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Enteroaggregative Escherichia coli Heat-Stable Enterotoxin 1 (EAST1): A New Toxin with an Old Twist
This review summarizes the various observations on EAST1 since its discovery and proposes as a virulence factor implicated in the mechanism of pathogenesis of EAEC and could play a role in the pathogenicity of other enteropathogens as well.
Actinobacillus pleuropneumoniae surface polysaccharides: their role in diagnosis and immunogenicity
- J. Dubreuil, M. Jacques, K. Mittal, M. Gottschalk
- BiologyAnimal Health Research Reviews
- 1 December 2000
Current knowledge on CPS and LPS of A. pleuropneumoniae used as diagnostic tools to monitor the infection and as immunogens for inclusion in vaccine preparations for animal protection are reviewed.
Production of virulence-related proteins by Canadian strains of Streptococcus suis capsular type 2.
- M. Gottschalk, A. Lebrun, H. Wisselink, J. Dubreuil, H. Smith, U. Vecht
- Biology, MedicineCanadian journal of veterinary research = Revue…
Most Canadian field isolates of S. suis capsular type 2 tested in this study do not produce the virulence-related proteins described so far for this bacterial pathogen.
Identification of a Surface Protein of Streptococcus suis and Evaluation of Its Immunogenic and Protective Capacity in Pigs
The apparent 110-kDa protein, designated Sao, exhibits typical features of membrane-anchored surface proteins of gram-positive bacteria, such as a signal sequence and an LPVTG membrane anchor motif, which suggests its high conservation in S. suis species.
Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis.
- M. Esgleas, Yuanyi Li, M. A. Hancock, J. Harel, J. Dubreuil, M. Gottschalk
- 1 September 2008
The present work is the first study, to the authors' knowledge, to demonstrate a fibronectin-binding activity of a bacterial enolase, and shows that, similar to other bacterial fibronECTin- binding proteins, SsEno may contribute to the virulence of S. suis.
Immunization with Recombinant Sao Protein Confers Protection against Streptococcus suis Infection
It is demonstrated that recombinant Sao formulated with Quil A triggers strong opsonizing antibody responses which confer efficient immunity against challenge infection with heterologous S. suis type 2.
Inactivation of the Pst System Reduces the Virulence of an Avian Pathogenic Escherichia coli O78 Strain
The results suggest that the mutation of pst genes induces a deregulation of phosphate sensing and changes in the cell surface composition that lead to decreased virulence, indicating the importance of the Pst system for the virulence of pathogenic E. coli strains from different hosts.
Helicobacter pylori Interactions with Host Serum and Extracellular Matrix Proteins: Potential Role in the Infectious Process
- J. Dubreuil, G. Giudice, R. Rappuoli
- BiologyMicrobiology and Molecular Biology Reviews
- 1 December 2002
This review examines the binding of host proteins (serum and extracellular matrix proteins) to H. pylori and considers the significance of these interactions in the infectious process and suggests that a more thorough understanding of the kinetics of these receptin interactions could provide a new approach to preventing deeper tissue invasion in H.
Escherichia coli STb toxin and colibacillosis: knowing is half the battle.
- J. Dubreuil
- BiologyFEMS microbiology letters
The effects of STb on the intestinal epithelium is revisits and the significance ofSTb in swine colibacillosis is enlightened as the role of the heat-stable E. coli enterotoxin STb as a diarrhea-causing toxin in animals is revisited.
Animal Enterotoxigenic Escherichia coli.
The disease and pathogenesis of animal ETEC, the corresponding virulence genes and protein products of these bacteria, their regulation and targets in animal hosts, as well as mechanisms of action are described.