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DsbA is required for stable expression of outer membrane protein YscC and for efficient Yop secretion in Yersinia

M W Jackson1, G V Plano

  • 1Department of Microbiology and Immunology, University of Miami School of Medicine, Miami, Florida 33176, USA.

Journal of Bacteriology
|August 10, 1999
PubMed

Insights

The periplasmic disulfide oxidoreductase DsbA is crucial for Yersinia pestis virulence. DsbA and YscC protein disulfide bonds are essential for Yop secretion and V antigen export.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Yersinia pestis is a Gram-negative bacterium responsible for plague.
  • Yop secretion is mediated by a type III secretion system (T3SS).
  • The periplasmic disulfide oxidoreductase DsbA is involved in protein folding and secretion.

Purpose of the Study:

  • To investigate the role of DsbA in Yop secretion in Yersinia pestis.
  • To determine if disulfide bonds in YscC are essential for Yop secretion.

Main Methods:

  • Construction and analysis of a Y. pestis dsbA mutant.
  • Site-directed mutagenesis of cysteine residues in YscC.
  • Assessment of V antigen and Yop secretion levels.
  • Analysis of YscC protein expression.

Main Results:

  • A dsbA mutant exhibited reduced secretion of V antigen and Yops.
  • The dsbA mutant showed reduced expression of full-sized YscC.
  • Mutagenesis of YscC cysteine residues mimicked the dsbA mutant phenotype.
  • These findings indicate YscC requires disulfide bonds for function.

Conclusions:

  • DsbA plays a significant role in Yop secretion in Yersinia pestis.
  • Disulfide bonds within YscC are critical for its function in the T3SS.
  • The DsbA-mediated disulfide bond formation in YscC is essential for Yop secretion.

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