Table of Contents
New Journal of Science
Volume 2014 (2014), Article ID 815102, 12 pages
Review Article

Between Amyloids and Aggregation Lies a Connection with Strength and Adhesion

1Biology Department, Brooklyn College, The City University of New York, 2900 Bedford Avenue, Brooklyn, NY 11210, USA
2The Graduate Center, The City University of New York, New York, NY 10016, USA
3Section of Infectious Diseases, University of Arizona, Tucson, AZ 85724, USA

Received 10 October 2013; Accepted 12 December 2013; Published 2 February 2014

Academic Editor: Yuri L. Lyubchenko

Copyright © 2014 Peter N. Lipke et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


We tell of a journey that led to discovery of amyloids formed by yeast cell adhesins and their importance in biofilms and host immunity. We begin with the identification of the adhesin functional amyloid-forming sequences that mediate fiber formation in vitro. Atomic force microscopy and confocal microscopy show 2-dimensional amyloid “nanodomains” on the surface of cells that are activated for adhesion. These nanodomains are arrays of adhesin molecules that bind multivalent ligands with high avidity. Nanodomains form when adhesin molecules are stretched in the AFM or under laminar flow. Treatment with anti-amyloid perturbants or mutation of the amyloid sequence prevents adhesion nanodomain formation and activation. We are now discovering biological consequences. Adhesin nanodomains promote formation and maintenance of biofilms, which are microbial communities. Also, in abscesses within candidiasis patients, we find adhesin amyloids on the surface of the fungi. In both human infection and a Caenorhabditis elegans infection model, the presence of fungal surface amyloids elicits anti-inflammatory responses. Thus, this is a story of how fungal adhesins respond to extension forces through formation of cell surface amyloid nanodomains, with key consequences for biofilm formation and host responses.