Discovery of catalases in members of the Chlamydiales order.

Détails

Ressource 1Télécharger: BIB_4529C5542108.P001.pdf (15021.87 [Ko])
Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_4529C5542108
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Discovery of catalases in members of the Chlamydiales order.
Périodique
Journal of Bacteriology
Auteur(s)
Rusconi B., Greub G.
ISSN
1098-5530 (Electronic)
ISSN-L
0021-9193
Statut éditorial
Publié
Date de publication
2013
Peer-reviewed
Oui
Volume
195
Numéro
16
Pages
3543-3551
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov'tPublication Status: ppublish
Résumé
Catalase is an important virulence factor for survival in macrophages and other phagocytic cells. In Chlamydiaceae, no catalase had been described so far. With the sequencing and annotation of the full genomes of Chlamydia-related bacteria, the presence of different catalase-encoding genes has been documented. However, their distribution in the Chlamydiales order and the functionality of these catalases remain unknown. Phylogeny of chlamydial catalases was inferred using MrBayes, maximum likelihood, and maximum parsimony algorithms, allowing the description of three clade 3 and two clade 2 catalases. Only monofunctional catalases were found (no catalase-peroxidase or Mn-catalase). All presented a conserved catalytic domain and tertiary structure. Enzymatic activity of cloned chlamydial catalases was assessed by measuring hydrogen peroxide degradation. The catalases are enzymatically active with different efficiencies. The catalase of Parachlamydia acanthamoebae is the least efficient of all (its catalytic activity was 2 logs lower than that of Pseudomonas aeruginosa). Based on the phylogenetic analysis, we hypothesize that an ancestral class 2 catalase probably was present in the common ancestor of all current Chlamydiales but was retained only in Criblamydia sequanensis and Neochlamydia hartmannellae. The catalases of class 3, present in Estrella lausannensis and Parachlamydia acanthamoebae, probably were acquired by lateral gene transfer from Rhizobiales, whereas for Waddlia chondrophila they likely originated from Legionellales or Actinomycetales. The acquisition of catalases on several occasions in the Chlamydiales suggests the importance of this enzyme for the bacteria in their host environment.
Mots-clé
Amino Acid Sequence, Bacterial Proteins/genetics, Bacterial Proteins/metabolism, Binding Sites, Catalase/classification, Catalase/genetics, Chlamydiales/enzymology, Chlamydiales/genetics, Cloning, Molecular, Epitopes, Gene Expression Regulation, Bacterial/physiology, Gene Expression Regulation, Enzymologic/physiology, Heme/genetics, Heme/metabolism, Models, Molecular, Phylogeny, Protein Binding, Protein Conformation
Pubmed
Web of science
Création de la notice
10/03/2014 17:07
Dernière modification de la notice
20/08/2019 14:49
Données d'usage