Fischbach Michael A, Lin Hening, Liu David R, Walsh Christopher T
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Nat Chem Biol. 2006 Mar;2(3):132-8. doi: 10.1038/nchembio771.
Many bacteria, including numerous human pathogens, synthesize small molecules known as siderophores to scavenge iron. Enterobactin, a siderophore produced by enteric bacteria, is surprisingly ineffective as an iron-scavenging agent for bacteria growing in animals because of its hydrophobicity and its sequestration by the mammalian protein siderocalin, a component of the innate immune system. However, pathogenic strains of Escherichia coli and Salmonella use enzymes encoded by the iroA gene cluster to tailor enterobactin by glycosylation and linearization. The resulting modified forms of enterobactin, known as salmochelins, can evade siderocalin and are less hydrophobic than enterobactin, restoring this siderophore's iron-scavenging ability in mammals.
许多细菌,包括众多人类病原体,会合成一种名为铁载体的小分子来获取铁元素。肠杆菌素是肠道细菌产生的一种铁载体,令人惊讶的是,由于其疏水性以及被哺乳动物蛋白质铁调素(先天免疫系统的一个组成部分)螯合,它作为动物体内生长细菌的铁获取剂效果不佳。然而,大肠杆菌和沙门氏菌的致病菌株利用iroA基因簇编码的酶对肠杆菌素进行糖基化和线性化修饰。由此产生的经修饰的肠杆菌素形式,即沙门菌素,能够避开铁调素,且疏水性比肠杆菌素低,从而恢复了这种铁载体在哺乳动物体内获取铁的能力。