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The 40‐kilodalton allergen of Candida albicans is an alcohol dehydrogenase: molecular cloning and immunological analysis using monoclonal antibodies
Author(s) -
SHEN HORNGDER,
CHOO KONGBUNG,
LEE HSIENHSIUNG,
HSIEH JIACHING,
LIN WINLING,
LEE WENRONG,
HAN SHOUHWA
Publication year - 1991
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.1991.tb03195.x
Subject(s) - monoclonal antibody , allergen , biology , microbiology and biotechnology , candida albicans , epitope , molecular cloning , complementary dna , antigen , antibody , biochemistry , immunology , gene , allergy
Summary To characterize the 40‐kilodalton (kD) major allergen of Candida albicans (C. albicans) , six monoclonal antibodies (MoAbs) against this allergen were generated. In SDS‐polyacrylamide gel electrophoresis and immunoblot analysis, these MoAbs showed four different reaction patterns to antigens of six different Candida species. With the exception of one MoAb, other MoAbs were resistant to periodate treatment indicating non‐carbohydrate epitopes were probably being recognized by these MoAbs. These MoAbs were used in the molecular cloning and immunological analysis of the gene coding for the 40‐kD allergen. Nucleotide sequence determination of the two λgtl 1 cDNA clones obtained showed that the 40‐kD allergen is an alcohol dehydrogenase (ADH) which shares a 70% amino acid sequence homology with the ADH isozyme I of Saccharomyces cerevisiae. This finding was confirmed by positive immunological response of the lysates of the clones obtained and a preparation of ADH of Saccharomyces cerevisiae to various MoAbs and to IgE antibodies in sera of allergic patients.