A role for amyloid in cell aggregation and biofilm formation.

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 subst...

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Autores principales:	Melissa C Garcia, Janis T Lee, Caleen B Ramsook, David Alsteens, Yves F Dufrêne, Peter N Lipke
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/19133788e2fa4d24be8b67f7deab60de
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spelling	oai:doaj.org-article:19133788e2fa4d24be8b67f7deab60de2021-11-18T06:57:40ZA role for amyloid in cell aggregation and biofilm formation.1932-620310.1371/journal.pone.0017632https://doaj.org/article/19133788e2fa4d24be8b67f7deab60de2011-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21408122/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Cell 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.Melissa C GarciaJanis T LeeCaleen B RamsookDavid AlsteensYves F DufrênePeter N LipkePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 3, p e17632 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Melissa C Garcia Janis T Lee Caleen B Ramsook David Alsteens Yves F Dufrêne Peter N Lipke A role for amyloid in cell aggregation and biofilm formation.
description	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.
format	article
author	Melissa C Garcia Janis T Lee Caleen B Ramsook David Alsteens Yves F Dufrêne Peter N Lipke
author_facet	Melissa C Garcia Janis T Lee Caleen B Ramsook David Alsteens Yves F Dufrêne Peter N Lipke
author_sort	Melissa C Garcia
title	A role for amyloid in cell aggregation and biofilm formation.
title_short	A role for amyloid in cell aggregation and biofilm formation.
title_full	A role for amyloid in cell aggregation and biofilm formation.
title_fullStr	A role for amyloid in cell aggregation and biofilm formation.
title_full_unstemmed	A role for amyloid in cell aggregation and biofilm formation.
title_sort	role for amyloid in cell aggregation and biofilm formation.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/19133788e2fa4d24be8b67f7deab60de
work_keys_str_mv	AT melissacgarcia aroleforamyloidincellaggregationandbiofilmformation AT janistlee aroleforamyloidincellaggregationandbiofilmformation AT caleenbramsook aroleforamyloidincellaggregationandbiofilmformation AT davidalsteens aroleforamyloidincellaggregationandbiofilmformation AT yvesfdufrene aroleforamyloidincellaggregationandbiofilmformation AT peternlipke aroleforamyloidincellaggregationandbiofilmformation AT melissacgarcia roleforamyloidincellaggregationandbiofilmformation AT janistlee roleforamyloidincellaggregationandbiofilmformation AT caleenbramsook roleforamyloidincellaggregationandbiofilmformation AT davidalsteens roleforamyloidincellaggregationandbiofilmformation AT yvesfdufrene roleforamyloidincellaggregationandbiofilmformation AT peternlipke roleforamyloidincellaggregationandbiofilmformation
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A role for amyloid in cell aggregation and biofilm formation.

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