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Interactions between mycoplasma lipid-associated membrane proteins and the host cells

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Abstract

Mycoplamas are a group of wall-less prokaryotes widely distributed in nature, some of which are pathogenic for humans and animals. There are many lipoproteins anchored on the outer face of the plasma membrane, called lipid-associated membrane proteins (LAMPs). LAMPs are highly antigenic and could undergo phase and size variation, and are recognized by the innate immune system through Toll-like receptors (TLR) 2 and 6. LAMPs can modulate the immune system, and could induce immune cells apoptosis or death. In addition, they may associate with malignant transformation of host cells and are also considered to be cofactors in the progression of AIDS.

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References

  • Akira, S., Takeda, K., Kaisho, T., 2001. Toll-like receptors: critical proteins linking innate and acquired immunity. Nat. Immunol., 2(8):675–680. [doi:10.1038/90609]

    Article  PubMed  CAS  Google Scholar 

  • Baseman, J.B., Lange, M., Criseimagna, N.L., Giron, J.A., Thomas, C.A., 1995. Interplay between mycoplasmas and host target cells. Microb. Pathog., 19(2):105–116. [doi:10.1006/mpat.1995.0050]

    Article  PubMed  CAS  Google Scholar 

  • Buwitt-Beckmann, U., Heine, H., Wiesmuller, K.H., Jung, G., Brock, R., Akira, S., Ulmer, A.J., 2005. Toll-like receptor 6-independent signaling by diacylated lipopeptides. Eur. J. Immunol., 35(1):282–289. [doi:10.1002/eji.200424955]

    Article  PubMed  CAS  Google Scholar 

  • Chambaud, I., Wroblewski, H., Blanchard, A., 1999. Interactions between mycoplasma lipoproteins and the host immune system. Trends Microbiol., 7(12):493–499. [doi:10.1016/S0966-842X(99)01641-8]

    Article  PubMed  CAS  Google Scholar 

  • Davis, K.L., Wise, K.S., 2002. Site-specific proteolysis of the MALP-404 lipoprotein determines the release of a soluble selective lipoprotein-associated motif-containing fragment and alteration of the surface phenotype of Mycoplasma fermentans. Infect. Immun., 70(3):1129–1135. [doi:10.1128/IAI.70.3.1129-1135.2002]

    Article  PubMed  CAS  Google Scholar 

  • Feng, S.H., Tsai, S., Rodriguez, J., Lo, S.C., 1999. Mycoplasmal infections prevent apoptosis and induce malignant transformation of interleukin-2-dependent 32D hematopoietic cells. Mol. Cell Biol., 19(12):7995–8002.

    PubMed  CAS  Google Scholar 

  • Fujita, M., Into, T., Yasuda, M., Okusawa, T., Hamahira, S., Kuroki, Y., Eto, A., Nisizawa, T., Morita, M., Shibata, K.I., 2003. Involvement of leucine resides at position 107, 112, and 115 in a leucine-rich repeat motif of human Toll-like receptor 2 in the recognition of diacylated lipoprotein and lipopeptide and Staphylococcus aureus peptidoglycans. J. Immunol., 171(7):3675–3683.

    PubMed  CAS  Google Scholar 

  • Garcia, J., Lemercier, B., Roman-Roman, S., Rawadi, G., 1998. A Mycoplasma fermentans-derived synthetic lipopeptide induces AP-1 and NF-κB activity and cytokine secretion in macrophages via the activation of mitogen-activated protein kinase pathways. J. Biol. Chem., 273(51):34391–34398. [doi:10.1074/jbc.273.51.34391]

    Article  PubMed  CAS  Google Scholar 

  • Hall, R.E., Agarwal, S., Kestler, D.P., 2000. Induction of leukemia cell differentiation and apoptosis by recombinant P48, a modulin derived from Mycoplasma fermentans. Biochem. Biophys. Res. Commun., 269(1):284–289. [doi:10.1006/bbrc.2000.2282]

    Article  PubMed  CAS  Google Scholar 

  • Henderson, B., Poole, S., Wleson, M., 1996. Bacterial modulins: a novel class of virulence factors which cause host tissue pathology by inducing cytokine synthesis. Microbiol. Rev., 60(2):316–341.

    PubMed  CAS  Google Scholar 

  • Horino, A., Sasaki, Y., Sasaki, T., Kenri, T., 2003. Multiple promoter inversions generate surface antigenic variation in Mycoplasma penetrans. J. Bacteriol., 185(1):231–242. [doi:10.1128/JB.185.1.231-242.2003]

    Article  PubMed  CAS  Google Scholar 

  • Into, T., Nodasaka, Y., Hasebe, A., Okuzawa, T., Nakamura, J., Ohata, N., Shibata, K., 2002a. Mycoplasmal lipoproteins induce Toll-like receptor 2 and caspases-mediated cell death in lymphocytes and monocytes. Microbiol. Immunol., 46(4):265–276.

    PubMed  CAS  Google Scholar 

  • Into, T., Okada, K., Inoue, N., Yasuda, M., Shibata, K., 2002b. Extracellular ATP regulates cell death of lymphocytes and monocytes induced by membrane-bound lipoproteins of Mycoplasma fermentans and Mycoplasma salivarium. Microbiol. Immunol., 46(10):667–675.

    PubMed  CAS  Google Scholar 

  • Into, T., Kiura, K., Yasuda, M., Kataoka, H., Inoue, N., Hasebe, A., Takeda, K., Akira, S., Shibata, K., 2004. Stimulation of human Toll-like receptor (TLR) 2 and TLR6 with membrane lipoproteins of Mycoplasma fermentans induces apoptotic cell death after NF-kappa B activation. Cell. Microbiol., 6(2):187–199. [doi:10.1046/j.1462-5822.2003.00356.x]

    Article  PubMed  CAS  Google Scholar 

  • Iyama, K., Zhang, S., Lo, S.C., 2001. Effects of mycoplasmal LAMPs on receptor responses to steroid hormones in mammalian cells. Curr. Microbiol., 43(3):163–169. [doi:10.1007/s002840010281]

    Article  PubMed  CAS  Google Scholar 

  • Mühlradt, P.F., Schade, U., 1991. MDHM, a macrophage-stimulatory product of Mycoplasma fermentans, leads to in vitro interleukin-1 (IL-1), IL-6, tumor necrosis factor, and prostaglandin production and is pyrogenic in rabbits. Infect. Immun., 59(11):3969–3974.

    PubMed  Google Scholar 

  • Mühlradt, P.F., Frisch, M., 1994. Purification and partial biochemical characterization of a Mycoplasma fermentans-derived substance that activates macrophages to release nitric oxide, tumor necrosis factor, and interleukin-6. Infect. Immun., 62(9):3801–3807.

    PubMed  Google Scholar 

  • Mühlradt, P.F., Kiess, M., Meyer, H., Sussmuth, R., Jung, G., 1997. Isolation, structure elucidation, and synthesis of a macrophage stimulatory lipopeptide from Mycoplasma fermentans acting at picomolar concentration. J. Exp. Med., 185(11):1951–1958. [doi:10.1084/jem.185.11.1951]

    Article  PubMed  Google Scholar 

  • Rawadi, G., 2000. Mycoplasma fermentans interaction with monocytes/macrophages: molecular basis. Microbes Infect., 2(8):955–964. [doi:10.1016/S1286-4579(00)00395-6]

    Article  PubMed  CAS  Google Scholar 

  • Rawadi, G., Roman-Roman, S., Castedo, M., Dutilleul, V., Susin, S., Marchetti, P., Geuskens, M., Kroemer, G., 1996. Effects of Mycoplasma fermentans on the myelomonocytic lineage. Different molecular entities with cytokine-inducing and cytocidal potential. J. Immunol., 156(2):670–678.

    PubMed  CAS  Google Scholar 

  • Rawadi, G., Garcia, J., Lemercier, B., Roman-Roman, S., 1999. Signal transduction pathways involved in the activation of NF-kappa B, AP-1, and c-fos by Mycoplasma fermentans membrane lipoproteins in macrophages. J. Immunol., 162(4):2193–2203.

    PubMed  CAS  Google Scholar 

  • Razin, S., Yogev, D., Naot, Y., 1998. Molecular biology and pathogenicity of mycoplasmas. Microbiol. Rev., 62(4):1094–1156.

    CAS  Google Scholar 

  • Rock, F.L., Hardiman, G., Timans, J.C., Kastelein, R.A., Bazan, J.F., 1998. A family of human receptors structurally related to Drosophila Toll. Proc. Natl. Acad. Sci. USA, 95(2):588–593.

    Article  PubMed  CAS  Google Scholar 

  • Romero, F., Moreno, E., Ruiz-Bravo, A., Jimenez-Valera, M., 2004. In vivo immunomodulation by Mycoplasma fermentans membrane lipoprotein. Curr. Microbiol., 48(3):237–239. [doi:10.1007/s00284-003-4134-1]

    Article  PubMed  CAS  Google Scholar 

  • Roske, K., Blanchard, A., Chambaud, I., Citti, C., Helbig, J.H., Prevost, M.C., Rosengarten, R., Jacobs, E., 2001. Phase variation among major surface antigens of Mycoplasma penetrans. Infect. Immun., 69(12):7642–7651. [doi:10.1128/IAI.69.12.7642-7651.2001]

    Article  PubMed  CAS  Google Scholar 

  • Rottem, S., 2003. Interaction of mycoplasmas with host cells. Physiol. Rev., 83(2):417–432.

    PubMed  CAS  Google Scholar 

  • Schroder, N.U., Heine, H., Alexander, C., Manukyan, M., Eckert, J., Hamann, L., Gobel, U.B., Schumann, R.R., 2004. Lipopolysaccharide binding protein binds to triacylated and diacylated lipopeptides and mediates innate immune responses. J. Immunol., 173(4):2683–2691.

    PubMed  Google Scholar 

  • Seya, T., Matsumoto, M., 2002. A lipoprotein family from Mycoplasma fermentans confers host immune activation through Toll-like receptor 2. Int. J. Biochem. Cell Biol., 34(8):901–906. [doi:10.1016/S1357-2725(01)00164-9]

    Article  PubMed  CAS  Google Scholar 

  • Shibata, K., Hasebe, A., Into, T., Yamada, M., Watanabe, T., 2000. The N-terminal lipopeptide of a 44-kDa membrane-bound lipoprotein of Mycoplasma salivarium is responsible for the expression of intercellular adhesion molecule-1 on the cell surface of normal human gingival fibroblasts. J. Immunol., 165(11):6538–6544.

    PubMed  CAS  Google Scholar 

  • Shimizu, T., Kida, Y., Kuwano, K., 2004. Lipid-associated membrane proteins of Mycoplasma fermentans and Mycoplasma penetrans activate human immunodeficiency virus long-terminal repeats through Toll-like receptors. Immunology, 113(1):121–129. [doi:10.1111/j.1365-2567.2004.01937.x]

    Article  PubMed  CAS  Google Scholar 

  • Shimizu, T., Kida, Y., Kuwano, K., 2005. A dipalmitoylated lipoprotein from Mycoplasma pneumoniae activates NF-κB through TLR1, TLR2, and TLR6. J. Immunol., 175(7):4641–4646.

    PubMed  CAS  Google Scholar 

  • Simmons, W.L., Dybvig, K., 2003. The Vsa proteins modulate susceptibility of Mycoplasma pulmonis to complement killing, hemadsorption, and adherence to polystyrene. Infect. Immun., 71(10):5733–5738. [doi:10.1128/IAI.71.10.5733-5738.2003]

    Article  PubMed  CAS  Google Scholar 

  • Takeda, K., Akira, S., 2001. Roles of Toll-like receptors in innate immune responses. Genes Cells, 6(9):733–742. [doi:10.1046/j.1365-2443.2001.00458.x]

    Article  PubMed  CAS  Google Scholar 

  • Takeuchi, O., Kaufmann, A., Grote, K., Kawai, T., Hoshino, K., Morr, M., Muhlradt, P.F., Akira, S., 2000. Cutting edge: preferentially the R-stereoisomer of the Mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a Toll-Like receptor 2-and MyD88-dependent signaling pathway. J. Immunol., 164(2):554–557.

    PubMed  CAS  Google Scholar 

  • Takeuchi, O., Sato, S., Horiuchi, T., Hoshino, K., Takeda, K., Dong, Z., Modlin, R.L., Akira, S., 2002. Cutting edge: role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J. Immunol., 169(1):10–14.

    PubMed  CAS  Google Scholar 

  • Tu, A.H., Clapper, B., Schoeb, T.R., Elgavish, A., Zhang, J., Liu, L., Yu, H., Dybvig, K., 2005. Association of a major protein antigen of Mycoplasma arthritidis with virulence. Infect. Immun., 73(1):245–249. [doi:10.1128/IAI.73.1.245-249.2005]

    Article  PubMed  CAS  Google Scholar 

  • Zeng, Y.H., Wu, Y.M., Zhang, W.B., Yu, M.J., Zhu, C.M., Tan, L.Z., 2004. Activation of nuclear factor kappaB and induction of inducible nitric oxide synthase by lipid-associated membrane proteins isolated from Mycoplasma penetrans. Chin. Med. J. (Engl.), 117(7):997–1001.

    CAS  Google Scholar 

  • Zhang, Q., Wise, K.S., 2001. Coupled phase-variable expression and epitope masking of selective surface lipoproteins increase surface phenotypic diversity in Mycoplasma hominis. Infect. Immun., 69(8):5177–5181. [doi:10.1128/IAI.69.8.5177-5181.2001]

    Article  PubMed  CAS  Google Scholar 

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Project (No. 30570093) supported by the National Natural Science Foundation of China

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You, Xx., Zeng, Yh. & Wu, Ym. Interactions between mycoplasma lipid-associated membrane proteins and the host cells. J. Zhejiang Univ. - Sci. B 7, 342–350 (2006). https://doi.org/10.1631/jzus.2006.B0342

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  • DOI: https://doi.org/10.1631/jzus.2006.B0342

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