SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide

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

Standard

SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide. / Petrlova, Jitka; Samsudin, Firdaus; Bond, Peter J.; Schmidtchen, Artur.

In: FEBS Letters, Vol. 596, No. 19, 2022, p. 2566-2575.

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

Harvard

Petrlova, J, Samsudin, F, Bond, PJ & Schmidtchen, A 2022, 'SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide', FEBS Letters, vol. 596, no. 19, pp. 2566-2575. https://doi.org/10.1002/1873-3468.14490

APA

Petrlova, J., Samsudin, F., Bond, P. J., & Schmidtchen, A. (2022). SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide. FEBS Letters, 596(19), 2566-2575. https://doi.org/10.1002/1873-3468.14490

Vancouver

Petrlova J, Samsudin F, Bond PJ, Schmidtchen A. SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide. FEBS Letters. 2022;596(19):2566-2575. https://doi.org/10.1002/1873-3468.14490

Author

Petrlova, Jitka ; Samsudin, Firdaus ; Bond, Peter J. ; Schmidtchen, Artur. / SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide. In: FEBS Letters. 2022 ; Vol. 596, No. 19. pp. 2566-2575.

Bibtex

@article{fd9b4de2b7bb465d96d2292dea8727ab,
title = "SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide",
abstract = "SARS-CoV-2 spike (S) protein is crucial for virus invasion in COVID-19. Here, we showed that lipopolysaccharide (LPS) can trigger S protein aggregation at high doses of LPS and S protein. We demonstrated the formation of S protein aggregates by microscopy analyses, aggregation and gel shift assays. LPS at high levels boosts the formation of S protein aggregates as detected by amytracker and thioflavin T dyes that specifically bind to aggregating proteins. We validated the role of LPS by blocking the formation of aggregates by the endotoxin-scavenging thrombin-derived peptide TCP-25. Aggregation-prone sequences in S protein are predicted to be nearby LPS binding sites, while molecular simulations showed stable formation of S protein-LPS higher-order oligomers. Collectively, our results provide evidence of LPS-induced S protein aggregation.",
keywords = "COVID-19, endotoxins, inflammation, lipopolysaccharide, protein-aggregation, spike protein, C-TERMINAL FRAGMENTS",
author = "Jitka Petrlova and Firdaus Samsudin and Bond, {Peter J.} and Artur Schmidtchen",
year = "2022",
doi = "10.1002/1873-3468.14490",
language = "English",
volume = "596",
pages = "2566--2575",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "19",

}

RIS

TY - JOUR

T1 - SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide

AU - Petrlova, Jitka

AU - Samsudin, Firdaus

AU - Bond, Peter J.

AU - Schmidtchen, Artur

PY - 2022

Y1 - 2022

N2 - SARS-CoV-2 spike (S) protein is crucial for virus invasion in COVID-19. Here, we showed that lipopolysaccharide (LPS) can trigger S protein aggregation at high doses of LPS and S protein. We demonstrated the formation of S protein aggregates by microscopy analyses, aggregation and gel shift assays. LPS at high levels boosts the formation of S protein aggregates as detected by amytracker and thioflavin T dyes that specifically bind to aggregating proteins. We validated the role of LPS by blocking the formation of aggregates by the endotoxin-scavenging thrombin-derived peptide TCP-25. Aggregation-prone sequences in S protein are predicted to be nearby LPS binding sites, while molecular simulations showed stable formation of S protein-LPS higher-order oligomers. Collectively, our results provide evidence of LPS-induced S protein aggregation.

AB - SARS-CoV-2 spike (S) protein is crucial for virus invasion in COVID-19. Here, we showed that lipopolysaccharide (LPS) can trigger S protein aggregation at high doses of LPS and S protein. We demonstrated the formation of S protein aggregates by microscopy analyses, aggregation and gel shift assays. LPS at high levels boosts the formation of S protein aggregates as detected by amytracker and thioflavin T dyes that specifically bind to aggregating proteins. We validated the role of LPS by blocking the formation of aggregates by the endotoxin-scavenging thrombin-derived peptide TCP-25. Aggregation-prone sequences in S protein are predicted to be nearby LPS binding sites, while molecular simulations showed stable formation of S protein-LPS higher-order oligomers. Collectively, our results provide evidence of LPS-induced S protein aggregation.

KW - COVID-19

KW - endotoxins

KW - inflammation

KW - lipopolysaccharide

KW - protein-aggregation

KW - spike protein

KW - C-TERMINAL FRAGMENTS

U2 - 10.1002/1873-3468.14490

DO - 10.1002/1873-3468.14490

M3 - Journal article

C2 - 36050806

VL - 596

SP - 2566

EP - 2575

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 19

ER -

ID: 320392486