5a0n: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a0n RCSB], [http://www.ebi.ac.uk/pdbsum/5a0n PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a0n RCSB], [http://www.ebi.ac.uk/pdbsum/5a0n PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
An internal thioester in a pathogen surface protein mediates covalent host binding.,Walden M, Edwards JM, Dziewulska AM, Bergmann R, Saalbach G, Kan SY, Miller OK, Weckener M, Jackson RJ, Shirran SL, Botting CH, Florence GJ, Rohde M, Banfield MJ, Schwarz-Linek U Elife. 2015 Jun 2;4. doi: 10.7554/eLife.06638. PMID:26032562<ref>PMID:26032562</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:31, 10 June 2015
N-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniaeN-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniae
Structural highlights
Publication Abstract from PubMedTo 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. An internal thioester in a pathogen surface protein mediates covalent host binding.,Walden M, Edwards JM, Dziewulska AM, Bergmann R, Saalbach G, Kan SY, Miller OK, Weckener M, Jackson RJ, Shirran SL, Botting CH, Florence GJ, Rohde M, Banfield MJ, Schwarz-Linek U Elife. 2015 Jun 2;4. doi: 10.7554/eLife.06638. PMID:26032562[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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