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An internal thioester in a pathogen surface protein mediates covalent host binding.
Walden, Miriam Edwards, John M Dziewulska, Aleksandra M Bergmann, Rene Saalbach, Gerhard Kan, Su-Yin Miller, Ona K Weckener, Miriam Jackson, Rosemary J Shirran, Sally L
Walden, Miriam
Edwards, John M
Dziewulska, Aleksandra M
Bergmann, Rene
Saalbach, Gerhard
Kan, Su-Yin
Miller, Ona K
Weckener, Miriam
Jackson, Rosemary J
Shirran, Sally L
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Abstract
To cause disease and persist in a host, pathogenic and commensal microbes must adhere to tissues. Colonization and infection depend on specific molecular interactions at the host-microbe interface that involve microbial surface proteins, or adhesins. To date, adhesins are only known to bind to host receptors non-covalently. Here we show that the streptococcal surface protein SfbI mediates covalent interaction with the host protein fibrinogen using an unusual internal thioester bond as a 'chemical harpoon'. This cross-linking reaction allows bacterial attachment to fibrin and SfbI binding to human cells in a model of inflammation. Thioester-containing domains are unexpectedly prevalent in Gram-positive bacteria, including many clinically relevant pathogens. Our findings support bacterial-encoded covalent binding as a new molecular principle in host-microbe interactions. This represents an as yet unexploited target to treat bacterial infection and may also offer novel opportunities for engineering beneficial interactions.
Citation
An internal thioester in a pathogen surface protein mediates covalent host binding. 2015, 4: Elife
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Journal
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Article
Language
en
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Series/Report no.
ISSN
2050-084X