Literature DB >> 1777830

The 40-kilodalton allergen of Candida albicans is an alcohol dehydrogenase: molecular cloning and immunological analysis using monoclonal antibodies.

H D Shen1, K B Choo, H H Lee, J C Hsieh, W L Lin, W R Lee, S H Han.   

Abstract

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 lambda gt11 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.

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Year:  1991        PMID: 1777830     DOI: 10.1111/j.1365-2222.1991.tb03195.x

Source DB:  PubMed          Journal:  Clin Exp Allergy        ISSN: 0954-7894            Impact factor:   5.018


  15 in total

1.  Identification of Immunoglobulin E-Binding Proteins of the Xerophilic Fungus Aspergillus penicillioides Crude Mycelial Mat Extract and Serological Reactivity Assessment in Subjects with Different Allergen Reactivity Profiles.

Authors:  Joenice González De León; Ricardo González Méndez; Carmen L Cadilla; Félix E Rivera-Mariani; Benjamín Bolaños-Rosero
Journal:  Int Arch Allergy Immunol       Date:  2018-02-03       Impact factor: 2.749

Review 2.  Cell wall and secreted proteins of Candida albicans: identification, function, and expression.

Authors:  W L Chaffin; J L López-Ribot; M Casanova; D Gozalbo; J P Martínez
Journal:  Microbiol Mol Biol Rev       Date:  1998-03       Impact factor: 11.056

Review 3.  The relationships between the biochemical properties of allergens and their immunogenicity.

Authors:  T Musu; C Grégoire; B David; J P Dandeu
Journal:  Clin Rev Allergy Immunol       Date:  1997       Impact factor: 8.667

4.  The cell wall-associated glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is also a fibronectin and laminin binding protein.

Authors:  D Gozalbo; I Gil-Navarro; I Azorín; J Renau-Piqueras; J P Martínez; M L Gil
Journal:  Infect Immun       Date:  1998-05       Impact factor: 3.441

5.  Allergen nomenclature. IUIS/WHO Allergen Nomenclature Subcommittee.

Authors: 
Journal:  Bull World Health Organ       Date:  1994       Impact factor: 9.408

Review 6.  Serologic response to cell wall mannoproteins and proteins of Candida albicans.

Authors:  J P Martínez; M L Gil; J L López-Ribot; W L Chaffin
Journal:  Clin Microbiol Rev       Date:  1998-01       Impact factor: 26.132

7.  Detection of candidal antigens in autoimmune polyglandular syndrome type I.

Authors:  P Peterson; J Perheentupa; K J Krohn
Journal:  Clin Diagn Lab Immunol       Date:  1996-05

8.  The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen.

Authors:  I Gil-Navarro; M L Gil; M Casanova; J E O'Connor; J P Martínez; D Gozalbo
Journal:  J Bacteriol       Date:  1997-08       Impact factor: 3.490

9.  Glycolytic enzymes of Candida albicans are nonubiquitous immunogens during candidiasis.

Authors:  R K Swoboda; G Bertram; H Hollander; D Greenspan; J S Greenspan; N A Gow; G W Gooday; A J Brown
Journal:  Infect Immun       Date:  1993-10       Impact factor: 3.441

10.  Expression of surface hydrophobic proteins by Candida albicans in vivo.

Authors:  P M Glee; P Sundstrom; K C Hazen
Journal:  Infect Immun       Date:  1995-04       Impact factor: 3.441

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