Biochemical, Structural and Molecular Dynamics Analyses of the Potential Virulence Factor RipA from Yersinia pestis
2011

Study of RipA Protein from Yersinia pestis

publication 10 minutes Evidence: moderate

Author Information

Author(s): Rodrigo Torres, Robert V. Swift, Nicholas Chim, Nicole Wheatley, Benson Lan, Brian R. Atwood, Céline Pujol, Banu Sankaran, James B. Bliska, Rommie E. Amaro, Celia W. Goulding

Primary Institution: University of California Irvine

Hypothesis

The end product of the rip operon is butyrate, which lowers nitric oxide levels in macrophages.

Conclusion

The study provides insights into the structure and function of RipA, suggesting it plays a role in lowering nitric oxide levels in macrophages, potentially aiding Yersinia pestis survival.

Supporting Evidence

  • RipA is essential for Yersinia pestis replication in macrophages.
  • The rip operon is conserved among several pathogenic bacteria.
  • RipA exhibits a unique tetrameric structure.
  • Molecular dynamics simulations suggest a gating mechanism for substrate binding.

Takeaway

This study looks at a protein from a germ that causes plague, showing how it helps the germ survive in our body's immune cells by lowering harmful substances.

Methodology

The study involved biochemical assays, structural analysis through X-ray crystallography, and molecular dynamics simulations.

Digital Object Identifier (DOI)

10.1371/journal.pone.0025084

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