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yopE  -  YopE

Yersinia enterocolitica

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Disease relevance of yopE


High impact information on yopE

  • These activities are consistent with previously proposed or demonstrated effects on higher eukaryotes and provide new insights into the roles of these proteins in pathogenesis: SspA in directing formation of membrane ruffles and YopE in arresting cell division [6].
  • YopHC403S stabilized focal adhesions, as shown by its dominant-negative effect on focal adhesion disassembly mediated by YopE, a translocated protein which disrupts actin stress fibers [7].
  • Treatment of HeLa cells with cytochalasin D prior to infection prevented internalization of bacteria, but translocation of YopE was still observed [2].
  • YopE was detected in the cytosol of the infected HeLa cells and the amount of translocated YopE correlated with the degree of cytotoxicity [2].
  • These results favour the hypothesis that YopE is translocated through the plasma membrane by surface-located bacteria [2].

Chemical compound and disease context of yopE

  • When bound to SycE chaperone in the Yersinia cytoplasm, YopE residues 1-100 are necessary and sufficient for the targeting of hybrid neomycin phosphotransferase [8].
  • YopD, the 33-kDa product of the lcrGVHyopBD operon, appears to be involved in delivering YopE and YopH (the Yersinia protein tyrosine phosphatase) into target cells [9].

Biological context of yopE

  • Systematic mutagenesis of yopE codons 1 to 7 reveals that, like yopQ, codons 2, 3, 5, and 7 are sensitive to mutagenesis, thereby defining the first empirical similarity between the secretion signals of two type III secreted substrates [10].
  • When introduced into the context of the full-length yopE gene, the single-nucleotide mutation reduces the type III injection of YopE into HeLa cells, even though the predicted amino acid sequence remains the same [10].
  • In contrast, a mutant no longer making YopE or YopH (a tyrosine phosphatase) induces apoptosis in macrophages similar to wild type [11].
  • SycE, a compact, globular dimer with a novel fold, has two large hydrophobic surface patches that may form binding sites for YopE or other type III components [12].
  • Pathogenic Yersinia enterocolitica produces two virulence plasmid-encoded cytotoxins, YopE and YopT, that are translocated into target cells where they disrupt the actin cytoskeleton [13].

Anatomical context of yopE

  • To understand the functional role of YopE, in vivo studies of the GAP activity in infected eukaryotic cells were conducted [14].
  • After oral inoculation of mice, Yersinia pseudotuberculosis yopE and yopH mutants colonize the intestines and Peyer's patches in single-strain infections but fail to persist in competition with wild-type Y. pseudotuberculosis, indicating that these two infection models provide different insights into the roles of Yops [15].
  • Translocation of YopE and YopH across host cell's membranes was also dependent on the secretion of YopB and YopD by the same bacterium [16].
  • YopE and YopT contribute to antiphagocytic effects by inactivating GTPases controlling cytoskeleton dynamics [17].
  • Upon infection of cultured epithelial cells, extracellular Yersinia pseudotuberculosis and Yersinia enterocolitica translocate cytotoxin YopE across the host cell plasma membrane [16].

Associations of yopE with chemical compounds

  • Conversely, YopH destabilized focal adhesions, even in the absence of YopE, as shown by loss of phosphotyrosine staining [7].
  • As compared with wild-type SycE, glutathione S-transferase-SycE bound and stabilized YopE in the bacterial cytoplasm but failed to release the polypeptide for export by the type III machinery [18].
  • YopE has an arginine finger motif showing homology with those found in other GAP proteins [19].
  • The results demonstrate that amphipathic N-terminal sequences, containing four or five serine residues, have a much greater probability than hydrophobic or hydrophilic sequences to target YopE for secretion [20].
  • Exchange of arginine 144 with alanine, located in this arginine finger motif, results in an inactive form of YopE that can no longer stimulate GTP hydrolysis by the GTPase [19].

Other interactions of yopE

  • Like that of yopQ, the secretion signal of yopE exhibits a bipartite nature [10].
  • Finally, competition infections with Y. pseudotuberculosis mutants with various abilities to induce inflammation demonstrated that survival of the yopE, but not the yopH, mutant was consistently decreased in inflamed tissues [15].

Analytical, diagnostic and therapeutic context of yopE

  • Bacterial mutants defective in their ability to express YopE are avirulent after oral or intraperitoneal infection but virulent following intravenous injection [21].
  • Immunofluorescence localization revealed that YopM, in contrast to YopE, is not only targeted to the cytoplasm but also trafficks to the cell's nucleus by means of a vesicle-associated pathway that is strongly inhibited by brefeldin A, perturbed by monensin or bafilomycin A1 and dependent upon microtubules (decreased by colchicine and nocodazole) [22].
  • Immunogold electron microscopy on cryosectioned Y. pseudotuberculosis revealed that YopE is secreted and deposited on the bacterial cell surface when the bacteria are grown in Ca(2+)-depleted media at 37 degrees C. No YopE was detected in the cytoplasm or in the membranes [23].
  • J774A.1 cells were infected with Y. pestis KIM5 in the presence of a protective polyclonal anti-LcrV antibody or a nonprotective polyclonal anti-YopM antibody, and delivery of YopH and YopE into the cytoplasm was assayed by immunoblotting [24].
  • In this study, we compared the localization of LcrV to that of the targeted proteins YopE and YopM by immunoblot analysis of fractions of Yersinia-infected HeLa cultures or by laser-scanning confocal microscopy of infected monolayers [25].


  1. Temperature sensing in Yersinia pestis: regulation of yopE transcription by lcrF. Hoe, N.P., Minion, F.C., Goguen, J.D. J. Bacteriol. (1992) [Pubmed]
  2. Functional conservation of the secretion and translocation machinery for virulence proteins of yersiniae, salmonellae and shigellae. Rosqvist, R., Håkansson, S., Forsberg, A., Wolf-Watz, H. EMBO J. (1995) [Pubmed]
  3. Intracellular membrane localization of pseudomonas ExoS and Yersinia YopE in mammalian cells. Krall, R., Zhang, Y., Barbieri, J.T. J. Biol. Chem. (2004) [Pubmed]
  4. Protection against murine listeriosis by oral vaccination with recombinant Salmonella expressing hybrid Yersinia type III proteins. Rüssmann, H., Igwe, E.I., Sauer, J., Hardt, W.D., Bubert, A., Geginat, G. J. Immunol. (2001) [Pubmed]
  5. The Yersinia Yops inhibit invasion of Listeria, Shigella and Edwardsiella but not Salmonella into epithelial cells. Mecsas, J., Raupach, B., Falkow, S. Mol. Microbiol. (1998) [Pubmed]
  6. Expression of microbial virulence proteins in Saccharomyces cerevisiae models mammalian infection. Lesser, C.F., Miller, S.I. EMBO J. (2001) [Pubmed]
  7. Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. Black, D.S., Bliska, J.B. EMBO J. (1997) [Pubmed]
  8. Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: one-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone. Lee, V.T., Anderson, D.M., Schneewind, O. Mol. Microbiol. (1998) [Pubmed]
  9. Contribution of YopB to virulence of Yersinia enterocolitica. Hartland, E.L., Bordun, A.M., Robins-Browne, R.M. Infect. Immun. (1996) [Pubmed]
  10. A synonymous mutation in Yersinia enterocolitica yopE affects the function of the YopE type III secretion signal. Ramamurthi, K.S., Schneewind, O. J. Bacteriol. (2005) [Pubmed]
  11. Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for this cell death. Monack, D.M., Mecsas, J., Ghori, N., Falkow, S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  12. Structure of the Yersinia type III secretory system chaperone SycE. Birtalan, S., Ghosh, P. Nat. Struct. Biol. (2001) [Pubmed]
  13. The cytotoxin YopT of Yersinia enterocolitica induces modification and cellular redistribution of the small GTP-binding protein RhoA. Zumbihl, R., Aepfelbacher, M., Andor, A., Jacobi, C.A., Ruckdeschel, K., Rouot, B., Heesemann, J. J. Biol. Chem. (1999) [Pubmed]
  14. Functional analysis of the YopE GTPase-activating protein (GAP) activity of Yersinia pseudotuberculosis. Aili, M., Isaksson, E.L., Hallberg, B., Wolf-Watz, H., Rosqvist, R. Cell. Microbiol. (2006) [Pubmed]
  15. The proinflammatory response induced by wild-type Yersinia pseudotuberculosis infection inhibits survival of yop mutants in the gastrointestinal tract and Peyer's patches. Logsdon, L.K., Mecsas, J. Infect. Immun. (2006) [Pubmed]
  16. Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach. Sory, M.P., Boland, A., Lambermont, I., Cornelis, G.R. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  17. Molecular and cell biology aspects of plague. Cornelis, G.R. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  18. Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells. Cheng, L.W., Schneewind, O. J. Biol. Chem. (1999) [Pubmed]
  19. GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: a mechanism for disruption of actin microfilament structure. Von Pawel-Rammingen, U., Telepnev, M.V., Schmidt, G., Aktories, K., Wolf-Watz, H., Rosqvist, R. Mol. Microbiol. (2000) [Pubmed]
  20. Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences. Lloyd, S.A., Sjöström, M., Andersson, S., Wolf-Watz, H. Mol. Microbiol. (2002) [Pubmed]
  21. The cytotoxic protein YopE of Yersinia obstructs the primary host defence. Rosqvist, R., Forsberg, A., Rimpiläinen, M., Bergman, T., Wolf-Watz, H. Mol. Microbiol. (1990) [Pubmed]
  22. Targeting of the Yersinia pestis YopM protein into HeLa cells and intracellular trafficking to the nucleus. Skrzypek, E., Cowan, C., Straley, S.C. Mol. Microbiol. (1998) [Pubmed]
  23. The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensible for targeting to the secretion loci. Frithz-Lindsten, E., Rosqvist, R., Johansson, L., Forsberg, A. Mol. Microbiol. (1995) [Pubmed]
  24. Anti-LcrV antibody inhibits delivery of Yops by Yersinia pestis KIM5 by directly promoting phagocytosis. Cowan, C., Philipovskiy, A.V., Wulff-Strobel, C.R., Ye, Z., Straley, S.C. Infect. Immun. (2005) [Pubmed]
  25. LcrV of Yersinia pestis enters infected eukaryotic cells by a virulence plasmid-independent mechanism. Fields, K.A., Straley, S.C. Infect. Immun. (1999) [Pubmed]
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