Purification, identification, and cDNA cloning of Cha o 2, the second major allergen of Japanese cypress pollen

Takeshi Mori, Minehiko Yokoyama, Naoki Komiyama, Mitsuhiro Okano, Kohsuke Kino

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

The second major allergen of Chamaecyparis obtusa (Japanese cypress) pollen, Cha o 2, has been purified and its cDNA cloned. Of patients with pollinosis caused by C. obtusa, 82.5% produce IgE antibodies which react with purified Cha o 2. The purified protein has a molecular mass of 46 kDa and its 12 N-terminal amino acid sequence displays a high homology with that of Cry j 2, the second major allergen of Cryptomeria japonica pollen. cDNA clones coding for Cha o 2 have been isolated using Cry j 2 cDNA as a probe. Cha o 2 cDNA clones were sequenced and found to code a putative 50-residue signal sequence and a 464-residue mature protein with a molecular weight of 50 kDa. Two possible N-linked glycosylation sites were found in the sequence. The deduced amino acid sequence of Cha o 2 shows 74.3% identity with that of Cry j 2. In its primary structure, Cha o 2 shows significant identity with those of the polygalacturonases of avocado, tomato, and maize as well as Cry j 2.

Original languageEnglish
Pages (from-to)166-171
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume263
Issue number1
DOIs
Publication statusPublished - Sep 16 1999

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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