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. 2019 Mar 15;10:1233. doi: 10.1038/s41467-019-09200-2

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 7 — Model for Irgb2-b1-mediated control of T. gondii infection in wild-derived mice. a In laboratory mice, effector proteins from canonical virulent T. gondii strains (like RH) specifically phosphorylate certain Immunity-Related GTPases (IRG) proteins, thereby inhibiting oligomerisation and destruction of the parasitophorous vacuolar membrane (PVM). Two rhoptry kinases, ROP18 and ROP17, have been demonstrated to preferentially phosphorylate Irga6_BL/6 or Irgb6_BL/6. The existence of additional parasite effectors specific for other IRG proteins is assumed. b In CIM and probably other wild-derived mice, canonical virulent T. gondii strains (like RH) are counteracted by direct binding of ROP5 isoform B by the polymorphic tandem IRG protein Irgb2-b1_CIM. IRG effector proteins are free to accumulate around the PVM, resulting in growth control, encystment and transmission of the parasite. Genetically more diverse T. gondii strains, like T. gondii VAND from South America, express polymorphic ROP5 variants that are not targeted by Irgb2-b1_CIM. Consequently, effector IRG proteins such as Irga6_CIM are phosphorylated and inactivated by a T. gondii VAND kinase complex. Infected animals die shortly after parasite challenge. Molecular interaction between ROP18 and ROP5 or Irga6 and ROP5 within the VAND kinase complex awaits experimental confirmation