Purification, characterization and molecular cloning of Cha o 1, a major allergen of Chamaecyparis obtusa (Japanese cypress) pollen
1996; Elsevier BV; Volume: 33; Issue: 4-5 Linguagem: Inglês
10.1016/0161-5890(95)00147-6
ISSN1872-9142
AutoresMotohiko Suzuki, Naoki Komiyama, Makoto Itoh, Hirotaka Itoh, Toshio Sone, Kohsuke Kino, Ippei Takagi, Nobuo Ohta,
Tópico(s)Antimicrobial Peptides and Activities
ResumoPollen of Chamaecyparis obtusa (Japanese cypress) is one of the causes of allergic pollinosis in Japan. A major allergen of the pollen designated Cha o 1, was purified by two-step ion exchange chromatography. Cha o 1 was separated into four components with molecular masses of 48.5 kDa and 52.0 kDa, each with pIs of 6.77 and 6.82. The 23-residue N-terminal sequence of Cha o 1 was determined and shown to have high identity with that of Cry j 1, a major allergen of Cryptomeria japonica pollen. cDNA coding for Cha o 1 was cloned by hybridization screening using Cry j 1 cDNA as a probe. One of the cDNA clones, pCHA-1 was sequenced and found to code for a putative 21-residue signal peptide and a 354-residue native protein with a derived molecular mass of 38.1 kDa. The deduced amino acid sequence of Cha o 1 showed 79-80% identity with those of Cry j 1. These findings were consistent with observations of a close crossreaction between the two allergens. Homology analyses revealed that Cha o 1 had 46-49% identity with Amb a 1 families and Amb a 2, the major allergens of short ragweed. Cry j 1 has pectate lyase enzyme activity, suggesting that Cha o 1 may have the same enzyme activity as Cry j 1.
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