Title |
The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping
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Published in |
Proceedings of the National Academy of Sciences of the United States of America, December 2013
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DOI | 10.1073/pnas.1311592111 |
Pubmed ID | |
Authors |
Begoña Heras, Makrina Totsika, Kate M. Peters, Jason J. Paxman, Christine L. Gee, Russell J. Jarrott, Matthew A. Perugini, Andrew E. Whitten, Mark A. Schembri |
Abstract |
Aggregation and biofilm formation are critical mechanisms for bacterial resistance to host immune factors and antibiotics. Autotransporter (AT) proteins, which represent the largest group of outer-membrane and secreted proteins in Gram-negative bacteria, contribute significantly to these phenotypes. Despite their abundance and role in bacterial pathogenesis, most AT proteins have not been structurally characterized, and there is a paucity of detailed information with regard to their mode of action. Here we report the structure-function relationships of Antigen 43 (Ag43a), a prototypic self-associating AT protein from uropathogenic Escherichia coli. The functional domain of Ag43a displays a twisted L-shaped β-helical structure firmly stabilized by a 3D hydrogen-bonded scaffold. Notably, the distinctive Ag43a L shape facilitates self-association and cell aggregation. Combining all our data, we define a molecular "Velcro-like" mechanism of AT-mediated bacterial clumping, which can be tailored to fit different bacterial lifestyles such as the formation of biofilms. |
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