Comparative analysis of type III effector translocation by Yersinia pseudotuberculosis expressing native LcrV or PcrV

Jeanette E Bröms1, Charlotta Sundin, Matthew S Francis

  • 1Department of Molecular Biology, Umeå University, Umeå, Sweden.

Insights

Pseudomonas aeruginosa PcrV forms smaller pores than Yersinia LcrV, reducing effector translocation. A complete PcrV complex with native components is necessary for functional pore formation and effector delivery in Yersinia.

Area of Science:

  • Microbiology and Immunology
  • Bacterial Pathogenesis
  • Molecular Biology

Background:

  • LcrV (Yersinia species) and PcrV (Pseudomonas aeruginosa) are homologous pore-forming proteins crucial for bacterial virulence.
  • Differences in pore formation between LcrV and PcrV affect the translocation of bacterial effector proteins into host cells.

Purpose of the Study:

  • To investigate the functional differences between LcrV and PcrV in Yersinia.
  • To determine the role of native translocon components in PcrV-mediated pore formation and effector translocation.

Main Methods:

  • Expressing PcrV in a Yersinia lcrV background and comparing pore size and effector translocation with native LcrV.
  • Introducing P. aeruginosa exoenzyme S and Yersinia YopE into Yersinia strains expressing LcrV or PcrV.
  • Analyzing effector translocation into HeLa cells and pore formation in erythrocyte membranes.

Main Results:

  • PcrV in a Yersinia background formed smaller pores than LcrV, leading to reduced Yersinia effector translocation.
  • Substrate recognition by LcrV/PcrV was not the primary regulator of effector translocation.
  • Yersinia expressing pcrV along with its native operon components efficiently translocated effectors and formed large pores.

Conclusions:

  • The PcrV complex, when reconstituted with native Pseudomonas aeruginosa translocon components, forms fully functional pores.
  • This functional PcrV complex can complement effector translocation in Yersinia, highlighting the importance of the complete translocon structure.