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The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping.


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 ?-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.

SUBMITTER: Heras B 

PROVIDER: S-EPMC3890832 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping.

Heras Begoña B   Totsika Makrina M   Peters Kate M KM   Paxman Jason J JJ   Gee Christine L CL   Jarrott Russell J RJ   Perugini Matthew A MA   Whitten Andrew E AE   Schembri Mark A MA  

Proceedings of the National Academy of Sciences of the United States of America 20131213 1


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 acti  ...[more]

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