Smith Kelly D
Department of Pathology, University of Washington, 1959 NE Pacific St. HSB E504, Box 357470, Seattle, WA 98195, United States.
Int J Biochem Cell Biol. 2007;39(10):1776-80. doi: 10.1016/j.biocel.2007.07.003. Epub 2007 Jul 18.
The host innate immune defense protein lipocalin 2 binds bacterial enterobactin siderophores to limit bacterial iron acquisition. To counteract this host defense mechanism bacteria have acquired the iroA gene cluster, which encodes enzymatic machinery and transporters that revitalize enterobactin in the form of salmochelin. The iroB enzyme introduces glucosyl residues at the C5 site on 2,3-dihydroxybenzoylserine moieties of enterobactin and thereby prevents lipocalin 2 binding. Additional strategies to evade lipocalin 2 have evolved in other bacteria, such as Mycobacteria tuberculosis and Bacillus anthracis. Targeting these specialized bacterial evasion strategy may provide a mechanism to reinvigorate lipocalin 2 in defense against specific pathogens.
宿主先天性免疫防御蛋白脂钙素2结合细菌肠杆菌素铁载体，以限制细菌获取铁。为了对抗这种宿主防御机制，细菌获得了iroA基因簇，该基因簇编码将肠杆菌素以沙门菌素形式复活的酶机制和转运蛋白。IroB酶在肠杆菌素的2,3-二羟基苯甲酰丝氨酸部分的C5位点引入葡萄糖基残基，从而阻止脂钙素2结合。其他细菌，如结核分枝杆菌和炭疽芽孢杆菌，也进化出了逃避脂钙素2的其他策略。针对这些特殊的细菌逃避策略可能提供一种机制，以增强脂钙素2抵御特定病原体的防御能力。
