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African Trypanosomes have developed elaborate immune evasion mechanisms. Here, the authors present the cryoelectron microscopy structures of a trypanosome surface receptor with human complement C3 and C3b, revealing several modes of complement interaction. African Trypanosomes have developed elaborate mechanisms to escape the adaptive immune response, but little is known about complement evasion particularly at the early stage of infection. Here we show that ISG65 of the human-infective parasite Trypanosoma brucei gambiense is a receptor for human complement factor C3 and its activation fragments and that it takes over a role in selective inhibition of the alternative pathway C5 convertase and thus abrogation of the terminal pathway. No deposition of C4b, as part of the classical and lectin pathway convertases, was detected on trypanosomes. We present the cryo-electron microscopy (EM) structures of native C3 and C3b in complex with ISG65 which reveal a set of modes of complement interaction. Based on these findings, we propose a model for receptor-ligand interactions as they occur at the plasma membrane of blood-stage trypanosomes and may facilitate innate immune escape of the parasite.

Der Isotopenaustausch, d. h. der Ersatz von Wasserstoff durch Deuterium, verursacht eine Verkurzung der Gitterkonstanten bei einfachen und komplexen Hydriden (resp. Deuteriden). Durch prazise rontgenographische Messungen an pulverformigen Proben wurden Gitterkonstanten folgender Hydride und Deuteride: NaHNaD, NaBH4NaBD4, NaAlH4NaAlD4, LiBH4LiBD4 ermittelt und verglichen. Substitution of D for H in simple and complex hydrides results in a decrease of the lattice constants. This has been proved for NaHNaD, NaBH4NaBD4,NaAlH4NaAlD4, and LiBH4LiBD4.