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Transaldolases are novel and immunoglobulin E cross‐reacting fungal allergens
Author(s) -
Chou H.,
Tam M. F.,
Chiang C.H.,
Chou C.T.,
Tai H.Y.,
Shen H.D.
Publication year - 2011
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.2011.03698.x
Subject(s) - immunology , antibody , cross reactions , immunoglobulin e , immunoglobulin g , medicine , microbiology and biotechnology , chemistry , biology
Summary Background Mould‐induced atopic respiratory diseases are a worldwide problem. Characterization of fungal allergens is of major clinical importance. Objective We identified a novel transaldolase family allergen of Cladosporium and Penicillium species. Methods Fungal allergens were identified by immunoblotting, peptide mass mapping and partial sequencing, cDNA cloning and IgE epitope mapping. Results A 36.5 kDa IgE‐binding component in a partially purified C. cladosporioides preparation was identified. Mass spectrometric analyses suggest that this novel IgE‐reacting allergen is a transaldolase. A corresponding full‐length 1246 bp cDNA encoding a polypeptide of 325 residues was isolated. The newly identified transaldolase allergen has been designated as Cla c 14.0101. The cDNA encoding the Pencillium chrysogenum transaldolase was isolated by RT‐PCR according to the cDNA sequence encoding a P. chrysogenum Wisconsin 54‐1255 hypothetical protein. The purified rCla c 14.0101 protein reacted with IgE antibodies in 10 (38%) of 26 Cladosporium clado s porioides ‐sensitized asthmatic patients. Nine of the 10 rCla c 14.0101‐positive sera have IgE binding against the recombinant Penicillium transaldolase (rPen ch 35.0101). Among the eight fungal transaldolase‐positive sera tested, three showed IgE binding against the recombinant human transaldolase. To determine cross‐reactivity between the Cladosporium and Penicillium fungi, IgE cross‐reactivity was detected between these two fungal transaldolase allergens by inhibition assays. Both the N‐ and the C‐terminal fragments of Cla c 14.0101 were recognized by IgE antibodies. The C‐terminal IgE‐reacting determinant was narrowed down to a region encompassing Thr257 to Ser278 of Cla c 14.0101. It was mapped onto a loop‐like structure of a 3D model constructed for Cla c 14.0101. Conclusion and Clinical Relevance We identified transaldolase as a novel and IgE cross‐reactive allergen family of C. cladosporioides and P. chrysogenum . In addition, an IgE‐reacting fragment (Thr257 to Ser278) was pinpointed to a loop‐like structure on Cla c 14.0101. Results obtained provide important information in clinical mould allergy. Cite this as : H. Chou, M. F. Tam, C.‐H. Chiang, C.‐T. Chou, H.‐Y. Tai and H.‐D. Shen, Clinical & Experimental Allergy, 2011 (41) 739–749.