小兒科CHOW, Lu-PingLu-PingCHOWSU, Ning-YuanNing-YuanSUYU, Chia-JungChia-JungYUCHIANG, Bor-LuenBor-LuenCHIANGSHEN, Horng-DerHorng-DerSHEN2008-12-292018-07-112008-12-292018-07-111999http://ntur.lib.ntu.edu.tw//handle/246246/94896The mould genus, Penicillium, is known to be a significant source of environmental aero-allergens. One important allergen from Penicillium citrinum, Pen c 2, has been identified by means of two-dimensional immunoblotting using IgE-containing patients' sera. This novel allergen was cloned, sequenced and expressed in Escherichia toll. The cloned cDNA encodes a large 457-amino acid protein precursor containing a 16-amino acid signal peptide, a 120-amino acid propeptide and the 321-amino acid mature protein. Comparison of the Pen c 2 sequence with known protein sequences revealed shared high sequence similarities with two vacuolar serine proteases from Aspergillus niger and Saccharomyces cerevisiae. Asp- 36, His-78 and Ser-244 were found to constitute the catalytic triad of the 39-kDa Pen c 2, The DNA coding for Pen c 2 was cloned into vector PQE-30 and expressed in E. coli as a His-tag fusion protein that bound serum IgE from Penicillium-allergic patients on immunoblots, Recombinant Pen c 2 could therefore be used effectively for diagnosis and also potentially for the treatment of mould-derived allergic disorders.en-USallergycDNA cloningIgE-binding activitymould allergensvacuolar serine proteaseGROUP-III ALLERGENjournal article