Nanobody mediated inhibition of attachment of F18 fimbriae expressing Escherichia coli
- Author
- Kristof Moonens, Maia De Kerpel, Annelies Coddens (UGent) , Eric Cox (UGent) , Els Pardon, Han Remaut and Henri De Greve
- Organization
- Abstract
- Post-weaning diarrhea and edema disease caused by F18 fimbriated E. coli are important diseases in newly weaned piglets and lead to severe production losses in farming industry. Protective treatments against these infections have thus far limited efficacy. In this study we generated nanobodies directed against the lectin domain of the F18 fimbrial adhesin FedF and showed in an in vitro adherence assay that four unique nanobodies inhibit the attachment of F18 fimbriated E. coli bacteria to piglet enterocytes. Crystallization of the FedF lectin domain with the most potent inhibitory nanobodies revealed their mechanism of action. These either competed with the binding of the blood group antigen receptor on the FedF surface or induced a conformational change in which the CDR3 region of the nanobody displaces the D ''-E loop adjacent to the binding site. This D ''-E loop was previously shown to be required for the interaction between F18 fimbriated bacteria and blood group antigen receptors in a membrane context. This work demonstrates the feasibility of inhibiting the attachment of fimbriated pathogens by employing nanobodies directed against the adhesin domain.
- Keywords
- URINARY-TRACT-INFECTIONS, GALABIOSE DERIVATIVES, DOMAIN ANTIBODY FRAGMENTS, FIMH ANTAGONISTS, EDEMA DISEASE, F107 FIMBRIAE, ADHESIN FEDF, PIGS, RECEPTOR, BINDING
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-5850261
- MLA
- Moonens, Kristof, et al. “Nanobody Mediated Inhibition of Attachment of F18 Fimbriae Expressing Escherichia Coli.” PLOS ONE, vol. 9, no. 12, 2014, doi:10.1371/journal.pone.0114691.
- APA
- Moonens, K., De Kerpel, M., Coddens, A., Cox, E., Pardon, E., Remaut, H., & De Greve, H. (2014). Nanobody mediated inhibition of attachment of F18 fimbriae expressing Escherichia coli. PLOS ONE, 9(12). https://doi.org/10.1371/journal.pone.0114691
- Chicago author-date
- Moonens, Kristof, Maia De Kerpel, Annelies Coddens, Eric Cox, Els Pardon, Han Remaut, and Henri De Greve. 2014. “Nanobody Mediated Inhibition of Attachment of F18 Fimbriae Expressing Escherichia Coli.” PLOS ONE 9 (12). https://doi.org/10.1371/journal.pone.0114691.
- Chicago author-date (all authors)
- Moonens, Kristof, Maia De Kerpel, Annelies Coddens, Eric Cox, Els Pardon, Han Remaut, and Henri De Greve. 2014. “Nanobody Mediated Inhibition of Attachment of F18 Fimbriae Expressing Escherichia Coli.” PLOS ONE 9 (12). doi:10.1371/journal.pone.0114691.
- Vancouver
- 1.Moonens K, De Kerpel M, Coddens A, Cox E, Pardon E, Remaut H, et al. Nanobody mediated inhibition of attachment of F18 fimbriae expressing Escherichia coli. PLOS ONE. 2014;9(12).
- IEEE
- [1]K. Moonens et al., “Nanobody mediated inhibition of attachment of F18 fimbriae expressing Escherichia coli,” PLOS ONE, vol. 9, no. 12, 2014.
@article{5850261, abstract = {{Post-weaning diarrhea and edema disease caused by F18 fimbriated E. coli are important diseases in newly weaned piglets and lead to severe production losses in farming industry. Protective treatments against these infections have thus far limited efficacy. In this study we generated nanobodies directed against the lectin domain of the F18 fimbrial adhesin FedF and showed in an in vitro adherence assay that four unique nanobodies inhibit the attachment of F18 fimbriated E. coli bacteria to piglet enterocytes. Crystallization of the FedF lectin domain with the most potent inhibitory nanobodies revealed their mechanism of action. These either competed with the binding of the blood group antigen receptor on the FedF surface or induced a conformational change in which the CDR3 region of the nanobody displaces the D ''-E loop adjacent to the binding site. This D ''-E loop was previously shown to be required for the interaction between F18 fimbriated bacteria and blood group antigen receptors in a membrane context. This work demonstrates the feasibility of inhibiting the attachment of fimbriated pathogens by employing nanobodies directed against the adhesin domain.}}, articleno = {{e114691}}, author = {{Moonens, Kristof and De Kerpel, Maia and Coddens, Annelies and Cox, Eric and Pardon, Els and Remaut, Han and De Greve, Henri}}, issn = {{1932-6203}}, journal = {{PLOS ONE}}, keywords = {{URINARY-TRACT-INFECTIONS,GALABIOSE DERIVATIVES,DOMAIN ANTIBODY FRAGMENTS,FIMH ANTAGONISTS,EDEMA DISEASE,F107 FIMBRIAE,ADHESIN FEDF,PIGS,RECEPTOR,BINDING}}, language = {{eng}}, number = {{12}}, pages = {{20}}, title = {{Nanobody mediated inhibition of attachment of F18 fimbriae expressing Escherichia coli}}, url = {{http://doi.org/10.1371/journal.pone.0114691}}, volume = {{9}}, year = {{2014}}, }
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