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Published online ahead of print on 16 April 2009 as doi:10.1099/mic.0.025379-0
Microbiology 2009;155:1489.

Microbiology (2009), DOI 10.1099/mic.0.025379-0
© 2009 Society for General Microbiology

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Microbiology 0 (2009), mic.0.025379; DOI  10.1099/mic.0.025379-0
© 2009 Society for General Microbiology


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

C. L. Schmerk1, B. N. Duplantis1, D. Wang1, R. D. Burke1, A. Y. Chou2, K. L. Elkins2, J. S. Ludu1 and F. E. Nano1,3

1 University of Victoria;
2 Food and Drug Administration

ABSTRACT

Francisella tularensis is a highly virulent, intracellular pathogen which causes the disease tularemia. A research surrogate for F. tularensis is F. novicida, which causes a tularemia-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, 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.

3 E-mail: fnano{at}uvic.ca




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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]




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