An internal thioester in a pathogen surface protein mediates covalent host binding.
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Edwards, John M
Dziewulska, Aleksandra M
Miller, Ona K
Jackson, Rosemary J
Shirran, Sally L
Botting, Catherine H
Florence, Gordon J
Banfield, Mark J
MetadataShow full item record
AbstractTo 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.
CitationAn internal thioester in a pathogen surface protein mediates covalent host binding. 2015, 4: Elife
AffiliationHelmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany.
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