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Identification of Yersinia pestis Pigment Receptor

  • Olga N. Podladchikova
  • Grigory G. Dikhanov
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 529)

Conclusions

In the present work the PR of Y. pestis was identified as a complex of a 17 kDa protein associated with two oppositely charged low molecular weight components that cooperatively form a pigment binding domain of PR. The pigment binding activity of PR is dependent on an appropriate proportion of the low molecular weight components and on the absence of the pigmentation inhibitor.

Keywords

Ammonium Sulfate Yersinia Pestis High Molecular Weight Fraction Pigment Binding Binding Mutation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Hare, J. M., and McDonough, K. A., 1999, High-freguency RecA-dependent and independent mechanisms of Congo red binding mutations in Yersinia pestis. J. Bacteriol. 181: 4896–4904.PubMedGoogle Scholar
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  3. Jones, H. A., Lillard, J. W., and Perry, R. D., 1999, HmsT, a protein essential for expression of the haemin storage (Hms+) phenotype of Yersinia pestis. Microbiology 145: 2117–2128.PubMedGoogle Scholar
  4. Podladchikova, O. N., Rykova, V. A., Ivanova, V. S., Eremenko, N. S., and Lebedeva, S. A., 2002, Study of Pgm mutation mechanism in Yersinia pestis vaccine strain EV76. Mol. Genet., Microbiol., Virusol. (Russian). 2: 14–19.Google Scholar

Copyright information

© Kluwer Academic Publishers 2004

Authors and Affiliations

  • Olga N. Podladchikova
    • 1
  • Grigory G. Dikhanov
    • 1
  1. 1.Research Institute for Plague ControlRostov-on DonRussia

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