Introductionmentioning

confidence: 99%

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cDNA Cloning and Immunological Characterization of a Newly Identified Enolase Allergen from Penicillium citrinum and Aspergillus fumigatus

Lai¹,

Tam

Tang

et al. 2002

Int Arch Allergy Immunol

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Background:Penicillium citrinum and Aspergillus fumigatus are prevalent indoor airborne fungal species that have been implicated in human respiratory allergic disorders. It is important to understand the allergenic profile of these fungal species. The purpose of the present study is to characterize a newly identified enolase allergen from P. citrinum and A. fumigatus. Methods: Fungal proteins were separated by two-dimensional (2D) gel electrophoresis and blotted onto polyvinylidene difluoride membranes. Protein spots that reacted with IgE antibodies in serum samples from asthmatic patients were identified and the N-terminal amino acid sequences were determined by Edman degradation. The peptide sequences obtained were utilized in cloning the cDNA of the allergen genes by reverse transcriptase-polymerase chain reaction and the 5′- and 3′-rapid amplification cDNA end reactions. Results: Our results from 2D immunoblotting identified a 47-kD IgE-reactive component in the extracts of P. citrinum and A. fumigatus. The N-terminal amino acid sequences of the 47-kD proteins are homologous to those of fungal enolases. The corresponding enolase cDNA from P. citrinum contains 1,552 bp and encodes a protein of 438 residues. In A. fumigatus, the isolated enolase cDNA has 1,649 bp and contains a 438-amino acid open reading frame. The deduced amino acid sequences of these two enolases have 94% identity. These enolases from P. citrinum and A. fumigatus were expressed in Escherichia coli as a His-tagged protein and designated as rPen c 22 and rAsp f 22, respectively. Sera from 7 (30%) of the 23 Penicillium-sensitized asthmatic patients showed IgE binding to the 47-kD P. citrinum component (Pen c 22) and rPen c 22. In addition, six of seven Pen c 22-positive serum samples have IgE immunoblot reactivity to the 47-kD A. fumigatus component (Asp f 22) and rAsp f 22. A polyclonal rabbit antiserum generated against the N-terminal peptide of Pen c 22 can react with Pen c 22, rPen c 22, Asp f 22 and rAsp f 22. In addition, the presence of IgE cross-reactivity between rPen c 22 and rAsp f 22 and between enolases from A. fumigatus and Alternaria alternata was also detected by immunoblot inhibition. Conclusions: These results demonstrated that a novel enolase allergen from P. citrinum (Pen c 22) and A. fumigatus (Asp f 22) was identified. In addition, IgE cross-reactivity between enolase allergens from A. fumigatus and P. citrinum and between enolases from A. fumigatus and A. alternata was also detected. Results obtained provide more information on fungal enolase allergens.

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Section: Methodsmentioning

confidence: 99%

“…The P. citrinum strain 52-5 [12]was isolated from the air in the Taipei area and verified by the American Type Culture Collection. The A. fumigatus strain used was CCRC33476 [16].…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

cDNA Cloning and Immunological Characterization of a Newly Identified Enolase Allergen from Penicillium citrinum and Aspergillus fumigatus

Lai¹,

Tam

Tang

et al. 2002

Int Arch Allergy Immunol

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“…Alkaline serine proteinases with allergenic properties such as Asp f'13, Asl~ f I 13, and Asp o 13 from A. fumigatus, A. flavus, and A. oryzae respectively have been reported (40). Similar serine proteinases Pen b 13, Pen c 13, and Pen n 13 with sequence homology to Aspergillus proteinase have also been identified from various species of Penicillium (28,29,41 Table 1 Alkaline serine protease Glucoamylase, cellulase and hemicellulase from A. nigerwere shown to be allergenic by skin prick tests and by in vitro specific IgE detection assays (44,45). In addition, c~ I~-xylosidase [Asp n 14] fronl A. niger was also identified as an occupational allergen present in baking additives, which causes sensitization in symptomatic bakers (45).…”

Section: Aspergillus Speciesmentioning

confidence: 88%

Molecular biology and immunology of fungal allergens

Kurup

Banerjee

Kelly

et al. 2000

Indian J Clin Biochem

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Fungi are non-chlorophyllus microorganisms, which constitutes the main source of outdoor and indoor allergens. The antigens present in the spores and fragments of hyphae induce allergic responses in sensitized patients. The frequently recognized fungi associated with asthma include Alternaria, Cladosporium, Aspergillus, and Penicillium. With the advent of molecular biology techniques a number of fungal genes encoding relevant allergens have been cloned and the expressed allergens purified and characterized. In this review, we have presented the recent developments, where recombinant allergens have been used in the precise diagnosis of fungal allergy. We have also discussed the role played by these allergens and the T-and B-cell epitopes in the immune mechanism in fungal allergy.

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Fungal Allergy and Allergens

Bush

2003

Encyclopedia of Environmental Microbiology

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Exposure to Fungal Allergens Mechanism of Fungal Allergy Prevalence of Fungal Sensitivity Association of the Fungal Sensitivity with Asthma Role of Fungal Exposure in Acute Asthma Attacks Role of Fungal Allergy in Severe and Fatal Asthma Indoor Fungal Exposure and Allergic Disease Purified Fungal Allergens Assessment of Fungal Allergen Exposure Abatement Measures to Reduce Fungal Allergen Exposure

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Characterization of the 33‐kilodalton major allergen of Penicillium citrinum by using MoAbs and N‐terminal amino acid sequencing

Abstract: Results obtained in the present study suggest that the 33 kD major allergen of P. citrinum may be an alkaline serine proteinase.

Cited by 33 publications

References 22 publications

cDNA Cloning and Immunological Characterization of a Newly Identified Enolase Allergen from <i>Penicillium citrinum</i> and <i>Aspergillus fumigatus</i>

cDNA Cloning and Immunological Characterization of a Newly Identified Enolase Allergen from <i>Penicillium citrinum</i> and <i>Aspergillus fumigatus</i>

Molecular biology and immunology of fungal allergens

Fungal Allergy and Allergens

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