Format

Send to

Choose Destination
PLoS One. 2011 Mar 8;6(3):e17632. doi: 10.1371/journal.pone.0017632.

A role for amyloid in cell aggregation and biofilm formation.

Author information

1
Biology Department, Brooklyn College of the City University of New York, Brooklyn, New York, United States of America.

Abstract

Cell adhesion molecules in Saccharomyces cerevisiae and Candida albicans contain amyloid-forming sequences that are highly conserved. We have now used site-specific mutagenesis and specific peptide perturbants to explore amyloid-dependent activity in the Candida albicans adhesin Als5p. A V326N substitution in the amyloid-forming region conserved secondary structure and ligand binding, but abrogated formation of amyloid fibrils in soluble Als5p and reduced cell surface thioflavin T fluorescence. When displayed on the cell surface, Als5p with this substitution prevented formation of adhesion nanodomains and formation of large cellular aggregates and model biofilms. In addition, amyloid nanodomains were regulated by exogenous peptides. An amyloid-forming homologous peptide rescued aggregation and biofilm activity of Als5p(V326N) cells, and V326N substitution peptide inhibited aggregation and biofilm activity in Als5p(WT) cells. Therefore, specific site mutation, inhibition by anti-amyloid peturbants, and sequence-specificity of pro-amyloid and anti-amyloid peptides showed that amyloid formation is essential for nanodomain formation and activation.

PMID:
21408122
PMCID:
PMC3050909
DOI:
10.1371/journal.pone.0017632
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Public Library of Science Icon for PubMed Central
Loading ...
Support Center