20 mayo 2020

Interfering with the Folding of Group A Streptococcal pili Proteins

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

DESCARGAR
Jaime Andrés Rivas-Pardo

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.

Investigadores Participantes del Centro

Laboratorio de Biología Mecánica

Doctor en Ciencias, Universidad de Chile, Chile


LEER MÁS
Edificio2

Contacto

Edificio Corporativo, 1er subterráneo - Campus Huechuraba - Camino La Pirámide 5750, Huechuraba
+56 2 2328 1323|cgbum@umayor.cl