Abstract:
: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.
journal_name
Front Microbioljournal_title
Frontiers in microbiologyauthors
Syed AK,Boles BRdoi
10.3389/fmicb.2014.00401subject
Has Abstractpub_date
2014-08-01 00:00:00pages
401issn
1664-302Xjournal_volume
5pub_type
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pub_type: 杂志文章
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journal_title:Frontiers in microbiology
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pub_type: 杂志文章,评审
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abstract::[This corrects the article DOI: 10.3389/fmicb.2019.03123.]. ...
journal_title:Frontiers in microbiology
pub_type: 已发布勘误
doi:10.3389/fmicb.2020.00325
更新日期:2020-02-25 00:00:00