Reply to Sleutel and Remaut, “Structural insights into Escherichia coli CsgA amyloid fibril assembly revisited”

Abstract

The our discovery understanding of functional of the amyloids Escherichia in coli bacteria curli dates biogenesis back several system decades, has steadily and evolved over time. Since Chapman’s seminal work in 2002, which involved isolation, characterization, and depolymerization of the major curli subunit CsgA, a variety of structural tools have been employed to elucidate curli architecture. Notably, later on, both solid-state nuclear magnetic resonance spectroscopy (NMR) and X-ray diffraction offered critical insights into the structure of E. coli CsgA fibrils, revealing their hallmark cross-β architecture (1, 2). Despite these advances, curli fibers have remained challenging to characterize structurally, primarily due to the high aggregation propensity and intrinsically disordered nature of monomeric CsgA.