Molecular interactions and inhibition of the staphylococcal biofilm-forming protein SdrC
Staphylococcus aureus forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic interactions between these proteins represent an important mechanism of cell accumulation during biofilm formation, but the underlying molec...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 114; no. 14; pp. 3738 - 3743 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
National Academy of Sciences
04.04.2017
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Abstract | Staphylococcus aureus forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic interactions between these proteins represent an important mechanism of cell accumulation during biofilm formation, but the underlying molecular mechanisms are still not well-understood. Here we report the direct measurement of homophilic binding forces by the serine-aspartate repeat protein SdrC and their inhibition by a peptide. Using single-cell and single-molecule force measurements, we find that SdrC is engaged in low-affinity homophilic bonds that promote cell–cell adhesion. Low-affinity intercellular adhesion may play a role in favoring biofilm dynamics. We show that SdrC also mediates strong cellular interactions with hydrophobic surfaces, which are likely to be involved in the initial attachment to biomaterials, the first stage of biofilm formation. Furthermore, we demonstrate that a peptide derived from β-neurexin is a powerful competitive inhibitor capable of efficiently blocking surface attachment, homophilic adhesion, and biofilm accumulation. Molecular modeling suggests that this blocking activity may originate from binding of the peptide to a sequence of SdrC involved in homophilic interactions. Our study opens up avenues for understanding the role of homophilic interactions in staphylococcal adhesion, and for the design of new molecules to prevent biofilm formation during infection. |
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AbstractList | Staphylococcus aureus forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic interactions between these proteins represent an important mechanism of cell accumulation during biofilm formation, but the underlying molecular mechanisms are still not well-understood. Here we report the direct measurement of homophilic binding forces by the serine-aspartate repeat protein SdrC and their inhibition by a peptide. Using single-cell and single-molecule force measurements, we find that SdrC is engaged in low-affinity homophilic bonds that promote cell-cell adhesion. Low-affinity intercellular adhesion may play a role in favoring biofilm dynamics. We show that SdrC also mediates strong cellular interactions with hydrophobic surfaces, which are likely to be involved in the initial attachment to biomaterials, the first stage of biofilm formation. Furthermore, we demonstrate that a peptide derived from β-neurexin is a powerful competitive inhibitor capable of efficiently blocking surface attachment, homophilic adhesion, and biofilm accumulation. Molecular modeling suggests that this blocking activity may originate from binding of the peptide to a sequence of SdrC involved in homophilic interactions. Our study opens up avenues for understanding the role of homophilic interactions in staphylococcal adhesion, and for the design of new molecules to prevent biofilm formation during infection. forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic interactions between these proteins represent an important mechanism of cell accumulation during biofilm formation, but the underlying molecular mechanisms are still not well-understood. Here we report the direct measurement of homophilic binding forces by the serine-aspartate repeat protein SdrC and their inhibition by a peptide. Using single-cell and single-molecule force measurements, we find that SdrC is engaged in low-affinity homophilic bonds that promote cell-cell adhesion. Low-affinity intercellular adhesion may play a role in favoring biofilm dynamics. We show that SdrC also mediates strong cellular interactions with hydrophobic surfaces, which are likely to be involved in the initial attachment to biomaterials, the first stage of biofilm formation. Furthermore, we demonstrate that a peptide derived from β-neurexin is a powerful competitive inhibitor capable of efficiently blocking surface attachment, homophilic adhesion, and biofilm accumulation. Molecular modeling suggests that this blocking activity may originate from binding of the peptide to a sequence of SdrC involved in homophilic interactions. Our study opens up avenues for understanding the role of homophilic interactions in staphylococcal adhesion, and for the design of new molecules to prevent biofilm formation during infection. Significance The bacterial pathogen Staphylococcus aureus shows a remarkable ability to aggregate, thereby contributing to the formation of cellular communities that are difficult to eradicate. In this study, we dissect the homophilic interactions at play during S. aureus cell–cell adhesion, focusing on the key surface protein SdrC. We discover that SdrC is engaged in low-affinity homophilic bonds that promote intercellular adhesion, and that it also favors strong hydrophobic interactions with surfaces, emphasizing that this protein is a multifunctional adhesin. We also show that SdrC-dependent cell-surface attachment, cell–cell adhesion, and biofilm formation can be efficiently blocked by a peptide, thus suggesting this approach could be used for antibiofilm therapy. Staphylococcus aureus forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic interactions between these proteins represent an important mechanism of cell accumulation during biofilm formation, but the underlying molecular mechanisms are still not well-understood. Here we report the direct measurement of homophilic binding forces by the serine-aspartate repeat protein SdrC and their inhibition by a peptide. Using single-cell and single-molecule force measurements, we find that SdrC is engaged in low-affinity homophilic bonds that promote cell–cell adhesion. Low-affinity intercellular adhesion may play a role in favoring biofilm dynamics. We show that SdrC also mediates strong cellular interactions with hydrophobic surfaces, which are likely to be involved in the initial attachment to biomaterials, the first stage of biofilm formation. Furthermore, we demonstrate that a peptide derived from β-neurexin is a powerful competitive inhibitor capable of efficiently blocking surface attachment, homophilic adhesion, and biofilm accumulation. Molecular modeling suggests that this blocking activity may originate from binding of the peptide to a sequence of SdrC involved in homophilic interactions. Our study opens up avenues for understanding the role of homophilic interactions in staphylococcal adhesion, and for the design of new molecules to prevent biofilm formation during infection. Staphylococcus aureus forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic interactions between these proteins represent an important mechanism of cell accumulation during biofilm formation, but the underlying molecular mechanisms are still not well-understood. Here we report the direct measurement of homophilic binding forces by the serine-aspartate repeat protein SdrC and their inhibition by a peptide. Using single-cell and single-molecule force measurements, we find that SdrC is engaged in low-affinity homophilic bonds that promote cell-cell adhesion. Low-affinity intercellular adhesion may play a role in favoring biofilm dynamics. We show that SdrC also mediates strong cellular interactions with hydrophobic surfaces, which are likely to be involved in the initial attachment to biomaterials, the first stage of biofilm formation. Furthermore, we demonstrate that a peptide derived from beta -neurexin is a powerful competitive inhibitor capable of efficiently blocking surface attachment, homophilic adhesion, and biofilm accumulation. Molecular modeling suggests that this blocking activity may originate from binding of the peptide to a sequence of SdrC involved in homophilic interactions. Our study opens up avenues for understanding the role of homophilic interactions in staphylococcal adhesion, and for the design of new molecules to prevent biofilm formation during infection. The bacterial pathogen Staphylococcus aureus shows a remarkable ability to aggregate, thereby contributing to the formation of cellular communities that are difficult to eradicate. In this study, we dissect the homophilic interactions at play during S. aureus cell–cell adhesion, focusing on the key surface protein SdrC. We discover that SdrC is engaged in low-affinity homophilic bonds that promote intercellular adhesion, and that it also favors strong hydrophobic interactions with surfaces, emphasizing that this protein is a multifunctional adhesin. We also show that SdrC-dependent cell-surface attachment, cell–cell adhesion, and biofilm formation can be efficiently blocked by a peptide, thus suggesting this approach could be used for antibiofilm therapy. Staphylococcus aureus forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic interactions between these proteins represent an important mechanism of cell accumulation during biofilm formation, but the underlying molecular mechanisms are still not well-understood. Here we report the direct measurement of homophilic binding forces by the serine-aspartate repeat protein SdrC and their inhibition by a peptide. Using single-cell and single-molecule force measurements, we find that SdrC is engaged in low-affinity homophilic bonds that promote cell–cell adhesion. Low-affinity intercellular adhesion may play a role in favoring biofilm dynamics. We show that SdrC also mediates strong cellular interactions with hydrophobic surfaces, which are likely to be involved in the initial attachment to biomaterials, the first stage of biofilm formation. Furthermore, we demonstrate that a peptide derived from β-neurexin is a powerful competitive inhibitor capable of efficiently blocking surface attachment, homophilic adhesion, and biofilm accumulation. Molecular modeling suggests that this blocking activity may originate from binding of the peptide to a sequence of SdrC involved in homophilic interactions. Our study opens up avenues for understanding the role of homophilic interactions in staphylococcal adhesion, and for the design of new molecules to prevent biofilm formation during infection. |
Author | Hays, Leanne M. C. Formosa-Dague, Cécile Geoghegan, Joan A. Feuillie, Cécile Dufrêne, Yves F. Vervaeck, Ophélie Foster, Timothy J. Derclaye, Sylvie Brennan, Marian P. |
Author_xml | – sequence: 1 givenname: Cécile surname: Feuillie fullname: Feuillie, Cécile organization: Institute of Life Sciences, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium – sequence: 2 givenname: Cécile surname: Formosa-Dague fullname: Formosa-Dague, Cécile organization: Institute of Life Sciences, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium – sequence: 3 givenname: Leanne M. C. surname: Hays fullname: Hays, Leanne M. C. organization: Department of Microbiology, Moyne Institute of Preventive Medicine, School of Genetics and Microbiology, Trinity College Dublin, Dublin 2, Ireland – sequence: 4 givenname: Ophélie surname: Vervaeck fullname: Vervaeck, Ophélie organization: Institute of Life Sciences, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium – sequence: 5 givenname: Sylvie surname: Derclaye fullname: Derclaye, Sylvie organization: Institute of Life Sciences, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium – sequence: 6 givenname: Marian P. surname: Brennan fullname: Brennan, Marian P. organization: Molecular and Cellular Therapeutics, Irish Centre for Vascular Biology, Royal College of Surgeons in Ireland, Dublin 2, Ireland – sequence: 7 givenname: Timothy J. surname: Foster fullname: Foster, Timothy J. organization: Department of Microbiology, Moyne Institute of Preventive Medicine, School of Genetics and Microbiology, Trinity College Dublin, Dublin 2, Ireland – sequence: 8 givenname: Joan A. surname: Geoghegan fullname: Geoghegan, Joan A. organization: Department of Microbiology, Moyne Institute of Preventive Medicine, School of Genetics and Microbiology, Trinity College Dublin, Dublin 2, Ireland – sequence: 9 givenname: Yves F. surname: Dufrêne fullname: Dufrêne, Yves F. organization: Walloon Excellence in Life Sciences and Biotechnology (WELBIO), 1300 Wavre, Belgium |
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DocumentTitleAlternate | Adhesion and inhibition of SdrC |
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Keywords | inhibition adhesion SdrC biofilms Staphylococcus aureus |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 PMCID: PMC5389287 1C.F., C.F.-D., and L.M.C.H. contributed equally to his work. Author contributions: C.F., C.F.-D., L.M.C.H., O.V., S.D., M.B., T.J.F., J.A.G., and Y.F.D. designed research; C.F., C.F.-D., L.M.C.H., O.V., and S.D. performed research; C.F., C.F.-D., L.M.C.H., O.V., S.D., M.B., T.J.F., J.A.G., and Y.F.D. analyzed data; and C.F., C.F.-D., L.M.C.H., O.V., S.D., M.B., T.J.F., J.A.G., and Y.F.D. wrote the paper. Edited by Richard P. Novick, New York University School of Medicine, New York, NY, and approved February 27, 2017 (received for review October 11, 2016) |
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Snippet | Staphylococcus aureus forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic... forms biofilms on indwelling medical devices using a variety of cell-surface proteins. There is growing evidence that specific homophilic interactions between... Significance The bacterial pathogen Staphylococcus aureus shows a remarkable ability to aggregate, thereby contributing to the formation of cellular... The bacterial pathogen Staphylococcus aureus shows a remarkable ability to aggregate, thereby contributing to the formation of cellular communities that are... |
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SubjectTerms | Bacterial Adhesion Bacterial Proteins - antagonists & inhibitors Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biochemistry, Molecular Biology Biofilms Biological Sciences Biophysics Hydrophobic and Hydrophilic Interactions Life Sciences Models, Molecular Molecules Nerve Tissue Proteins - chemistry Peptides - chemistry Peptides - pharmacology Protein Binding Proteins Single-Cell Analysis Staphylococcus aureus Staphylococcus aureus - physiology Staphylococcus infections |
Title | Molecular interactions and inhibition of the staphylococcal biofilm-forming protein SdrC |
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