Trimeric autotransporter adhesins: variable structure, common function

Linke, D; Riess, T; Autenrieth, IB; Lupas, A; Kempf, VAJ

doi:10.1016/j.tim.2006.04.005

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Trimeric autotransporter adhesins: variable structure, common function

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Linke, D
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Lupas, A
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Linke, D., Riess, T., Autenrieth, I., Lupas, A., & Kempf, V. (2006). Trimeric autotransporter adhesins: variable structure, common function. Trends in Microbiology, 14(6), 264-270. doi:10.1016/j.tim.2006.04.005.

Cite as: https://hdl.handle.net/21.11116/0000-000B-4366-7

Abstract

Trimeric autotransporter adhesins (TAAs) are important virulence factors in gram-negative pathogens. Despite the variety of hosts ranging from plants to mammals and the specialized regulation of TAAs, their molecular organization follows surprisingly simple rules: they form trimeric surface structures with a head-stalk-anchor architecture. The head and stalk are composed of a small set of domains, building blocks that are frequently arranged repetitively. We propose that this repetitive arrangement facilitates recombination of domains to modulate the specificity of the common function: adhesion to the host.