Theme and variations in autotransporter adhesins
7th World Congress on Microbiology
November 28-29, 2016 Valencia, Spain

Begona Heras

La Trobe University, Australia

Posters & Accepted Abstracts: J Bacteriol Parasitol

Abstract:

Many persistent and chronic bacterial infections are associated with the formation of aggregates and biofilms that are difficult to treat, including respiratory and urinary tract infections (UTIs), infections on medical devices and infections of the ear, gums and heart. Thus, an increased understanding of the mechanisms employed by bacteria to form biofilms is essential for the development of strategies to combat these persistent and intrinsically resistant communities. One mechanism of bacterial aggregation and biofilm formation involves the expression of self-associating surface located autotransporter (AT) proteins. Our work focuses on investigating the structural diversity of AT proteins to understand their mechanism of action. We have recently elucidated the structure of Antigen 43 (Ag43), an AT protein from uropathogenic E. coli (UPEC) that self associates forming bacterial aggregates and biofilms. Our studies have shown how Ag43's L-shaped structure drives the formation of cell aggregates via a molecular Velcrolike mechanism. Furthermore, our recent studies on other AT proteins from E. coli pathotypes show unexpected structural diversity among this family of proteins, which results in different virulence functions. For example UpaB shares low sequence and structural similarity with Ag43, does not self associate to form bacterial aggregates but binds extracellular matrix proteins (e.g., fibronectin) and increases bladder colonization.

Biography :

Email: B.Heras@latrobe.edu.au