title: Extending the aerolysin family: from bacteria to vertebrates.
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.
authors.affiliation: Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
authors.forename: Pawel
authors.initials: P
authors.lastname: Szczesny
authors.forename: Ioan
authors.initials: I
authors.lastname: Iacovache
authors.forename: Anna
authors.initials: A
authors.lastname: Muszewska
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Ginalski
authors.forename: F Gisou
authors.initials: FG
authors.lastname: van der Goot
authors.forename: Marcin
authors.initials: M
authors.lastname: Grynberg
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism*; D017124:Conserved Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D052899:Pore Forming Cytotoxic Proteins / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013045:Species Specificity; D014714:Vertebrates
chemical_list: D001427:Bacterial Toxins; D052899:Pore Forming Cytotoxic Proteins; C032676:aerolysin