Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation. / Sønderby, Thorbjørn V.; Louros, Nikolaos N.; Khodaparast, Ladan; Khodaparast, Laleh; Madsen, Daniel J.; Olsen, William P.; Moonen, Nele; Nagaraj, Madhu; Sereikaite, Vita; Strømgaard, Kristian; Rousseau, Frederic; Schymkowitz, Joost; Otzen, Daniel E.

In: Journal of Molecular Biology, Vol. 435, No. 11, 168039, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Sønderby, TV, Louros, NN, Khodaparast, L, Khodaparast, L, Madsen, DJ, Olsen, WP, Moonen, N, Nagaraj, M, Sereikaite, V, Strømgaard, K, Rousseau, F, Schymkowitz, J & Otzen, DE 2023, 'Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation', Journal of Molecular Biology, vol. 435, no. 11, 168039. https://doi.org/10.1016/j.jmb.2023.168039

APA

Sønderby, T. V., Louros, N. N., Khodaparast, L., Khodaparast, L., Madsen, D. J., Olsen, W. P., Moonen, N., Nagaraj, M., Sereikaite, V., Strømgaard, K., Rousseau, F., Schymkowitz, J., & Otzen, D. E. (2023). Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation. Journal of Molecular Biology, 435(11), [168039]. https://doi.org/10.1016/j.jmb.2023.168039

Vancouver

Sønderby TV, Louros NN, Khodaparast L, Khodaparast L, Madsen DJ, Olsen WP et al. Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation. Journal of Molecular Biology. 2023;435(11). 168039. https://doi.org/10.1016/j.jmb.2023.168039

Author

Sønderby, Thorbjørn V. ; Louros, Nikolaos N. ; Khodaparast, Ladan ; Khodaparast, Laleh ; Madsen, Daniel J. ; Olsen, William P. ; Moonen, Nele ; Nagaraj, Madhu ; Sereikaite, Vita ; Strømgaard, Kristian ; Rousseau, Frederic ; Schymkowitz, Joost ; Otzen, Daniel E. / Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation. In: Journal of Molecular Biology. 2023 ; Vol. 435, No. 11.

Bibtex

@article{e2cd766feba244c6869d63e3d07fdd2c,
title = "Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation",
abstract = "Functional bacterial amyloid provides structural stability in biofilm, making it a promising target for anti-biofilm therapeutics. Fibrils formed by CsgA, the major amyloid component in E. coli are extremely robust and can withstand very harsh conditions. Like other functional amyloids, CsgA contains relatively short aggregation-prone regions (APR) which drive amyloid formation. Here, we demonstrate the use of aggregation-modulating peptides to knock down CsgA protein into aggregates with low stability and altered morphology. Remarkably, these CsgA-peptides also modulate fibrillation of the unrelated functional amyloid protein FapC from Pseudomonas, possibly through recognition of FapC segments with structural and sequence similarity with CsgA. The peptides also reduce the level of biofilm formation in E. coli and P. aeruginosa, demonstrating the potential for selective amyloid targeting to combat bacterial biofilm.",
keywords = "amyloid inhibition, biofilm, functional bacterial amyloid, modulation, peptides",
author = "S{\o}nderby, {Thorbj{\o}rn V.} and Louros, {Nikolaos N.} and Ladan Khodaparast and Laleh Khodaparast and Madsen, {Daniel J.} and Olsen, {William P.} and Nele Moonen and Madhu Nagaraj and Vita Sereikaite and Kristian Str{\o}mgaard and Frederic Rousseau and Joost Schymkowitz and Otzen, {Daniel E.}",
note = "Publisher Copyright: {\textcopyright} 2023 The Authors",
year = "2023",
doi = "10.1016/j.jmb.2023.168039",
language = "English",
volume = "435",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "11",

}

RIS

TY - JOUR

T1 - Sequence-targeted Peptides Divert Functional Bacterial Amyloid Towards Destabilized Aggregates and Reduce Biofilm Formation

AU - Sønderby, Thorbjørn V.

AU - Louros, Nikolaos N.

AU - Khodaparast, Ladan

AU - Khodaparast, Laleh

AU - Madsen, Daniel J.

AU - Olsen, William P.

AU - Moonen, Nele

AU - Nagaraj, Madhu

AU - Sereikaite, Vita

AU - Strømgaard, Kristian

AU - Rousseau, Frederic

AU - Schymkowitz, Joost

AU - Otzen, Daniel E.

N1 - Publisher Copyright: © 2023 The Authors

PY - 2023

Y1 - 2023

N2 - Functional bacterial amyloid provides structural stability in biofilm, making it a promising target for anti-biofilm therapeutics. Fibrils formed by CsgA, the major amyloid component in E. coli are extremely robust and can withstand very harsh conditions. Like other functional amyloids, CsgA contains relatively short aggregation-prone regions (APR) which drive amyloid formation. Here, we demonstrate the use of aggregation-modulating peptides to knock down CsgA protein into aggregates with low stability and altered morphology. Remarkably, these CsgA-peptides also modulate fibrillation of the unrelated functional amyloid protein FapC from Pseudomonas, possibly through recognition of FapC segments with structural and sequence similarity with CsgA. The peptides also reduce the level of biofilm formation in E. coli and P. aeruginosa, demonstrating the potential for selective amyloid targeting to combat bacterial biofilm.

AB - Functional bacterial amyloid provides structural stability in biofilm, making it a promising target for anti-biofilm therapeutics. Fibrils formed by CsgA, the major amyloid component in E. coli are extremely robust and can withstand very harsh conditions. Like other functional amyloids, CsgA contains relatively short aggregation-prone regions (APR) which drive amyloid formation. Here, we demonstrate the use of aggregation-modulating peptides to knock down CsgA protein into aggregates with low stability and altered morphology. Remarkably, these CsgA-peptides also modulate fibrillation of the unrelated functional amyloid protein FapC from Pseudomonas, possibly through recognition of FapC segments with structural and sequence similarity with CsgA. The peptides also reduce the level of biofilm formation in E. coli and P. aeruginosa, demonstrating the potential for selective amyloid targeting to combat bacterial biofilm.

KW - amyloid inhibition

KW - biofilm

KW - functional bacterial amyloid

KW - modulation

KW - peptides

U2 - 10.1016/j.jmb.2023.168039

DO - 10.1016/j.jmb.2023.168039

M3 - Journal article

C2 - 37330291

AN - SCOPUS:85165677584

VL - 435

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 11

M1 - 168039

ER -

ID: 362338210