Identification of amino acids involved in the Flo11p-mediated adhesion of Saccharomyces cerevisiae to a polystyrene surface using phage display with competitive elution.
OBJECTIVE
To identify the main amino acids involved in the Flo11p-mediated adhesion of Saccharomyces cerevisiae to the polystyrene surface PolySorp.


RESULTS
Using a combination of phage display and competitive elution revealed that 12-mer peptides of phages from competitive panning with S. cerevisiae FLO11 wild-type (TBR1) cells had a higher consensus than those from competitive panning with S. cerevisiae flo11Delta mutant (TBR5) cells, suggesting that the wild-type cells interact with the plastic surface in a stronger and more similar way than the mutant cells. Tryptophan and proline were more abundant in the peptides of phages from competitive elution with FLO11 cells than in those from competitive elution with flo11Delta cells. Furthermore, two phages with hydrophobic peptides containing 1 or 2 tryptophan, and 3 or 5 proline, residues inhibited the adhesion of FLO11 cells to PolySorp more than a phage with a hydrophobic peptide containing no tryptophan and only two proline residues.


CONCLUSIONS
Our results suggest a key role of tryptophan and proline in the hydrophobic interactions between Flo11p on the S. cerevisiae cell surface and the PolySorp surface.


CONCLUSIONS
Our study may contribute to the development of novel strategies to limit yeast infections in hospitals and other medical environments.
Mortensen
H D
HD
Department of Food Science, The Royal Veterinary and Agricultural University, Frederiksberg C, Denmark.
Dupont
K
K
Jespersen
L
L
Willats
W G T
WG
Arneborg
N
N
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis / Q000235:genetics / Q000502:physiology*; D002448:Cell Adhesion / Q000502:physiology; D003470:Culture Media; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D019151:Peptide Library; D011137:Polystyrenes; D011392:Proline / Q000032:analysis / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology*; D014364:Tryptophan / Q000032:analysis / Q000502:physiology
D000596:Amino Acids; D003470:Culture Media; D019151:Peptide Library; D011137:Polystyrenes; D029701:Saccharomyces cerevisiae Proteins; D014364:Tryptophan; D011392:Proline