Trimeric autotransporter adhesins: variable structure, common function.

Dirk Linke; Tanja Riess; Ingo B Autenrieth; Andrei Lupas; Volkhard A J Kempf

doi:10.1016/j.tim.2006.04.005

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Trimeric autotransporter adhesins: variable structure, common function.

Dirk Linke·Tanja Riess·Ingo B Autenrieth·Andrei Lupas·Volkhard A J Kempf

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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.

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Adhesins, Bacterial Biological Transport Gram-Negative Bacteria Protein Structure, Tertiary Structure-Activity Relationship Virulence Factors Journal Article Research Support, Non-U.S. Gov't

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Dirk Linke, Tanja Riess, Ingo B Autenrieth, Andrei Lupas, Volkhard A J Kempf. 2006-05-05. Trimeric autotransporter adhesins: variable structure, common function.. https://doi.org/10.1016/j.tim.2006.04.005

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