Differential clearance and host-pathogen interactions of YopE- and YopK- YopL- Yersinia pestis in BALB/c mice

S C Straley1, M L Cibull

  • 1Department of Microbiology and Immunology, University of Kentucky, Lexington 40536.

Insights

Yersinia pestis virulence plasmids are crucial for Yersinia outer proteins (YOPs) to cause infection. YOPs E, K, and L are essential for bacterial growth in host organs and preventing immune responses.

Area of Science:

  • Microbiology
  • Immunology
  • Pathogenesis

Background:

  • Yersinia pestis causes plague, a severe infectious disease.
  • Virulence factors, including Yersinia outer proteins (YOPs), play a critical role in Y. pestis pathogenesis.
  • The low-Ca2+-response virulence plasmid pCD1 encodes key YOPs.

Purpose of the Study:

  • To characterize the role of YOPs E, K, and L in Y. pestis infection.
  • To investigate the mechanisms by which YOPs contribute to bacterial growth and immune evasion.

Main Methods:

  • Infection of BALB/c mice with wild-type Y. pestis and mutant strains lacking pCD1 or specific YOPs.
  • Monitoring bacterial growth in the liver and spleen.
  • Histopathological examination of infected tissues.
  • Assessment of complement factor C3 binding.

Main Results:

  • Wild-type Y. pestis exhibited rapid growth in the spleen and liver, leading to host death.
  • Mutants lacking YOP E, K, or L showed reduced growth in the spleen but initial growth in the liver.
  • Absence of YOPs E, K, and L led to acute inflammation and granulomatous responses in the liver, indicating cell-mediated immunity.
  • YOP mutants showed only slightly increased C3 binding, suggesting YOPs protect via non-complement-related mechanisms.

Conclusions:

  • YOPs E, K, and L are essential for Y. pestis to achieve sustained growth in the spleen and liver during early infection.
  • These YOPs are critical for suppressing host inflammatory and immune responses, particularly cell-mediated immunity in the liver.
  • YOPs likely confer protection through mechanisms independent of interfering with complement binding.