Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Naka-cho, Koganei, Tokyo 184-8588, Japan.
Department of Biological Production, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Saiwai-cho 3-5-8, Fuchu, Tokyo 183-8509, Japan.
J Insect Physiol. 2014 Jan;60:40-9. doi: 10.1016/j.jinsphys.2013.11.003. Epub 2013 Nov 19.
Nodules consisting of hemocytes and trapped microorganisms are important targets for melanization, which is best known in the insect immune system. We investigated factors functioning in nodule melanization and the mechanism by which these factors congregate in the nodule. BmHP21, BmSPH1 and BmSPH2, Bombyx mori orthologs of Manduca sexta serine protease HP21, serine protease homologs (SPH1 and SPH2), and a prophenoloxidase, BmPO1 were observed as inactive forms in the plasma, but as putatively active forms in the nodule. Production of prophenoloxidase-activating proteinases, BmPAP1 and BmPAP3/PPAE and BmPO1 were confirmed in hemocytes. BmSPH1 and BmSPH2 were observed on trapped bacterial cells in the nodule and were isolated from the surface of bacterial cells incubated with plasma. BmSPH1 and BmSPH2 were found in plasma in complex with a pattern recognition receptor, BmLBP. These data suggest that melanization-regulating factors congregate in nodules through a combination of microorganism-dependent and hemocyte-dependent routes.
由血细胞和捕获的微生物组成的结节是黑化的重要靶点,黑化在昆虫免疫系统中最为人所知。我们研究了在结节黑化中起作用的因素以及这些因素在结节中聚集的机制。在血浆中,家蚕的 Manduca sexta 丝氨酸蛋白酶 HP21、丝氨酸蛋白酶同源物 (SPH1 和 SPH2) 和一种原酚氧化酶 BmPO1 作为无活性形式被观察到,但在结节中作为假定的活性形式被观察到。在血细胞中证实了原酚氧化酶激活蛋白酶 BmPAP1 和 BmPAP3/PPAE 和 BmPO1 的产生。BmSPH1 和 BmSPH2 在家蚕的结节中被观察到在捕获的细菌细胞上,并从与血浆孵育的细菌细胞表面分离出来。BmSPH1 和 BmSPH2 与一种模式识别受体 BmLBP 一起存在于血浆中。这些数据表明,黑化调节因子通过微生物依赖和血细胞依赖的途径聚集在结节中。