Description

• Title:
  Extending the aerolysin family: from bacteria to vertebrates.
• Creator:
  Szczesny, Pawel;
  Lacovache, Ioan;
  Muszewska, Anna;
  Ginalski, Krzysztof;
  van der Goot, F Gisou;
  Grynberg, Marcin
• Description:
  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.
• Object availability:
  free access
• Rights:
  cc_by
• Date:
  2011.06.09
• Type:
  Article;
  PeerReviewed
• Language:
  English
• Format:
  application/pdf
• Relation: http://eprints.ibb.waw.pl/144
• Subject:
  QH301 Biology;
  QR180 Immunology
• Identifier: http://eprints.ibb.waw.pl/144/1/journal.pone.0020349.pdf ;
  Szczesny, Pawel and Lacovache, Ioan and Muszewska, Anna and Ginalski, Krzysztof and van der Goot, F Gisou and Grynberg, Marcin (2011) Extending the aerolysin family: from bacteria to vertebrates. PloS one, 6 (6). e20349. ISSN 1932-6203
• Data provider:
  Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk
• Can I use it?:
  check license
• Type:
  other