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PLoS One. 2011;6(6):e20349. doi: 10.1371/journal.pone.0020349. Epub 2011 Jun 8.

Extending the aerolysin family: from bacteria to vertebrates.

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1
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.

Abstract

A number of bacterial virulence factors have been observed to adopt structures similar to that of aerolysin, the principal toxin of Aeromonas species. However, a comprehensive description of architecture and structure of the aerolysin-like superfamily has not been determined. In this study, we define a more compact aerolysin-like domain--or aerolysin fold--and show that this domain is far more widely spread than anticipated since it can be found throughout kingdoms. The aerolysin-fold could be found in very diverse domain and functional contexts, although a toxic function could often be assigned. Due to this diversity, the borders of the superfamily could not be set on a sequence level. As a border-defining member, we therefore chose pXO2-60--a protein from the pathogenic pXO2 plasmid of Bacillus anthracis. This fascinating protein, which harbors a unique ubiquitin-like fold domain at the C-terminus of the aerolysin-domain, nicely illustrates the diversity of the superfamily. Its putative role in the virulence of B. anthracis and its three dimensional model are discussed.

PMID:
21687664
PMCID:
PMC3110756
DOI:
10.1371/journal.pone.0020349
[Indexed for MEDLINE]
Free PMC Article
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