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Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: assessment with novel Amytracker™ stains

View ORCID ProfileEtheresia Pretorius, Martin J Page, Lisa Hendricks, Nondumiso B Nkosi, Sven R Benson, View ORCID ProfileDouglas B Kell
doi: https://doi.org/10.1101/143867
Etheresia Pretorius
1Department of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 MATIELAND, 7602, SOUTH AFRICA
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Martin J Page
1Department of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 MATIELAND, 7602, SOUTH AFRICA
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Lisa Hendricks
1Department of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 MATIELAND, 7602, SOUTH AFRICA
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Nondumiso B Nkosi
1Department of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 MATIELAND, 7602, SOUTH AFRICA
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Sven R Benson
1Department of Physiological Sciences, Stellenbosch University, Stellenbosch Private Bag X1 MATIELAND, 7602, SOUTH AFRICA
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Douglas B Kell
2School of Chemistry
3The Manchester Institute of Biotechnology
4Centre for Synthetic Biology of Fine and Speciality Chemicals, The University of Manchester, 131 Princess St, MANCHESTER M1 7DN, Lancs, UK
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Abstract

In recent work, we discovered that the presence of highly substoichiometric amounts (10-8 molar ratio) of lipopolysaccharide (LPS) from Gram-negative bacteria caused fibrinogen clotting to lead to the formation of an amyloid form of fibrin. We here show that the broadly equivalent lipoteichoic acids (LTAs) from two species of Gram-positive bacteria have similarly (if not more) potent effects. Using thioflavin T fluorescence to detect amyloid as before, the addition of low concentrations of free ferric ion is found to have similar effects. Luminescent conjugated oligothiophene dyes (LCOs), marketed under the trade name AmytrackerTM, also stain classical amyloid structures. We here show that they too give very large fluorescence enhancements when clotting is initiated in the presence of the four amyloidogens (LPS, ferric ions and two LTA types). The staining patterns differ significantly as a function of both the amyloidogens and the dyes used to assess them, indicating clearly that the nature of the clots formed is different. This is also the case when clotting is measured viscometrically using thermoelastography. Overall, the data provide further evidence for an important role of bacterial cell wall products in the various coagulopathies that are observable in chronic, inflammatory diseases. The assays may have potential in both diagnostics and therapeutics.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted May 30, 2017.
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Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: assessment with novel Amytracker™ stains
Etheresia Pretorius, Martin J Page, Lisa Hendricks, Nondumiso B Nkosi, Sven R Benson, Douglas B Kell
bioRxiv 143867; doi: https://doi.org/10.1101/143867
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Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: assessment with novel Amytracker™ stains
Etheresia Pretorius, Martin J Page, Lisa Hendricks, Nondumiso B Nkosi, Sven R Benson, Douglas B Kell
bioRxiv 143867; doi: https://doi.org/10.1101/143867

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