Fold modulating function: bacterial toxins to functional amyloids

Many bacteria produce cytolytic toxins that target host cells or other competing microbes. It is well known that environmental factors control toxin expression, however, recent work suggests that some bacteria manipulate the fold of these protein toxins to control their function. The β-sheet rich am...

Full description

Saved in:
Bibliographic Details
Published in:Frontiers in microbiology 2014-08, Vol.5, p.401-401
Main Authors: Syed, Adnan K, Boles, Blaise R
Format: Article
Language:English
Subjects:
Aggregation
bacterial toxin
Bifunctional protein
Biofilm
Functional Amyloid
Microbiology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Many bacteria produce cytolytic toxins that target host cells or other competing microbes. It is well known that environmental factors control toxin expression, however, recent work suggests that some bacteria manipulate the fold of these protein toxins to control their function. The β-sheet rich amyloid fold is a highly stable ordered aggregate that many toxins form in response to specific environmental conditions. When in the amyloid state, toxins become inert, losing the cytolytic activity they display in the soluble form. Emerging evidence suggest that some amyloids function as toxin storage systems until they are again needed, while other bacteria utilize amyloids as a structural matrix component of biofilms. This amyloid matrix component facilitates resistance to biofilm disruptive challenges. The bacterial amyloids discussed in this review reveal an elegant system where changes in protein fold and solubility dictate the function of proteins in response to the environment.
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2014.00401