Use of synthetic peptides to confirm that the Pseudomonas aeruginosa PAK pilus adhesin and the Candida albicans fimbrial adhesin possess a homologous receptor-binding domain

Authors

  • Lei Yu,

    1. Departments of Medical Microbiology and Immunology,
    2. Canadian Bacterial Diseases Network of Centers of Excellence, University of Alberta, Edmonton, Alberta T6G 2H7, Canada,
    3. Protein Engineering Network of Centres of Excellence,
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  • Kok K. Lee,

    1. Departments of Medical Microbiology and Immunology,
    2. Canadian Bacterial Diseases Network of Centers of Excellence, University of Alberta, Edmonton, Alberta T6G 2H7, Canada,
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  • William Paranchych,

    1. Biological Sciences,
    2. Canadian Bacterial Diseases Network of Centers of Excellence, University of Alberta, Edmonton, Alberta T6G 2H7, Canada,
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  • Robert S. Hodges,

    1. Biochemistry,
    2. Canadian Bacterial Diseases Network of Centers of Excellence, University of Alberta, Edmonton, Alberta T6G 2H7, Canada,
    3. Protein Engineering Network of Centres of Excellence,
    4. SPI Synthetic Peptides Incorporated, 4465–4499 Street, Edmonton, Alberta T6E 5B6, Canada.
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  • Randall T. Irvin

    1. Departments of Medical Microbiology and Immunology,
    2. Canadian Bacterial Diseases Network of Centers of Excellence, University of Alberta, Edmonton, Alberta T6G 2H7, Canada,
    3. Protein Engineering Network of Centres of Excellence,
    4. SPI Synthetic Peptides Incorporated, 4465–4499 Street, Edmonton, Alberta T6E 5B6, Canada.
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Randall T. Irvin E-mail Randy.Irvin@ualberta.ca; Tel. (403) 492 5374; Fax (403) 492 7521.

Abstract

Pseudomonas aeruginosa PAK pili and Candida albicans fimbriae are adhesins present on the microbial cell surfaces which mediate binding to epithelial cell-surface receptors. The receptor-binding domain (adhesintope) of the PAK pilus adhesin has been shown previously to reside in the carboxy-terminal disulphide-bonded region of P. aeruginosa pilin (PAK128-144). The delineation of the C. albicans fimbrial adhesintope was investigated in these studies using synthetic peptides which correspond to the whole (PAK128-144) or part of (PAK134-140) adhesintope of the PAK pilus and their respective anti-peptide antisera and biotinylated PAK pili (Bt-PAK pili), fimbriae (Bt-fimbriae), P. aeruginosa whole cells (Bt-P. aeruginosa) and C. albicans whole cells (Bt-C. albicans). The results from these studies confirmed that a structurally conserved motif akin to the PAK(128-144) peptide sequence is present in C. albicans fimbrial adhesin and that the seven-amino-acid residue PAK(134-140) sequence plays an important role in forming the adhesintope for both P. aeruginosa PAK pilus and C. albicans fimbrial adhesins.

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