Saccharomyces cerevisiae--a model to uncover molecular mechanisms for yeast biofilm biology

FEMS Immunol Med Microbiol. 2012 Jul;65(2):169-82. doi: 10.1111/j.1574-695X.2012.00943.x. Epub 2012 Mar 8.

Abstract

Microbial biofilms can be defined as multi-cellular aggregates adhering to a surface and embedded in an extracellular matrix (ECM). The nonpathogenic yeast, Saccharomyces cerevisiae, follows the common traits of microbial biofilms with cell-cell and cell-surface adhesion. S. cerevisiae is shown to produce an ECM and respond to quorum sensing, and multi-cellular aggregates have lowered susceptibility to antifungals. Adhesion is mediated by a family of cell surface proteins of which Flo11 has been shown to be essential for biofilm development. FLO11 expression is regulated via a number of regulatory pathways including the protein kinase A and a mitogen-activated protein kinase pathway. Advanced genetic tools and resources have been developed for S. cerevisiae including a deletion mutant-strain collection in a biofilm-forming strain background and GFP-fusion protein collections. Furthermore, S. cerevisiae biofilm is well applied for confocal laser scanning microscopy and fluorophore tagging of proteins, DNA and RNA. These techniques can be used to uncover the molecular mechanisms for biofilm development, drug resistance and for the study of molecular interactions, cell response to environmental cues, cell-to-cell variation and niches in S. cerevisiae biofilm. Being closely related to Candida species, S. cerevisiae is a model to investigate biofilms of pathogenic yeast.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Biofilms / growth & development*
  • Biomedical Research / methods*
  • Biomedical Research / trends
  • Cell Adhesion
  • Humans
  • Macromolecular Substances / metabolism
  • Membrane Glycoproteins / metabolism
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins / metabolism

Substances

  • FLO11 protein, S cerevisiae
  • Macromolecular Substances
  • Membrane Glycoproteins
  • Saccharomyces cerevisiae Proteins