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Characterization of the pathogenicity island protein PdpA and its role in the virulence of Francisella novicida

¹ Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada
² Center for Biologics Evaluation and Research, Food and Drug Administration, Rockville, MD, USA

Francisella tularensis is a highly virulent, intracellular pathogen that causes the disease tularaemia. A research surrogate for F. tularensis is Francisella novicida, which causes a tularaemia-like disease in mice, grows similarly in macrophages, and yet is unable to cause disease in humans. Both Francisella species contain a cluster of genes referred to as the Francisella pathogenicity island (FPI). Pathogenicity determinant protein A (PdpA), encoded by the pdpA gene, is located within the FPI and has been associated with the virulence of Francisella species. In this work we examined the properties of PdpA protein expression and localization as well as the phenotype of a F. novicida pdpA deletion mutant. Monoclonal antibody detection of PdpA showed that it is a soluble protein that is upregulated in iron-limiting conditions and undetectable in an mglA or mglB mutant background. Deletion of pdpA resulted in a strain that was highly attenuated for virulence in chicken embryos and mice.

Correspondence
Francis E. Nano
fnano{at}uvic.ca

The GenBank/EMBL/DDBJ accession number for the sequence of the genomic regions in the pdpA deletions is EU810409.

This article has been cited by other articles:

				C. L. Schmerk, B. N. Duplantis, P. L. Howard, and F. E. Nano A Francisella novicida pdpA mutant exhibits limited intracellular replication and remains associated with the lysosomal marker LAMP-1 Microbiology, May 1, 2009; 155(5): 1498 - 1504. [Abstract] [Full Text] [PDF]