Interfering with the Folding of Group A Streptococcal pili 2 Proteins

Contreras, Fernanda; Rivas-Pardo, Jaime Andrés; Proft, Thomas; Loh, Jacelyn M. S.

Abstract

Gram-positive bacteria use their adhesive pili to attach to host cells during early stages of a bacterial infection. These extracellular hair-like appendages experience mechanical stresses of hundreds of picoNewtons; however, the presence of an internal isopeptide bond prevents the pilus protein from unfolding. Here, we describe a method to interfere with nascent pili proteins through a peptide that mimics one of the β-strands of the molecule. By using AFM-based force spectroscopy, we study the isopeptide bond formation and the effect of the peptide in the elasticity of the pilus protein. This method could be used to afford a new strategy for mechanically targeted antibiotics by simply blocking the folding of the bacterial pilus protein.

Más información

Título de la Revista: PLANT CIRCULAR RNAS
Editorial: Humana Press, Inc.
Fecha de publicación: 2020