Department of Virology, Institute for Medical Microbiology and Hygiene, University of Freiburg, Hermann-Herder-Strasse 11, D-79104 Freiburg, Germany.
J Biol Chem. 2010 Sep 10;285(37):28419-24. doi: 10.1074/jbc.R110.145839. Epub 2010 Jun 10.
The interferon-inducible MxA GTPase is a key mediator of cell-autonomous innate immunity against a broad range of viruses such as influenza and bunyaviruses. MxA shares a similar domain structure with the dynamin superfamily of mechanochemical enzymes, including an N-terminal GTPase domain, a central middle domain, and a C-terminal GTPase effector domain. Recently, crystal structures of a GTPase domain dimer of dynamin 1 and of the oligomerized stalk of MxA (built by the middle and GTPase effector domains) were determined. These data provide exciting insights into the architecture and antiviral function of the MxA oligomer. Moreover, the structural knowledge paves the way for the development of novel antiviral drugs against influenza and other highly pathogenic viruses.
干扰素诱导的 MxA GTP 酶是细胞自主固有免疫的关键介质，可抵抗广泛的病毒，如流感病毒和布尼亚病毒。MxA 与机械化学酶的 dynamin 超级家族具有相似的结构域，包括 N 端 GTP 酶结构域、中央中间结构域和 C 端 GTP 酶效应结构域。最近，确定了 dynamin 1 的 GTP 酶结构域二聚体和 MxA 的寡聚化柄（由中间和 GTP 酶效应结构域组成）的晶体结构。这些数据为 MxA 寡聚体的结构和抗病毒功能提供了令人兴奋的见解。此外，结构知识为开发针对流感和其他高致病性病毒的新型抗病毒药物铺平了道路。
