Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes.

ABSTRACT: In the early stages of an infection, pathogenic bacteria use long fibrous structures known as pili as adhesive anchors for attachment to the host cells. These structures also play key roles in colony and biofilm formation. In all those processes, pili must withstand large mechanical forces. The pili of the nasty gram-positive human pathogen Streptococcus pyogenes are assembled as single, micrometer long tandem modular proteins of covalently linked repeats of pilin proteins. Here we use single molecule force spectroscopy techniques to study the mechanical properties of the major pilin Spy0128. In our studies, we engineer polyproteins containing repeats of Spy0128 flanked by the well characterized I27 protein which provides an unambiguous mechanical fingerprint. We find that Spy0128 is an in

SUBMITTER: Alegre-Cebollada J 

PROVIDER: S-EPMC2857001 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature