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The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin. / Khan, Nasar; Aslan, Hüsnü; Büttner, Henning et al.

In: eLife, Vol. 11, e76164, 07.2022.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Khan, N, Aslan, H, Büttner, H, Rohde, H, Golbek, TW, Roeters, SJ, Woutersen, S, Weidner, T & Meyer, RL 2022, 'The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin', eLife, vol. 11, e76164. https://doi.org/10.7554/elife.76164

APA

Khan, N., Aslan, H., Büttner, H., Rohde, H., Golbek, T. W., Roeters, S. J., Woutersen, S., Weidner, T., & Meyer, R. L. (2022). The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin. eLife, 11, [e76164]. https://doi.org/10.7554/elife.76164

CBE

Khan N, Aslan H, Büttner H, Rohde H, Golbek TW, Roeters SJ, Woutersen S, Weidner T, Meyer RL. 2022. The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin. eLife. 11:Article e76164. https://doi.org/10.7554/elife.76164

MLA

Khan, Nasar et al. "The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin". eLife. 2022. 11. https://doi.org/10.7554/elife.76164

Vancouver

Khan N, Aslan H, Büttner H, Rohde H, Golbek TW, Roeters SJ et al. The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin. eLife. 2022 Jul;11:e76164. doi: 10.7554/elife.76164

Author

Khan, Nasar ; Aslan, Hüsnü ; Büttner, Henning et al. / The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin. In: eLife. 2022 ; Vol. 11.

Bibtex

@article{fb012b0bfe1f4a9cb0c0a898c4ffd6f9,
title = "The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin",
abstract = "Staphylococcus epidermidis causes some of the most hard-to-treat clinical infections by forming biofilms: Multicellular communities of bacteria encased in a protective matrix, supporting immune evasion and tolerance against antibiotics. Biofilms occur most commonly on medical implants, and a key event in implant colonization is the robust adherence to the surface, facilitated by interactions between bacterial surface proteins and host matrix components. S. epidermidis is equipped with a giant adhesive protein, Embp, which facilitates bacterial interactions with surface-deposited, but not soluble fibronectin. The structural basis behind this selective binding process has remained obscure. Using a suite of single-cell and single-molecule analysis techniques, we show that S. epidermidis is capable of such distinction because Embp binds specifically to fibrillated fibronectin on surfaces, while ignoring globular fibronectin in solution. S. epidermidis adherence is critically dependent on multi-valent interactions involving 50 fibronectin-binding repeats of Embp. This unusual, Velcro-like interaction proved critical for colonization of surfaces under high flow, making this newly identified attachment mechanism particularly relevant for colonization of intravascular devices, such as prosthetic heart valves or vascular grafts. Other biofilm-forming pathogens, such as Staphylococcus aureus, express homologs of Embp and likely deploy the same mechanism for surface colonization. Our results may open for a novel direction in efforts to combat devastating, biofilm-associated infections, as the development of implant materials that steer the conformation of adsorbed proteins is a much more manageable task than avoiding protein adsorption altogether.",
keywords = "ADHESIN, AFM, ATOMIC-FORCE MICROSCOPY, AUREUS, BINDING, CHEMISTRY, EPIDERMIDIS, Embp, IDENTIFICATION, INFECTIONS, Other, PLASMA, SDRG, Staphylococcus epidermidis, bacterial adhesion, fibronectin, multivalent",
author = "Nasar Khan and H{\"u}sn{\"u} Aslan and Henning B{\"u}ttner and Holger Rohde and Golbek, {Thaddeus Wayne} and Roeters, {Steven Joop} and Sander Woutersen and Tobias Weidner and Meyer, {Rikke Louise}",
note = "Publisher Copyright: {\textcopyright} 2022, eLife Sciences Publications Ltd. All rights reserved.",
year = "2022",
month = jul,
doi = "10.7554/elife.76164",
language = "English",
volume = "11",
journal = "eLife",
issn = "2050-084X",
publisher = "eLife Sciences Publications Ltd.",

}

RIS

TY - JOUR

T1 - The giant staphylococcal protein Embp facilitates colonization of surfaces through Velcro-like attachment to fibrillated fibronectin

AU - Khan, Nasar

AU - Aslan, Hüsnü

AU - Büttner, Henning

AU - Rohde, Holger

AU - Golbek, Thaddeus Wayne

AU - Roeters, Steven Joop

AU - Woutersen, Sander

AU - Weidner, Tobias

AU - Meyer, Rikke Louise

N1 - Publisher Copyright: © 2022, eLife Sciences Publications Ltd. All rights reserved.

PY - 2022/7

Y1 - 2022/7

N2 - Staphylococcus epidermidis causes some of the most hard-to-treat clinical infections by forming biofilms: Multicellular communities of bacteria encased in a protective matrix, supporting immune evasion and tolerance against antibiotics. Biofilms occur most commonly on medical implants, and a key event in implant colonization is the robust adherence to the surface, facilitated by interactions between bacterial surface proteins and host matrix components. S. epidermidis is equipped with a giant adhesive protein, Embp, which facilitates bacterial interactions with surface-deposited, but not soluble fibronectin. The structural basis behind this selective binding process has remained obscure. Using a suite of single-cell and single-molecule analysis techniques, we show that S. epidermidis is capable of such distinction because Embp binds specifically to fibrillated fibronectin on surfaces, while ignoring globular fibronectin in solution. S. epidermidis adherence is critically dependent on multi-valent interactions involving 50 fibronectin-binding repeats of Embp. This unusual, Velcro-like interaction proved critical for colonization of surfaces under high flow, making this newly identified attachment mechanism particularly relevant for colonization of intravascular devices, such as prosthetic heart valves or vascular grafts. Other biofilm-forming pathogens, such as Staphylococcus aureus, express homologs of Embp and likely deploy the same mechanism for surface colonization. Our results may open for a novel direction in efforts to combat devastating, biofilm-associated infections, as the development of implant materials that steer the conformation of adsorbed proteins is a much more manageable task than avoiding protein adsorption altogether.

AB - Staphylococcus epidermidis causes some of the most hard-to-treat clinical infections by forming biofilms: Multicellular communities of bacteria encased in a protective matrix, supporting immune evasion and tolerance against antibiotics. Biofilms occur most commonly on medical implants, and a key event in implant colonization is the robust adherence to the surface, facilitated by interactions between bacterial surface proteins and host matrix components. S. epidermidis is equipped with a giant adhesive protein, Embp, which facilitates bacterial interactions with surface-deposited, but not soluble fibronectin. The structural basis behind this selective binding process has remained obscure. Using a suite of single-cell and single-molecule analysis techniques, we show that S. epidermidis is capable of such distinction because Embp binds specifically to fibrillated fibronectin on surfaces, while ignoring globular fibronectin in solution. S. epidermidis adherence is critically dependent on multi-valent interactions involving 50 fibronectin-binding repeats of Embp. This unusual, Velcro-like interaction proved critical for colonization of surfaces under high flow, making this newly identified attachment mechanism particularly relevant for colonization of intravascular devices, such as prosthetic heart valves or vascular grafts. Other biofilm-forming pathogens, such as Staphylococcus aureus, express homologs of Embp and likely deploy the same mechanism for surface colonization. Our results may open for a novel direction in efforts to combat devastating, biofilm-associated infections, as the development of implant materials that steer the conformation of adsorbed proteins is a much more manageable task than avoiding protein adsorption altogether.

KW - ADHESIN

KW - AFM

KW - ATOMIC-FORCE MICROSCOPY

KW - AUREUS

KW - BINDING

KW - CHEMISTRY

KW - EPIDERMIDIS

KW - Embp

KW - IDENTIFICATION

KW - INFECTIONS

KW - Other

KW - PLASMA

KW - SDRG

KW - Staphylococcus epidermidis

KW - bacterial adhesion

KW - fibronectin

KW - multivalent

UR - http://www.scopus.com/inward/record.url?scp=85133881361&partnerID=8YFLogxK

U2 - 10.7554/elife.76164

DO - 10.7554/elife.76164

M3 - Journal article

C2 - 35796649

AN - SCOPUS:85133881361

VL - 11

JO - eLife

JF - eLife

SN - 2050-084X

M1 - e76164

ER -