20 May 2020

Interfering with the Folding of Group A Streptococcal pili Proteins

DOI : 10.1007/978-1-0716-0467-0_28

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Andrés Rivas-Pardo, PhD.

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.

Participating Center Researchers

Mechanical Biology Laboratory

PhD in Sciences, Universidad de Chile, Chile.


LEER MÁS
Edificio2

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