Molecular cloning and expression of a Penicillium citrinum allergen with sequence homology and antigenic crossreactivity to a hsp 70 human heat shock protein

Shen, Horng-Der; Au, Lo‐Chun; Lin, Wei; Liaw, S.-F.; Tsai, Jaw‐Ji; Han, Shou‐Hwa

doi:10.1111/j.1365-2222.1997.tb01197.x

Cited by 34 publications

(16 citation statements)

References 27 publications

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“…IgE cross-reactivity among these serine protease allergens was also detected [13, 14, 15, 16]. In addition, we have documented that a heat shock protein in the hsp70 family [18]and an 18-kD peroxisomal membrane protein [19]are also important allergens of P. citrinum. In addition to the serine protease and peroxisomal membrane protein [20]allergens, more than 10 different A. fumigatus allergens have also been identified through molecular approaches [21, 22].…”

Section: Introductionmentioning

confidence: 90%

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: Introductionmentioning

confidence: 90%

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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“…Besides the serine protease allergens, a 68-kD allergen N-acetylglucosaminidase and an allergenic heat-shock protein belonging to the HSP-70 family have also been identified from P. chrysogenum and in P. citrinum , respectively [55, 56]. They have been designated by the Allergen Nomenclature Subcommittee as Pen ch 20 and Pen c 19, respectively [23].…”

Section: Characterization Of Fungal Allergensmentioning

confidence: 99%

Immunobiology of Fungal Allergens

Kurup

Shen

Vijay

2002

Int Arch Allergy Immunol

100

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In recent years, considerable attention has been paid in obtaining purified relevant allergens from fungi associated with allergy. Using molecular biology techniques, a number of mold allergens have been obtained by cloning the genes encoding the allergens. Currently, about 70 fungal allergens have been approved by the International Allergen Nomenclature Committee. In this review, we have presented major allergens from Aspergillus, Penicillium, Cladosporium, and Alternaria and discussed their immunochemical characteristics and their role in the diagnosis of allergy and possible usefulness in understanding the pathogenesis of the disease. The structure-function properties and the potential role of these recombinant allergens in the immunomodulatory therapy also are presented.

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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: 84%

“…In addition, the purified Pen n 13 demonstrated positive immediate skin test reactivity in asthmatic patients and showed histamine release from the peripheral leukocytes of asthmatic patients. Other allergens, particularly the 68 KD 6-Nactylglucosaminidase and a heat shock protein in the hsp 70 family have been identified from R notatum and P. citrinum, respectively (28,29). Furthermore, an 18 KD peroxisomal membrane protein [Pen c 3] having IgE cross-reactivity with recombinant Asp f 3 has also been reported (48).…”

Section: Aspergillus Speciesmentioning

confidence: 99%

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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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Molecular cloning and expression of a Penicillium citrinum allergen with sequence homology and antigenic crossreactivity to a hsp 70 human heat shock protein

Abstract: Results obtained suggest that hsp 70 is an allergen of P. citrinum and that clones SC4 and XL contain partial cDNAs of this allergen gene.

Cited by 34 publications

References 27 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>

Immunobiology of Fungal Allergens

Molecular biology and immunology of fungal allergens

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