Purification, characterization and molecular cloning of Cha o 1, a major allergen of Chamaecyparis obtusa (Japanese cypress) pollen

被引:56
作者
Suzuki, M
Komiyama, N
Itoh, M
Itoh, H
Sone, T
Kino, K
Takagi, I
Ohta, N
机构
[1] MEIJI INST HLTH SCI,ODAWARA 250,JAPAN
[2] NAGOYA CITY UNIV,SCH MED,DEPT MED ZOOL,NAGOYA,AICHI 467,JAPAN
关键词
Chamaecyparis obtusa; Cha o 1; cDNA cloning; major allergen;
D O I
10.1016/0161-5890(95)00147-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Pollen 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 Cryj 1, a major allergen of Cryptomeria japonica pollen. cDNA coding for Cha o 1 was cloned by hybridization screening using Cryj 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 Cryj 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. Cryj 1 has pectate lyase enzyme activity, suggesting that Cha o 1 may have the same enzyme activity as Cryj 1. Copyright (C) 1996 Elsevier Science Ltd.
引用
收藏
页码:451 / 460
页数:10
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