Characterization of Pen n 13, a major allergen from the mold Penicillium notatum

Lu Ping Chow*, Shyh Horng Chiou, Meng Chin Hsiao, Chia Jung Yu, Bor Luen Chiang

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

21 Scopus citations


Penicillium notatum is a well-known indoor aeroallergen and is frequently included in skin test panels for allergic diagnosis. On two-dimensional immunoblotting using patients' sera containing IgE and monoclonal antibody D7B8 specific for Pen c 1 of P. citrinum, two allergens with a molecular mass of 33 kDa but different isoelectric points were identified. A novel cDNA coding for Pen n 13 was cloned and sequenced. The nucleotide sequence codes for a protein 397 amino acids including a putative signal peptide of 25 amino acids and a propeptide of 90 amino acids. The allergen is an alkaline serine protease that shares more than 39% identical residues with other kinds of mold allergens. The coding cDNA of Pen n 13 was cloned into vector pQE-30 and expressed in E. coli M15 as a His-tag fusion protein and purified to homogeneity. The fusion protein reacted with monoclonal antibodies of Pen c 1 and with IgE from Penicillium-allergic patients. Furthermore, it also cross-reacted strongly with IgE specific for the natural Pen c 1, indicating that similar IgE binding epitopes may exist in the allergens of P. notatum and P. citrinum. Antigenicity index plots indicated that there are several similar epitope regions of high antigenic indices in Pen c 1 and Pen n 13, corroborating that mold allergens belonging to the alkaline serine protease family possess similar protein structure and strong antigenic cross-reactivity. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)14-20
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 05 03 2000
Externally publishedYes


  • Alkaline serine protease
  • IgE-binding activity
  • Mold allergens
  • Penicillium notatum


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