Oliva Chávez Adela S, Fairman James W, Felsheim Roderick F, Nelson Curtis M, Herron Michael J, Higgins LeeAnn, Burkhardt Nicole Y, Oliver Jonathan D, Markowski Todd W, Kurtti Timothy J, Edwards Thomas E, Munderloh Ulrike G
Department of Entomology, University of Minnesota, Saint Paul, Minnesota, United States of America.
Emerald Bio, Bainbridge Island, Washington, United States of America.
PLoS Pathog. 2015 Nov 6;11(11):e1005248. doi: 10.1371/journal.ppat.1005248. eCollection 2015.
Anaplasma phagocytophilum, the causative agent of Human Granulocytic Anaplasmosis (HGA), is an obligately intracellular α-proteobacterium that is transmitted by Ixodes spp ticks. However, the pathogen is not transovarially transmitted between tick generations and therefore needs to survive in both a mammalian host and the arthropod vector to complete its life cycle. To adapt to different environments, pathogens rely on differential gene expression as well as the modification of proteins and other molecules. Random transposon mutagenesis of A. phagocytophilum resulted in an insertion within the coding region of an o-methyltransferase (omt) family 3 gene. In wild-type bacteria, expression of omt was up-regulated during binding to tick cells (ISE6) at 2 hr post-inoculation, but nearly absent by 4 hr p.i. Gene disruption reduced bacterial binding to ISE6 cells, and the mutant bacteria that were able to enter the cells were arrested in their replication and development. Analyses of the proteomes of wild-type versus mutant bacteria during binding to ISE6 cells identified Major Surface Protein 4 (Msp4), but also hypothetical protein APH_0406, as the most differentially methylated. Importantly, two glutamic acid residues (the targets of the OMT) were methyl-modified in wild-type Msp4, whereas a single asparagine (not a target of the OMT) was methylated in APH_0406. In vitro methylation assays demonstrated that recombinant OMT specifically methylated Msp4. Towards a greater understanding of the overall structure and catalytic activity of the OMT, we solved the apo (PDB_ID:4OA8), the S-adenosine homocystein-bound (PDB_ID:4OA5), the SAH-Mn2+ bound (PDB_ID:4PCA), and SAM- Mn2+ bound (PDB_ID:4PCL) X-ray crystal structures of the enzyme. Here, we characterized a mutation in A. phagocytophilum that affected the ability of the bacteria to productively infect cells from its natural vector. Nevertheless, due to the lack of complementation, we cannot rule out secondary mutations.
嗜吞噬细胞无形体是人类粒细胞无形体病(HGA)的病原体,是一种专性细胞内α-变形菌,通过硬蜱属蜱传播。然而,该病原体不会在蜱的代际间经卵传播,因此需要在哺乳动物宿主和节肢动物媒介中都存活下来才能完成其生命周期。为了适应不同的环境,病原体依赖于差异基因表达以及蛋白质和其他分子的修饰。嗜吞噬细胞无形体的随机转座子诱变导致在一个o-甲基转移酶(omt)家族3基因的编码区内发生插入。在野生型细菌中,omt的表达在接种后2小时与蜱细胞(ISE6)结合时上调,但在接种后4小时几乎不存在。基因破坏减少了细菌与ISE6细胞的结合,并且能够进入细胞的突变细菌在其复制和发育中被阻断。在与ISE6细胞结合过程中对野生型与突变型细菌蛋白质组的分析确定主要表面蛋白4(Msp4)以及假定蛋白APH_0406是甲基化差异最大的蛋白。重要的是,野生型Msp4中的两个谷氨酸残基(OMT的作用靶点)被甲基化修饰,而APH_0406中的一个天冬酰胺(不是OMT的作用靶点)被甲基化。体外甲基化试验表明重组OMT特异性地甲基化Msp4。为了更深入了解OMT的整体结构和催化活性,我们解析了该酶的无配体(PDB_ID:4OA8)、结合S-腺苷同型半胱氨酸(PDB_ID:4OA5)、结合SAH-Mn2+(PDB_ID:4PCA)以及结合SAM-Mn2+(PDB_ID:4PCL)的X射线晶体结构。在此,我们鉴定了嗜吞噬细胞无形体中的一个突变,该突变影响了细菌有效感染其自然媒介细胞的能力。然而,由于缺乏互补作用,我们不能排除二次突变的可能性。