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In silico Identification of Novel Toxin Homologs and Associated Mobile Genetic Elements in Clostridium perfringens

Authors
  • Lacey, Jake A.1, 2
  • Johanesen, Priscilla A.1
  • Lyras, Dena1
  • Moore, Robert J.1, 3
  • 1 (D.L.)
  • 2 Department of Doherty, The Peter Doherty Institute for Infection and Immunology, University of Melbourne, Victoria 3000, Australia
  • 3 School of Science, RMIT University, Bundoora, Victoria 3083, Australia
Type
Published Article
Journal
Pathogens
Publisher
MDPI
Publication Date
Jan 29, 2019
Volume
8
Issue
1
Identifiers
DOI: 10.3390/pathogens8010016
PMID: 30699957
PMCID: PMC6471305
Source
PubMed Central
Keywords
License
Green

Abstract

Clostridium perfringens causes a wide range of diseases in a variety of hosts, due to the production of a diverse set of toxins and extracellular enzymes. The C. perfringens toxins play an important role in pathogenesis, such that the presence and absence of the toxins is used as a typing scheme for the species. In recent years, several new toxins have been discovered that have been shown to be essential or highly correlated to diseases; these include binary enterotoxin (BecAB), NetB and NetF. In the current study, genome sequence analysis of C. perfringens isolates from diverse sources revealed several putative novel toxin homologs, some of which appeared to be associated with potential mobile genetic elements, including transposons and plasmids. Four novel toxin homologs encoding proteins related to the pore-forming Leukocidin/Hemolysin family were found in type A and G isolates. Two novel toxin homologs encoding proteins related to the epsilon aerolysin-like toxin family were identified in Type A and F isolates from humans, contaminated food and turkeys. A novel set of proteins related to clostridial binary toxins was also identified. While phenotypic characterisation is required before any of these homologs can be established as functional toxins, the in silico identification of these novel homologs on mobile genetic elements suggests the potential toxin reservoir of C. perfringens may be much larger than previously thought.

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