Proteomic identification and characterization of bacterial factors associated with Burkholderia cenocepacia survival in a murine host

• Published in: Microbiology (Society for General Microbiology) Vol. 153; no. 1; pp. 206 - 214
• Main Authors: Chung, Jacqueline W, Speert, David P
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.01.2007; Society for General Microbiology
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Bacteria; Bacterial Proteins - analysis; Bacterial Proteins - metabolism; Bacteriology; Biological and medical sciences; Burkholderia cepacia; Burkholderia cepacia complex - metabolism; Burkholderia cepacia complex - pathogenicity; Burkholderia Infections - microbiology; Disease Models, Animal; Electrophoresis, Gel, Two-Dimensional; Flagellin - analysis; Flagellin - metabolism; Fundamental and applied biological sciences. Psychology; Lung Diseases - microbiology; Mice; Microbiology; Miscellaneous; Peroxidases - analysis; Peroxidases - metabolism; Peroxiredoxins; Proteins; Proteomics; Virulence; Infection; Vertebrata; Mammalia; Mouse; Rodentia; Proteomics; Bacteriosis; Bacteria; Identification; Burkholderia; Survival
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/mic.0.2006/000455-0

Department of Paediatrics, University of British Columbia, Child and Family Research Institute, Vancouver, British Columbia, Canada Correspondence David P. Speert dspeert{at}cw.bc.ca Burkholderia cenocepacia is a member of the Burkholderia cepacia complex, a diverse family of Gram-negative bacteria that are serious respiratory pathogens in immunocompromised patients and individuals with cystic fibrosis. To identify putative bacterial virulence determinants, proteomic profiles were compared between two B. cenocepacia isolates that demonstrated differential persistence in a mouse model of pulmonary infection; clinical isolate C1394 is rapidly cleared from the murine lung whereas the strain variant, C1394mp2, persists. Two-dimensional (2D) gel electrophoresis was used to identify candidate proteins involved in B. cenocepacia survival in a susceptible host. The 2D proteome of the persistent isolate (C1394mp2) revealed loss of an alkyl hydroperoxide reductase subunit C (AhpC) protein spot and increased production of flagellin proteins. Loss of AhpC expression in C1394mp2 correlated with enhanced susceptibility to oxidative stress. C1394mp2 expressed increased flagellin production and enhanced swimming motility, traits that were subject to regulation by heat and low pH. Together, these results revealed differential expression and stress regulation of putative virulence determinants associated with B. cenocepacia persistence in a susceptible host. Abbreviations: AhpC, alkyl hydroperoxide reductase subunit C; ASL, airway surface liquid; BCC, Burkholderia cepacia complex; CF, cystic fibrosis; EPS, exopolysaccharide; IM, inner membrane; OM, outer membrane; RNI, reactive nitrogen intermediates Present address: Department of Microbiology and Immunology, McGill University, Montreal, Quebec, Canada. Present address: Research Institute, Rm 377, 950 West 28th Avenue, Vancouver, BC V5Z 4H4, Canada