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 Kok K Lee William Paranchych Robert S Hodges & Randall T Irvin |
| |
| Institution: | Departments of Medical Microbiology and Immunology,;Biological Sciences,;Biochemistry,;Canadian Bacterial Diseases Network of Centers of Excellence, University of Alberta, Edmonton, Alberta T6G 2H7, Canada,;Protein Engineering Network of Centres of Excellence,;SPI Synthetic Peptides Incorporated, 4465–4499 Street, Edmonton, Alberta T6E 5B6, Canada. |
| |
| 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. |
| |
| Keywords: | |
|
|
