LEE-encoded effector EspF (EspF) is an effector protein part of enteropathogenic Escherichia coli’s (EPEC’s) arsenal for intestinal infection. This intrinsically disordered protein contains three highly conserved repeats which together compose over half of the protein’s complete amino acid sequence. EPEC uses EspF to hijack host proteins in order to promote infection. In the attack EspF is translocated, together with other effector proteins, to host cell via type III secretion system. Inside host EspF stimulates actin polymerization by interacting with Neural Wiskott-Aldrich syndrome protein (N-WASP), a regulator in actin polymerization machinery. It is presumed that EspF acts by disrupting the autoinhibitory state of N-WASP GTPase binding domain. In this NMR spectroscopy study, we report the ¹H, ¹³C, and ¹⁵N resonance assignments for the complex formed by the first 47-residue repeat of EspF and N-WASP GTPase binding domain. These near-complete resonance assignments provide the basis for further studies which aim to characterize structure, interactions, and dynamics between these two proteins in solution.

LEE 编码的效应子 EspF (EspF) 是用于肠道感染的肠病原性大肠杆菌(EPEC) 库的效应蛋白部分。这种本质上无序的蛋白质包含三个高度保守的重复序列，它们共同构成了蛋白质完整氨基酸序列的一半以上。EPEC 使用 EspF 劫持宿主蛋白质以促进感染。在攻击中，EspF 与其他效应蛋白一起通过 III 型分泌系统易位到宿主细胞。内部宿主 EspF 通过与神经 Wiskott-Aldrich 综合征蛋白 (N-WASP)（肌动蛋白聚合机制中的调节剂）相互作用来刺激肌动蛋白聚合。据推测，EspF 通过破坏 N-WASP GTPase 结合域的自身抑制状态起作用。在这项 NMR 光谱研究中，我们报告了¹由 EspF 和 N-WASP GTPase 结合域的第一个 47 个残基重复序列形成的复合物的H、¹³ C 和¹⁵ N 共振分配。这些近乎完整的共振分配为进一步研究奠定了基础，旨在表征溶液中这两种蛋白质之间的结构、相互作用和动力学。