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Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system

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

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Citation

Gerlach, R., Jäckel, D., Stecher, B., Wagner, C., Lupas, A., Hardt, W.-D., et al. (2007). Salmonella Pathogenicity Island 4 encodes a giant non-fimbrial adhesin and the cognate type 1 secretion system. Cellular Microbiology, 9(7), 1834-1850. doi:10.1111/j.1462-5822.2007.00919.x.


Cite as: https://hdl.handle.net/21.11116/0000-000B-3D8A-6
Abstract
Pathogenicity Islands play a major role in the pathogenesis of infections by Salmonella enterica. The molecular function of Salmonella Pathogenicity Island 4 (SPI4) is largely unknown, but recent work indicated a role of SPI4 for Salmonella pathogenesis in certain animal models. We analysed the virulence functions of SPI4 and observed that SPI4 is contributing to intestinal inflammation in a mouse model. On a cellular level, SPI4 mediates adhesion to epithelial cells. We demonstrate the function of SPI4-encoded proteins as a type I secretion system (T1SS) and identify SiiE as the substrate protein of the T1SS. SiiE is secreted into the culture medium but mediates contact-dependent adhesion to epithelial cell surfaces. SiiE is a very large non-fimbrial adhesin of 600 kDa and consists of 53 repeats of Ig domains. Our study describes the first T1SS-secreted protein that functions as a non-fimbrial adhesin in binding to eukaryotic cells. The SPI4-encoded T1SS and SiiE might functionally resemble the type I fimbrial adhesins.