메뉴 건너뛰기




Volumn 67, Issue 9, 1999, Pages 4801-4813

LcrV of Yersinia pestis enters infected eukaryotic cells by a virulence plasmid-independent mechanism

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0032797583     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.67.9.4801-4813.1999     Document Type: Article
Times cited : (46)

References (73)
  • 1
    • 0030913232 scopus 로고    scopus 로고
    • cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
    • cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J. 16: 2730-2744.
    • (1997) EMBO J. , vol.16 , pp. 2730-2744
    • Black, D.S.1    Bliska, J.B.2
  • 2
    • 0026022459 scopus 로고
    • Analysis of the V antigen lcrGVH-yopBD operon of Yersinia pseudotuberculosis: Evidence for a regulatory role of LcrH and LcrV
    • Bergman, T., S. Håkansson, Å. Forsberg, L. Norlander, A. Macellaro, A. Backman, I. Bölin, and H. Wolf-Watz. 1991. Analysis of the V antigen lcrGVH-yopBD operon of Yersinia pseudotuberculosis: evidence for a regulatory role of LcrH and LcrV. J. Bacteriol. 173:1607-1616.
    • (1991) J. Bacteriol. , vol.173 , pp. 1607-1616
    • Bergman, T.1    Håkansson, S.2    Forsberg, Å.3    Norlander, L.4    Macellaro, A.5    Backman, A.6    Bölin, I.7    Wolf-Watz, H.8
  • 3
    • 0029814613 scopus 로고    scopus 로고
    • Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus
    • Boland, A., M. P. Sory, M. Iriarte, C. Kerbourch, P. Wattiau, and G. R. Cornelis. 1996. Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1.8 macrophages by the YopB, D, N delivery apparatus. EMBO J. 15:5191-5201.
    • (1996) EMBO J. , vol.15 , pp. 5191-5201
    • Boland, A.1    Sory, M.P.2    Iriarte, M.3    Kerbourch, C.4    Wattiau, P.5    Cornelis, G.R.6
  • 4
    • 0000972368 scopus 로고
    • The role of multiplication of Pasteurella pestis in mononuclear phagocytes in the pathogenesis of flea-borne plague
    • Cavanaugh, D. C., and R. Randall. 1959. The role of multiplication of Pasteurella pestis in mononuclear phagocytes in the pathogenesis of flea-borne plague. J. Immunol. 83:348-363.
    • (1959) J. Immunol. , vol.83 , pp. 348-363
    • Cavanaugh, D.C.1    Randall, R.2
  • 5
    • 0031771288 scopus 로고    scopus 로고
    • The Yersinia deadly kiss
    • Cornelis, G. R. 1998. The Yersinia deadly kiss. J. Bacteriol. 180:5495-5504.
    • (1998) J. Bacteriol. , vol.180 , pp. 5495-5504
    • Cornelis, G.R.1
  • 7
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis, G. R., and H. Wolf-Watz. 1997. The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol. Microbiol. 23:861-867.
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 9
    • 0344140441 scopus 로고    scopus 로고
    • Virulence role of V antigen of Yersinia pestis at the bacterial surface
    • in press
    • Fields, K. A., and S. C. Straley. Virulence role of V antigen of Yersinia pestis at the bacterial surface. Infect. Immun., in press.
    • Infect. Immun.
    • Fields, K.A.1    Straley, S.C.2
  • 10
    • 0030954706 scopus 로고    scopus 로고
    • Failure to detect binding of LcrH to the V antigen of Yersinia pestis
    • Fields, K. A., A. W. Williams, and S. C. Straley. 1997. Failure to detect binding of LcrH to the V antigen of Yersinia pestis. Infect. Immun. 65: 3954-3957.
    • (1997) Infect. Immun. , vol.65 , pp. 3954-3957
    • Fields, K.A.1    Williams, A.W.2    Straley, S.C.3
  • 11
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis
    • Forsberg, Å., A. M. Viitanen, M. Skurnik, and H. Wolf-Watz. 1991. The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis. Mol. Microbiol. 5:977-986.
    • (1991) Mol. Microbiol. , vol.5 , pp. 977-986
    • Forsberg, Å.1    Viitanen, A.M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 12
    • 0027996027 scopus 로고
    • Physiological basis of the low calcium response in Yersinia pestis
    • Fowler, J. M., and R. R. Brubaker. 1994. Physiological basis of the low calcium response in Yersinia pestis. Infect. Immun. 62:5234-5241.
    • (1994) Infect. Immun. , vol.62 , pp. 5234-5241
    • Fowler, J.M.1    Brubaker, R.R.2
  • 13
    • 0031928329 scopus 로고    scopus 로고
    • YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: Evidence of a structural domain necessary for translocation
    • Francis, M. S., and H. Wolf-Watz. 1998. YopD of Yersinia pseudotuberculosis is translocated into the cytosol of HeLa epithelial cells: evidence of a structural domain necessary for translocation. Mol. Microbiol. 29:799-813.
    • (1998) Mol. Microbiol. , vol.29 , pp. 799-813
    • Francis, M.S.1    Wolf-Watz, H.2
  • 15
    • 0029930059 scopus 로고    scopus 로고
    • The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane
    • Håkansson, S., E. E. Galyov, R. Rosqvist, and H. Wolf-Watz. 1996. The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol. Microbiol. 20: 593-603.
    • (1996) Mol. Microbiol. , vol.20 , pp. 593-603
    • Håkansson, S.1    Galyov, E.E.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 16
    • 0029908022 scopus 로고    scopus 로고
    • The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact dependent membrane disrupting activity
    • Håkansson, S., K. Schesser, C. Persson, E. E. Galyov, R. Rosqvist, F. Homble, and H. Wolf-Watz. 1996. The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact dependent membrane disrupting activity. EMBO J. 15:5812-5823.
    • (1996) EMBO J. , vol.15 , pp. 5812-5823
    • Håkansson, S.1    Schesser, K.2    Persson, C.3    Galyov, E.E.4    Rosqvist, R.5    Homble, F.6    Wolf-Watz, H.7
  • 19
    • 0031880899 scopus 로고    scopus 로고
    • YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells
    • Iriarte, M., and G. R. Cornelis. 1998. YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells. Mol. Microbiol. 29:915-929.
    • (1998) Mol. Microbiol. , vol.29 , pp. 915-929
    • Iriarte, M.1    Cornelis, G.R.2
  • 20
    • 0032055051 scopus 로고    scopus 로고
    • TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors
    • Iriarte, M., M. P. Sory, A. Boland, A. P. Boyd, S. D. Mills, I. Lambermont, and G. R. Cornelis. 1998. TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors. EMBO J. 17:1907-1918.
    • (1998) EMBO J. , vol.17 , pp. 1907-1918
    • Iriarte, M.1    Sory, M.P.2    Boland, A.3    Boyd, A.P.4    Mills, S.D.5    Lambermont, I.6    Cornelis, G.R.7
  • 21
    • 0030716279 scopus 로고    scopus 로고
    • The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex
    • Koster, M., W. Bitter, H. Cock, A. Allaoui, G. R. Cornelis, and J. Tommassen. 1997. The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol. Microbiol. 26:789-797.
    • (1997) Mol. Microbiol. , vol.26 , pp. 789-797
    • Koster, M.1    Bitter, W.2    Cock, H.3    Allaoui, A.4    Cornelis, G.R.5    Tommassen, J.6
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0026542646 scopus 로고
    • Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica
    • Lambert de Rouvroit, C. L., C. Sluiters, and G. R. Cornelis. 1992. Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica. Mol. Microbiol. 6:395-409.
    • (1992) Mol. Microbiol. , vol.6 , pp. 395-409
    • Lambert De Rouvroit, C.L.1    Sluiters, C.2    Cornelis, G.R.3
  • 25
    • 0031970595 scopus 로고    scopus 로고
    • 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., M. Anderson, and O. Schneewind. 1998. 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. Mol. Microbiol. 28:593-601.
    • (1998) Mol. Microbiol. , vol.28 , pp. 593-601
    • Lee, V.T.1    Anderson, M.2    Schneewind, O.3
  • 26
    • 0025006850 scopus 로고
    • YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice
    • Leung, K. Y., B. S. Reisner, and S. C. Straley. 1990. YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice. Infect. Immun. 58:3262-3271.
    • (1990) Infect. Immun. , vol.58 , pp. 3262-3271
    • Leung, K.Y.1    Reisner, B.S.2    Straley, S.C.3
  • 28
    • 0344147262 scopus 로고    scopus 로고
    • Conditionally replicative and conjugative plasmids carrying lacZα for cloning, mutagenesis, and allele replacement in bacteria
    • Metcalf, W. W., W. Jiang, L. L. Daniels, S.-K. Kim, A. Haldimann, and B. L. Wanner. 1996. Conditionally replicative and conjugative plasmids carrying lacZα for cloning, mutagenesis, and allele replacement in bacteria. Mol. Microbiol. 24:73-91.
    • (1996) Mol. Microbiol. , vol.24 , pp. 73-91
    • Metcalf, W.W.1    Jiang, W.2    Daniels, L.L.3    Kim, S.-K.4    Haldimann, A.5    Wanner, B.L.6
  • 31
    • 0030730859 scopus 로고    scopus 로고
    • Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and trans-location mechanisms and involving YopP, presumably acting as an effector protein
    • Mills, S. D., A. Boland, M. P. Sory, P. Van der Smissen, C. Kerbourch, B. B. Finlay, and G. R. Cornelis. 1997. Yersinia enterocolitica induces apoptosis in macrophages by a process requiring functional type III secretion and trans-location mechanisms and involving YopP, presumably acting as an effector protein. Proc. Natl. Acad. Sci. USA 94:12638-12643.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12638-12643
    • Mills, S.D.1    Boland, A.2    Sory, M.P.3    Van Der Smissen, P.4    Kerbourch, C.5    Finlay, B.B.6    Cornelis, G.R.7
  • 32
    • 0030985415 scopus 로고    scopus 로고
    • Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for cell death
    • Monack, D. M., J. Mecsas, N. Ghori, and S. Falkow. 1997. Yersinia signals macrophages to undergo apoptosis and YopJ is necessary for cell death. Proc. Natl. Acad. Sci. USA 94:10385-10390.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10385-10390
    • Monack, D.M.1    Mecsas, J.2    Ghori, N.3    Falkow, S.4
  • 33
    • 0024397462 scopus 로고
    • Identification of additional virulence determinants on the pYV plasmid of Yersinia enterocolitica W227
    • Mulder, B., T. Michiels, M. Simonet, M. P. Sory, and G. Cornelis. 1989. Identification of additional virulence determinants on the pYV plasmid of Yersinia enterocolitica W227. Infect. Immun. 57:2534-2541.
    • (1989) Infect. Immun. , vol.57 , pp. 2534-2541
    • Mulder, B.1    Michiels, T.2    Simonet, M.3    Sory, M.P.4    Cornelis, G.5
  • 34
    • 0029021978 scopus 로고
    • Suppression of cytokines in mice by protein A-V antigen fusion and restoration of synthesis by active immunization
    • Nakajima, R., V. L. Motin, and R. R. Brubaker. 1995. Suppression of cytokines in mice by protein A-V antigen fusion and restoration of synthesis by active immunization. Infect. Immun. 63:3021-3029.
    • (1995) Infect. Immun. , vol.63 , pp. 3021-3029
    • Nakajima, R.1    Motin, V.L.2    Brubaker, R.R.3
  • 35
    • 0030946572 scopus 로고    scopus 로고
    • Resistance to lipopolysaccharide mediated by the Yersinia pestis V antigen-polyhistidine fusion peptide: Amplification of interleukin-10
    • Nedialkov, Y. A., V. L. Motin, and R. R. Brubaker. 1997. Resistance to lipopolysaccharide mediated by the Yersinia pestis V antigen-polyhistidine fusion peptide: amplification of interleukin-10. Infect. Immun. 65:1196-1203.
    • (1997) Infect. Immun. , vol.65 , pp. 1196-1203
    • Nedialkov, Y.A.1    Motin, V.L.2    Brubaker, R.R.3
  • 36
    • 0032947515 scopus 로고    scopus 로고
    • Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopB
    • Neyt, C., and G. R. Cornelis. 1999. Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopB. Mol. Microbiol. 31:143-156.
    • (1999) Mol. Microbiol. , vol.31 , pp. 143-156
    • Neyt, C.1    Cornelis, G.R.2
  • 37
    • 0031802098 scopus 로고    scopus 로고
    • The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG
    • Nilles, M. L., K. A. Fields, and S. C. Straley. 1998. The V antigen of Yersinia pestis regulates Yop vectorial targeting as well as Yop secretion through effects on YopB and LcrG. J. Bacteriol. 180:3410-3420.
    • (1998) J. Bacteriol. , vol.180 , pp. 3410-3420
    • Nilles, M.L.1    Fields, K.A.2    Straley, S.C.3
  • 39
    • 0031780201 scopus 로고    scopus 로고
    • YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-α production and downstream regulation of the MAP kinase p38 and JNK
    • Palmer, L. E., S. Hobbie, J. E. Galán, and J. B. Bliska. 1998. YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-α production and downstream regulation of the MAP kinase p38 and JNK. Mol. Microbiol. 27:953-965.
    • (1998) Mol. Microbiol. , vol.27 , pp. 953-965
    • Palmer, L.E.1    Hobbie, S.2    Galán, J.E.3    Bliska, J.B.4
  • 40
    • 0031029062 scopus 로고    scopus 로고
    • Yersinia pestis - Etiologic agent of plague
    • Perry, R. D., and J. D. Fetherston. 1997. Yersinia pestis - etiologic agent of plague. Clin. Microbiol. Rev. 10:35-66.
    • (1997) Clin. Microbiol. Rev. , vol.10 , pp. 35-66
    • Perry, R.D.1    Fetherston, J.D.2
  • 41
    • 0024992438 scopus 로고
    • Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis
    • Perry, R. D., M. Pendrak, and P. Schuetze. 1990. Identification and cloning of a hemin storage locus involved in the pigmentation phenotype of Yersinia pestis. J. Bacteriol. 172:5929-5937.
    • (1990) J. Bacteriol. , vol.172 , pp. 5929-5937
    • Perry, R.D.1    Pendrak, M.2    Schuetze, P.3
  • 43
    • 0030978909 scopus 로고    scopus 로고
    • cas and FAK, and the associated accumulation of these proteins in focal adhesions
    • cas and FAK, and the associated accumulation of these proteins in focal adhesions. EMBO J. 16:2307-2318.
    • (1997) EMBO J. , vol.16 , pp. 2307-2318
    • Persson, C.1    Carballeira, N.2    Wolf-Watz, H.3    Fallman, M.4
  • 44
    • 0028802323 scopus 로고
    • Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell
    • Persson, C., R. Nordfelth, A. Holmström, S. Håkansson, R. Rosqvist, and H. Wolf-Watz. 1995. Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell. Mol. Microbiol. 18:135-150.
    • (1995) Mol. Microbiol. , vol.18 , pp. 135-150
    • Persson, C.1    Nordfelth, R.2    Holmström, A.3    Håkansson, S.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 46
    • 0025840282 scopus 로고
    • LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response
    • Plano, G. V., S. S. Barve, and S. C. Straley. 1991. LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response. J. Bacteriol. 173:7293-7303.
    • (1991) J. Bacteriol. , vol.173 , pp. 7293-7303
    • Plano, G.V.1    Barve, S.S.2    Straley, S.C.3
  • 47
    • 0027297680 scopus 로고
    • Multiple effects of lcrD mutations in Yersinia pestis
    • Plano, G. V., and S. C. Straley. 1993. Multiple effects of lcrD mutations in Yersinia pestis. J. Bacteriol. 175:3536-3545.
    • (1993) J. Bacteriol. , vol.175 , pp. 3536-3545
    • Plano, G.V.1    Straley, S.C.2
  • 48
    • 0029039020 scopus 로고
    • Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis
    • Plano, G. V., and S. C. Straley. 1995. Mutations in yscC, yscD, and yscG prevent high-level expression and secretion of V antigen and Yops in Yersinia pestis. J. Bacteriol. 177:3843-3854.
    • (1995) J. Bacteriol. , vol.177 , pp. 3843-3854
    • Plano, G.V.1    Straley, S.C.2
  • 50
    • 0024437782 scopus 로고
    • Molecular analysis of lcrGVH, the V antigen operon of Yersinia pestis
    • Price, S. B., K. Y. Leung, S. S. Barve, and S. C. Straley. 1989. Molecular analysis of lcrGVH, the V antigen operon of Yersinia pestis. J. Bacteriol. 171: 5646-5653.
    • (1989) J. Bacteriol. , vol.171 , pp. 5646-5653
    • Price, S.B.1    Leung, K.Y.2    Barve, S.S.3    Straley, S.C.4
  • 52
    • 0025788249 scopus 로고
    • Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption
    • Rosqvist, R., Å. Forsberg, and H. Wolf-Watz. 1991. Intracellular targeting of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption. Infect. Immun. 59:4562-4569.
    • (1991) Infect. Immun. , vol.59 , pp. 4562-4569
    • Rosqvist, R.1    Forsberg, Å.2    Wolf-Watz, H.3
  • 53
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., K.-E. Magnusson, and H. Wolf-Wate. 1994. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13:964-972.
    • (1994) EMBO J. , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.-E.2    Wolf-Wate, H.3
  • 54
    • 0032489918 scopus 로고    scopus 로고
    • Yersinia enterocolitica impairs activation of transcription factor NF-κB: Involvement in the induction of programmed cell death and in the suppression of macrophage TNF-α production
    • Ruckdeschel, K., S. Harb, A. Roggenkamp, M. Hornef, R. Zumbihl, S. Kohler, J. Heesemann, and B. Rouot. 1998. Yersinia enterocolitica impairs activation of transcription factor NF-κB: involvement in the induction of programmed cell death and in the suppression of macrophage TNF-α production. J. Exp. Med. 187:1069-1079.
    • (1998) J. Exp. Med. , vol.187 , pp. 1069-1079
    • Ruckdeschel, K.1    Harb, S.2    Roggenkamp, A.3    Hornef, M.4    Zumbihl, R.5    Kohler, S.6    Heesemann, J.7    Rouot, B.8
  • 56
    • 0030041090 scopus 로고    scopus 로고
    • Differential contribution of Yersinia enterocolitica virulence factors to evasion of microbicidal action of neurophils
    • Ruckdeschel, K., A. Roggenkamp, S. Schubert, and J. Heesemann. 1996. Differential contribution of Yersinia enterocolitica virulence factors to evasion of microbicidal action of neurophils. Infect. Immun. 64:724-733.
    • (1996) Infect. Immun. , vol.64 , pp. 724-733
    • Ruckdeschel, K.1    Roggenkamp, A.2    Schubert, S.3    Heesemann, J.4
  • 57
    • 0031885218 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD
    • Sarker, M., C. Neyt, I. Stainier, and G. R. Cornelis. 1998. The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD. J. Bacteriol. 180:1207-1214.
    • (1998) J. Bacteriol. , vol.180 , pp. 1207-1214
    • Sarker, M.1    Neyt, C.2    Stainier, I.3    Cornelis, G.R.4
  • 58
    • 0031770757 scopus 로고    scopus 로고
    • Targeting of the Yersinia pestis YopM protein into HeLa cells and intracellular trafficking to the nucleus
    • Skrzypek, E., C. Cowan, and S. C. Straley. 1998. Targeting of the Yersinia pestis YopM protein into HeLa cells and intracellular trafficking to the nucleus. Mol. Microbiol. 30:1051-1065.
    • (1998) Mol. Microbiol. , vol.30 , pp. 1051-1065
    • Skrzypek, E.1    Cowan, C.2    Straley, S.C.3
  • 59
    • 0027420061 scopus 로고
    • New suicide vector for gene replacement in yersiniae and other gram-negative bacteria
    • Skrzypek, E., P. L. Haddix, G. V. Plano, and S. C. Straley. 1993. New suicide vector for gene replacement in yersiniae and other gram-negative bacteria. Plasmid 29:160-163.
    • (1993) Plasmid , vol.29 , pp. 160-163
    • Skrzypek, E.1    Haddix, P.L.2    Plano, G.V.3    Straley, S.C.4
  • 60
    • 0029031698 scopus 로고
    • 2+ response, and virulence of Yersinia pestis
    • 2+ response, and virulence of Yersinia pestis. J. Bacteriol. 177:2530-2542.
    • (1995) J. Bacteriol. , vol.177 , pp. 2530-2542
    • Skrzypek, E.1    Straley, S.C.2
  • 62
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory, M. P., and G. R. Cornelis. 1994. Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol. Microbiol. 14:583-594.
    • (1994) Mol. Microbiol. , vol.14 , pp. 583-594
    • Sory, M.P.1    Cornelis, G.R.2
  • 63
    • 0027524658 scopus 로고
    • Adhesins in Yersinia pestis
    • Straley, S. C. 1993. Adhesins in Yersinia pestis. Trends Microbiol. 1:285-286.
    • (1993) Trends Microbiol. , vol.1 , pp. 285-286
    • Straley, S.C.1
  • 64
    • 0022629859 scopus 로고
    • 2+ in Yersinia pestis include structural genes for outer membrane proteins
    • 2+ in Yersinia pestis include structural genes for outer membrane proteins. Infect. Immun. 51:445-454.
    • (1986) Infect. Immun. , vol.51 , pp. 445-454
    • Straley, S.C.1    Bowmer, W.S.2
  • 65
    • 0021276287 scopus 로고
    • Yersinia pestis grows within phagolysosomes in mouse peritoneal macrophages
    • Straley, S. C., and P. A. Harmon. 1984. Yersinia pestis grows within phagolysosomes in mouse peritoneal macrophages. Infect. Immun. 45:655-659.
    • (1984) Infect. Immun. , vol.45 , pp. 655-659
    • Straley, S.C.1    Harmon, P.A.2
  • 66
    • 0029134671 scopus 로고
    • Environmental modulation of gene expression and pathogenesis in Yersinia
    • Straley, S. C., and R. D. Perry. 1995. Environmental modulation of gene expression and pathogenesis in Yersinia. Trends Microbiol. 3:310-317.
    • (1995) Trends Microbiol. , vol.3 , pp. 310-317
    • Straley, S.C.1    Perry, R.D.2
  • 68
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 70
    • 0029073803 scopus 로고
    • Role of Yops in inhibition of phagocytosis of opsonized Yersinia enterocolitica by human granulocytes
    • Visser, L. G., A. Annema, and R. van Furth. 1995. Role of Yops in inhibition of phagocytosis of opsonized Yersinia enterocolitica by human granulocytes. Infect. Immun. 63:2570-2575.
    • (1995) Infect. Immun. , vol.63 , pp. 2570-2575
    • Visser, L.G.1    Annema, A.2    Van Furth, R.3
  • 72
    • 0031936516 scopus 로고    scopus 로고
    • YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops
    • Williams, A. W., and S. C. Straley. 1998. YopD of Yersinia pestis plays a role in negative regulation of the low-calcium response in addition to its role in translocation of Yops. J. Bacteriol. 180:350-358.
    • (1998) J. Bacteriol. , vol.180 , pp. 350-358
    • Williams, A.W.1    Straley, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.