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Science 6 November 1992:
Vol. 258. no. 5084, pp. 1004 - 1007
DOI: 10.1126/science.1439793

Articles

Science, Vol 258, Issue 5084, 1004-1007
Copyright © 1992 by American Association for the Advancement of Science


articles

A surface protease and the invasive character of plague

OA Sodeinde, YV Subrahmanyam, K Stark, T Quan, Y Bao, and JD Goguen

Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655.

A 9.5-kilobase plasmid of Yersinia pestis, the causative agent of plague, is required for high virulence when mice are inoculated with the bacterium by subcutaneous injection. Inactivation of the plasmid gene pla, which encodes a surface protease, increased the median lethal dose of the bacteria for mice by a millionfold. Moreover, cloned pla was sufficient to restore segregants lacking the entire pla-bearing plasmid to full virulence. Both pla+ strains injected subcutaneously and pla- mutants injected intravenously reached high titers in liver and spleen of infected mice, whereas pla- mutants injected subcutaneously failed to do so even though they establish a sustained local infection at the injection site. More inflammatory cells accumulated in lesions caused by the pla- mutants than in lesions produced by the pla+ parent. The Pla protease was shown to be a plasminogen activator with unusual kinetic properties. It can also cleave complement C3 at a specific site.


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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »
Expression of Plasminogen Activator Pla of Yersinia pestis Enhances Bacterial Attachment to the Mammalian Extracellular Matrix.
K. Lahteenmaki, R. Virkola, A. Saren, L. Emody, and T. K. Korhonen (1998)
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   Abstract »    Full Text »    PDF »
Identification of Two Laminin-Binding Fimbriae, the Type 1 Fimbria of Salmonella enterica Serovar Typhimurium and the G Fimbria of Escherichia coli, as Plasminogen Receptors.
M. Kukkonen, S. Saarela, K. Lahteenmaki, U. Hynonen, B. Westerlund-Wikstrom, M. Rhen, and T. K. Korhonen (1998)
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   Abstract »    Full Text »    PDF »
YscO of Yersinia pestis Is a Mobile Core Component of the Yop Secretion System.
P. L. Payne and S. C. Straley (1998)
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Type III Protein Secretion Systems in Bacterial Pathogens of Animals and Plants.
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Molecular Co-operation between Protein PAM and Streptokinase for Plasmin Acquisition by Streptococcus pyogenes.
U. Ringdahl, M. Svensson, A. C. Wistedt, T. Renne, R. Kellner, W. Muller-Esterl, and U. Sjobring (1998)
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   Abstract »    Full Text »    PDF »
Convergent evolution of apolipoprotein(a) in primates and hedgehog.
R. M. Lawn, K. Schwartz, and L. Patthy (1997)
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