Skip to main content
Infection and Immunity logoLink to Infection and Immunity
. 1997 Mar;65(3):924–930. doi: 10.1128/iai.65.3.924-930.1997

Effect of Yersinia pestis YopM on experimental plague.

J Nemeth 1, S C Straley 1
PMCID: PMC175070  PMID: 9038298

Abstract

YopM of Yersinia pestis has previously been shown to be necessary for full virulence in mice and to be able to bind human alpha-thrombin. This activity prompted the hypothesis that YopM, functioning extracellularly during plague, might be accessible to neutralization by antibody and hence might be a protective antigen. This study tested this hypothesis and found that YopM was not protective, either by passive or active immunization, in inbred or outbred mice. These findings showed that either YopM-specific antibody does not have access to YopM during experimental plague or the function of extracellular YopM is not neutralizable by antibody. Exogenously supplied YopM partially restored virulence to a YopM- strain of Y. pestis while having no effect on lethality of Listeria monocytogenes. These findings indicate that YopM does not significantly alter host defenses important for resistance against heterologous infection (Listeria monocytogenes) but raise the possibility that YopM has a minor extracellular function specific to homologous infection (Y. pestis).

Full Text

The Full Text of this article is available as a PDF (147.1 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson G. W., Jr, Leary S. E., Williamson E. D., Titball R. W., Welkos S. L., Worsham P. L., Friedlander A. M. Recombinant V antigen protects mice against pneumonic and bubonic plague caused by F1-capsule-positive and -negative strains of Yersinia pestis. Infect Immun. 1996 Nov;64(11):4580–4585. doi: 10.1128/iai.64.11.4580-4585.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Andrews G. P., Heath D. G., Anderson G. W., Jr, Welkos S. L., Friedlander A. M. Fraction 1 capsular antigen (F1) purification from Yersinia pestis CO92 and from an Escherichia coli recombinant strain and efficacy against lethal plague challenge. Infect Immun. 1996 Jun;64(6):2180–2187. doi: 10.1128/iai.64.6.2180-2187.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boland A., Sory M. P., Iriarte M., Kerbourch C., Wattiau P., Cornelis G. R. 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. 1996 Oct 1;15(19):5191–5201. [PMC free article] [PubMed] [Google Scholar]
  4. Ferber D. M., Brubaker R. R. Plasmids in Yersinia pestis. Infect Immun. 1981 Feb;31(2):839–841. doi: 10.1128/iai.31.2.839-841.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Goguen J. D., Yother J., Straley S. C. Genetic analysis of the low calcium response in Yersinia pestis mu d1(Ap lac) insertion mutants. J Bacteriol. 1984 Dec;160(3):842–848. doi: 10.1128/jb.160.3.842-848.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Håkansson S., Galyov E. E., Rosqvist R., Wolf-Watz H. The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol Microbiol. 1996 May;20(3):593–603. doi: 10.1046/j.1365-2958.1996.5251051.x. [DOI] [PubMed] [Google Scholar]
  7. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  8. Leary S. E., Williamson E. D., Griffin K. F., Russell P., Eley S. M., Titball R. W. Active immunization with recombinant V antigen from Yersinia pestis protects mice against plague. Infect Immun. 1995 Aug;63(8):2854–2858. doi: 10.1128/iai.63.8.2854-2858.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Leung K. Y., Reisner B. S., Straley S. C. YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice. Infect Immun. 1990 Oct;58(10):3262–3271. doi: 10.1128/iai.58.10.3262-3271.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Leung K. Y., Straley S. C. The yopM gene of Yersinia pestis encodes a released protein having homology with the human platelet surface protein GPIb alpha. J Bacteriol. 1989 Sep;171(9):4623–4632. doi: 10.1128/jb.171.9.4623-4632.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Meyer K. F. Effectiveness of live or killed plague vaccines in man. Bull World Health Organ. 1970;42(5):653–666. [PMC free article] [PubMed] [Google Scholar]
  12. Motin V. L., Nakajima R., Smirnov G. B., Brubaker R. R. Passive immunity to yersiniae mediated by anti-recombinant V antigen and protein A-V antigen fusion peptide. Infect Immun. 1994 Oct;62(10):4192–4201. doi: 10.1128/iai.62.10.4192-4201.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Nakajima R., Brubaker R. R. Association between virulence of Yersinia pestis and suppression of gamma interferon and tumor necrosis factor alpha. Infect Immun. 1993 Jan;61(1):23–31. doi: 10.1128/iai.61.1.23-31.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Nakajima R., Motin V. L., Brubaker R. R. Suppression of cytokines in mice by protein A-V antigen fusion peptide and restoration of synthesis by active immunization. Infect Immun. 1995 Aug;63(8):3021–3029. doi: 10.1128/iai.63.8.3021-3029.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Persson C., Nordfelth R., Holmström A., Håkansson S., Rosqvist R., Wolf-Watz H. Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell. Mol Microbiol. 1995 Oct;18(1):135–150. doi: 10.1111/j.1365-2958.1995.mmi_18010135.x. [DOI] [PubMed] [Google Scholar]
  16. Plano G. V., Barve S. S., Straley S. C. LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response. J Bacteriol. 1991 Nov;173(22):7293–7303. doi: 10.1128/jb.173.22.7293-7303.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Protsenko O. A., Anisimov P. I., Mozharov O. T., Konnov N. P., Popov Iu A. Vyiavlenie i kharakteristika plazmid chumnogo mikroba, determiniruiushchikh sintez pestitsina I, antigena fraktsiia I i ékzotoksina "myshinogo" toksina. Genetika. 1983 Jul;19(7):1081–1090. [PubMed] [Google Scholar]
  18. Reisner B. S., Straley S. C. Yersinia pestis YopM: thrombin binding and overexpression. Infect Immun. 1992 Dec;60(12):5242–5252. doi: 10.1128/iai.60.12.5242-5252.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Rosqvist R., Magnusson K. E., Wolf-Watz H. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 1994 Feb 15;13(4):964–972. doi: 10.1002/j.1460-2075.1994.tb06341.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sample A. K., Brubaker R. R. Post-translational regulation of Lcr plasmid-mediated peptides in pesticinogenic Yersinia pestis. Microb Pathog. 1987 Oct;3(4):239–248. doi: 10.1016/0882-4010(87)90057-x. [DOI] [PubMed] [Google Scholar]
  21. Simpson W. J., Thomas R. E., Schwan T. G. Recombinant capsular antigen (fraction 1) from Yersinia pestis induces a protective antibody response in BALB/c mice. Am J Trop Med Hyg. 1990 Oct;43(4):389–396. doi: 10.4269/ajtmh.1990.43.389. [DOI] [PubMed] [Google Scholar]
  22. Skrzypek E., Straley S. C. Interaction between Yersinia pestis YopM protein and human alpha-thrombin. Thromb Res. 1996 Oct 1;84(1):33–43. doi: 10.1016/0049-3848(96)00159-4. [DOI] [PubMed] [Google Scholar]
  23. Sodeinde O. A., Goguen J. D. Genetic analysis of the 9.5-kilobase virulence plasmid of Yersinia pestis. Infect Immun. 1988 Oct;56(10):2743–2748. doi: 10.1128/iai.56.10.2743-2748.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Sory M. P., Boland A., Lambermont I., Cornelis G. R. Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach. Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):11998–12002. doi: 10.1073/pnas.92.26.11998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Straley S. C., Bowmer W. S. Virulence genes regulated at the transcriptional level by Ca2+ in Yersinia pestis include structural genes for outer membrane proteins. Infect Immun. 1986 Feb;51(2):445–454. doi: 10.1128/iai.51.2.445-454.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Straley S. C., Plano G. V., Skrzypek E., Haddix P. L., Fields K. A. Regulation by Ca2+ in the Yersinia low-Ca2+ response. Mol Microbiol. 1993 Jun;8(6):1005–1010. doi: 10.1111/j.1365-2958.1993.tb01644.x. [DOI] [PubMed] [Google Scholar]
  27. Straley S. C., Skrzypek E., Plano G. V., Bliska J. B. Yops of Yersinia spp. pathogenic for humans. Infect Immun. 1993 Aug;61(8):3105–3110. doi: 10.1128/iai.61.8.3105-3110.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Straley S. C. The plasmid-encoded outer-membrane proteins of Yersinia pestis. Rev Infect Dis. 1988 Jul-Aug;10 (Suppl 2):S323–S326. doi: 10.1093/cid/10.supplement_2.s323. [DOI] [PubMed] [Google Scholar]
  29. Une T., Brubaker R. R. In vivo comparison of avirulent Vwa- and Pgm- or Pstr phenotypes of yersiniae. Infect Immun. 1984 Mar;43(3):895–900. doi: 10.1128/iai.43.3.895-900.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Williams J. E., Cavanaugh D. C. Measuring the efficacy of vaccination in affording protection against plague. Bull World Health Organ. 1979;57(2):309–313. [PMC free article] [PubMed] [Google Scholar]
  31. Williamson E. D., Eley S. M., Griffin K. F., Green M., Russell P., Leary S. E., Oyston P. C., Easterbrook T., Reddin K. M., Robinson A. A new improved sub-unit vaccine for plague: the basis of protection. FEMS Immunol Med Microbiol. 1995 Dec;12(3-4):223–230. doi: 10.1111/j.1574-695X.1995.tb00196.x. [DOI] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES