Abstract
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.
Highlights
An intrinsically disordered protein (IDP) is a functional polypeptide which cannot fold spontaneously into a stable three-dimensional conformation and extensive disorder is important for its function
Arginine and tryptophan side chain resonances are marked by asterisk protein (N-WASP) GTPase binding domain (GBD) binding motif (Marchès et al 2006; Alto et al 2007)
Neural Wiskott-Aldrich syndrome protein (N-WASP) plays a role in actin polymerization machinery where it regulates actin filament branching and assembly through the activation of actin-related protein 2/3 (ARP2/3) complex
Summary
An intrinsically disordered protein (IDP) is a functional polypeptide which cannot fold spontaneously into a stable three-dimensional conformation and extensive disorder is important for its function. Previous research has revealed that pathogens can produce protein mimics which target the components of the cellular signalling machinery. These mimics outcompete their model proteins and change the host metabolism making it favourable to the pathogen EPEC EspF is a 21 kDa IDP which contains three similar 40–47 amino acid proline-rich repeats at its C-terminus (McNamara and Donnenberg 1998; Alto et al 2007). EspF repeats include amino acid sequences which mimic bona fide interaction sites in human proteins. The N-terminal proline-rich region has been shown to interact with the Src homology 3 (SH3) domain of sorting nexin 9 (SNX9). In the C-terminal half resides a putative Neural Wiskott-Aldrich syndrome
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
