2 Newman, M. A., Sundelin, T., Nielsen, J. T. & Erbs, G. Frontiers in Plant 4, 139 (2013). Science 3 Zipfel, C. 35, 345-351 (2014). Trends in Immunology 4 Erbs, G. & Newman, M. A. 13, 95-104 (2012). Molecular Plant Pathology 5 Ranf, S. (2015). et al. Nature Immunology 6 Leulier, F. 4, 478-484 (2003). et al. Nature Immunology 7 Dangl, J. L., Horvath, D. M. & Staskawicz, B. J. 341, 746-751 (2013). Science 8 M. & Takayama, S. 15, 78-83 (2012). Current Opinion in Plant Biology 9 Liu, X. 3, doi:10.7554/eLife.01990 (2014). et al. eLife 10 Shi, J. 514, 187-192 (2014). et al.. Nature Figure 1 LPS recognition in mammals and plants. a, In mammals, the soluble protein (LBP) extracts and disaggregates LPS from the outer membrane of bacteria that have infected the host. The cell-surface protein CD14 then transfers LPS to a heterodimeric complex of MD-2 bound to TLR4, which triggers an intracellular response. LPS can also be detected intracellularly in mammals by caspaces 4, 5 and 11. b, Ranf show that, in plants of the family, recognition of the et al.5 Brassicaceae lipid A moiety of LPS from and bacteria, and subsequent Pseudomonas Xanthomonas induction of an immune response, requires the transmembrane receptor kinase LORE. But further details of this recognition process, such as whether it directly binds LPS, requires LPS-binding and/or the activity of LPS-extracting proteins, remain to be elucidated.
2 Newman, M. A., Sundelin, T., Nielsen, J. T. & Erbs, G. Frontiers in Plant Science 4, 139 (2013). 3 Zipfel, C. Trends in Immunology 35, 345-351 (2014). 4 Erbs, G. & Newman, M. A. Molecular Plant Pathology 13, 95-104 (2012). 5 Ranf, S. et al. Nature Immunology (2015). 6 Leulier, F. et al. Nature Immunology 4, 478-484 (2003). 7 Dangl, J. L., Horvath, D. M. & Staskawicz, B. J. Science 341, 746-751 (2013). 8 M. & Takayama, S. Current Opinion in Plant Biology 15, 78-83 (2012). 9 Liu, X. et al. eLife 3, doi:10.7554/eLife.01990 (2014). 10 Shi, J. et al.. Nature 514, 187-192 (2014). Figure 1 LPS recognition in mammals and plants. a, In mammals, the soluble protein (LBP) extracts and disaggregates LPS from the outer membrane of bacteria that have infected the host. The cell-surface protein CD14 then transfers LPS to a heterodimeric complex of MD-2 bound to TLR4, which triggers an intracellular response. LPS can also be detected intracellularly in mammals by caspaces 4, 5 and 11. b, Ranf et al.5 show that, in plants of the Brassicaceae family, recognition of the lipid A moiety of LPS from Pseudomonas and Xanthomonas bacteria, and subsequent induction of an immune response, requires the transmembrane receptor kinase LORE. But further details of this recognition process, such as whether it directly binds LPS, requires LPS-binding and/or the activity of LPS-extracting proteins, remain to be elucidated.