An internal thioester in a pathogen surface protein mediates covalent host binding
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...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
2015
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| Subjects: | |
| Online Access: | http://eprints.unisza.edu.my/6442/1/FH02-FSK-15-03509.jpg http://eprints.unisza.edu.my/6442/ |
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| Institution: | Universiti Sultan Zainal Abidin |
| Language: | English |
| Summary: | 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. |
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