Asgari Sassan, Zareie Reza, Zhang Guangmei, Schmidt Otto
Department of Applied and Molecular Ecology, The University of Adelaide, Glen Osmond, South Australia.
Arch Insect Biochem Physiol. 2003 Jun;53(2):92-100. doi: 10.1002/arch.10088.
Insects are important vectors of diseases with remarkable immune defense capabilities. Hymenopteran endoparasitoids are adapted to overcome the host defense system and, therefore, are useful sources of immune-suppressing proteins. Not much is known about venom proteins in endoparasitoids, especially those that have a functional relationship with polydnaviruses (PDVs). Here, we describe the isolation and characterization of a small venom protein (Vn4.6) from an endoparasitoid, Cotesia rubecula, which interferes with the activation of the host hemolymph prophenoloxidase. The coding region for Vn4.6 is located upstream in the opposite direction of a gene coding for a C. rubecula PDV-protein (Crp32).
昆虫是具有卓越免疫防御能力的重要疾病传播媒介。膜翅目内寄生蜂能够适应并克服宿主的防御系统,因此是免疫抑制蛋白的有用来源。关于内寄生蜂的毒液蛋白,尤其是那些与多分DNA病毒(PDVs)存在功能关系的毒液蛋白,人们了解得并不多。在此,我们描述了从内寄生蜂小红腹茧蜂中分离并鉴定出一种小毒液蛋白(Vn4.6),它会干扰宿主血淋巴前酚氧化酶的激活。Vn4.6的编码区位于与小红腹茧蜂PDV蛋白(Crp32)编码基因相反方向的上游。