SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide
(2022) In FEBS Letters 596(19). p.2566-2575- 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... (More)
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.
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- author
- Petrlova, Jitka LU ; Samsudin, Firdaus ; Bond, Peter J. and Schmidtchen, Artur LU
- organization
- publishing date
- 2022-10
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- COVID-19, endotoxins, inflammation, lipopolysaccharide, protein-aggregation, spike protein
- in
- FEBS Letters
- volume
- 596
- issue
- 19
- pages
- 10 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:36050806
- scopus:85137838999
- ISSN
- 0014-5793
- DOI
- 10.1002/1873-3468.14490
- language
- English
- LU publication?
- yes
- id
- 555d1f82-97b0-4720-a6cd-49b3e10a50a8
- date added to LUP
- 2022-12-05 16:00:29
- date last changed
- 2024-07-11 23:36:34
@article{555d1f82-97b0-4720-a6cd-49b3e10a50a8,
abstract = {{<p>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.</p>}},
author = {{Petrlova, Jitka and Samsudin, Firdaus and Bond, Peter J. and Schmidtchen, Artur}},
issn = {{0014-5793}},
keywords = {{COVID-19; endotoxins; inflammation; lipopolysaccharide; protein-aggregation; spike protein}},
language = {{eng}},
number = {{19}},
pages = {{2566--2575}},
publisher = {{Wiley-Blackwell}},
series = {{FEBS Letters}},
title = {{SARS-CoV-2 spike protein aggregation is triggered by bacterial lipopolysaccharide}},
url = {{http://dx.doi.org/10.1002/1873-3468.14490}},
doi = {{10.1002/1873-3468.14490}},
volume = {{596}},
year = {{2022}},
}