This recombinant Yersinia enterocolitica Tyrosine-protein phosphatase yopH is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
Yersinia enterocolitica Tyrosine-protein phosphatase YopH is a crucial virulence factor in Y. enterocolitica. YopH is translocated into host cells via a type III secretion system. Once inside the host cell, YopH disrupts tyrosine phosphorylation, inhibiting respiratory burst activity in macrophages, which is essential for the pathogenicity of Yersinia [1][2].
The phosphatase activity of YopH is vital for the virulence of Yersinia pathogens. Inhibitors targeting YopH have been investigated as potential anti-plague agents due to the essential role of YopH in Yersinia pathogenicity [3][4]. YopH acts on tyrosine-phosphorylated proteins in macrophages, contributing to the inhibition of bacterial uptake, thus aiding in the evasion of host immune responses [5][6][7].
YopH dephosphorylates many host cell proteins such as focal adhesion kinase (Fak), paxillin, and Fyn-binding protein (FYB), which are involved in cell adhesion and signaling processes. By inhibiting the phosphorylation of these proteins, YopH interferes with the normal functioning of host cells, contributing to the pathogenicity of Yersinia [8][9].
References:
[1] S. Green, E. Hartland, R. Robins‐Browne, & W. Phillips, Role of yoph in the suppression of tyrosine phosphorylation and respiratory burst activity in murine macrophages infected with yersinia enterocolitica, Journal of Leukocyte Biology, vol. 57, no. 6, p. 972-977, 1995. https://doi.org/10.1002/jlb.57.6.972
[2] D. Black, A. Marie‐Cardine, B. Schraven, & J. Bliska, The yersinia tyrosine phosphatase yoph targets a novel adhesion-regulated signalling complex in macrophages, Cellular Microbiology, vol. 2, no. 5, p. 401-414, 2000. https://doi.org/10.1046/j.1462-5822.2000.00061.x
[3] J. Sun, W. Li, A. Fedorov, S. Almo, & Z. Zhang, Crystal structure of the yersinia protein-tyrosine phosphatase yoph complexed with a specific small molecule inhibitor, Journal of Biological Chemistry, vol. 278, no. 35, p. 33392-33399, 2003. https://doi.org/10.1074/jbc.m304693200
[4] F. Liang, Z. Huang, S. Lee, L. Ji, M. Ivanov, A. Alonsoet al., Aurintricarboxylic acid blocks in vitro and in vivo activity of yoph, an essential virulent factor of yersinia pestis, the agent of plague, Journal of Biological Chemistry, vol. 278, no. 43, p. 41734-41741, 2003. https://doi.org/10.1074/jbc.m307152200
[5] K. Brzostek, The level of yop proteins secreted by yersinia enterocolitica is changed in maltose mutants, Fems Microbiology Letters, vol. 204, no. 1, p. 95-100, 2001. https://doi.org/10.1016/s0378-1097(01)00387-1
[6] K. Brzostek and A. Raczkowska, The level of yop proteins secreted byyersinia enterocoliticais changed in maltose mutants, Fems Microbiology Letters, vol. 204, no. 1, p. 95-100, 2001. https://doi.org/10.1111/j.1574-6968.2001.tb10869.x
[7] E. Hartland, S. Green, W. Phillips, & R. Robins-Browne, Essential role of yopd in inhibition of the respiratory burst of macrophages by yersinia enterocolitica, Infection and Immunity, vol. 62, no. 10, p. 4445-4453, 1994. https://doi.org/10.1128/iai.62.10.4445-4453.1994
[8] K. Trülzsch, T. Sporleder, E. Igwe, H. Rüssmann, & J. Heesemann, Contribution of the major secreted yops of yersinia enterocolitica
o:8 to pathogenicity in the mouse infection model, Infection and Immunity, vol. 72, no. 9, p. 5227-5234, 2004. https://doi.org/10.1128/iai.72.9.5227-5234.2004
[9] C. Persson, N. Carballeira, H. Wolf‐Watz, & M. Fällman, The ptpase yoph inhibits uptake ofyersinia, tyrosine phosphorylation of p130casand fak, and the associated accumulation of these proteins in peripheral focal adhesions, The Embo Journal, vol. 16, no. 9, p. 2307-2318, 1997. https://doi.org/10.1093/emboj/16.9.2307
