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Polyphosphates form antigenic complexes with platelet factor 4 (PF4) and enhance PF4-binding to bacteria

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Polyphosphates form antigenic complexes with platelet factor 4 (PF4) and enhance PF4-binding to bacteria. / Brandt, Sven; Krauel, Krystin; Jaax, Miriam; Renné, Thomas; Helm, Christiane A; Hammerschmidt, Sven; Delcea, Mihaela; Greinacher, Andreas.

In: THROMB HAEMOSTASIS, Vol. 114, No. 6, 25.11.2015, p. 1189-98.

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

Harvard

Brandt, S, Krauel, K, Jaax, M, Renné, T, Helm, CA, Hammerschmidt, S, Delcea, M & Greinacher, A 2015, 'Polyphosphates form antigenic complexes with platelet factor 4 (PF4) and enhance PF4-binding to bacteria', THROMB HAEMOSTASIS, vol. 114, no. 6, pp. 1189-98. https://doi.org/10.1160/TH15-01-0062

APA

Brandt, S., Krauel, K., Jaax, M., Renné, T., Helm, C. A., Hammerschmidt, S., Delcea, M., & Greinacher, A. (2015). Polyphosphates form antigenic complexes with platelet factor 4 (PF4) and enhance PF4-binding to bacteria. THROMB HAEMOSTASIS, 114(6), 1189-98. https://doi.org/10.1160/TH15-01-0062

Vancouver

Brandt S, Krauel K, Jaax M, Renné T, Helm CA, Hammerschmidt S et al. Polyphosphates form antigenic complexes with platelet factor 4 (PF4) and enhance PF4-binding to bacteria. THROMB HAEMOSTASIS. 2015 Nov 25;114(6):1189-98. https://doi.org/10.1160/TH15-01-0062

Bibtex

@article{ba32d0bf7856480da82257ea8da0e225,
title = "Polyphosphates form antigenic complexes with platelet factor 4 (PF4) and enhance PF4-binding to bacteria",
abstract = "Short chain polyphosphates (polyP) are pro-coagulant and pro-inflammatory platelet released inorganic polymers. The platelet chemokine platelet factor 4 (PF4) binds to lipid A on bacteria, inducing an antibody mediated host defense mechanism, which can be misdirected against PF4/heparin complexes leading to the adverse drug reaction heparin-induced thrombocytopenia (HIT). Here, we demonstrate that PF4 complex formation with soluble short chain polyP contributes to host defense mechanisms. Circular dichroism spectroscopy and isothermal titration calorimetry revealed that PF4 changed its structure upon binding to polyP in a similar way as seen in PF4/heparin complexes. Consequently, PF4/polyP complexes exposed neoepitopes to which human anti-PF4/heparin antibodies bound. PolyP enhanced binding of PF4 to Escherichia coli, hereby facilitating bacterial opsonisation and, in the presence of human anti-PF4/polyanion antibodies, phagocytosis. Our study indicates a role of polyP in enhancing PF4-mediated defense mechanisms of innate immunity.",
author = "Sven Brandt and Krystin Krauel and Miriam Jaax and Thomas Renn{\'e} and Helm, {Christiane A} and Sven Hammerschmidt and Mihaela Delcea and Andreas Greinacher",
year = "2015",
month = nov,
day = "25",
doi = "10.1160/TH15-01-0062",
language = "English",
volume = "114",
pages = "1189--98",
journal = "THROMB HAEMOSTASIS",
issn = "0340-6245",
publisher = "Schattauer",
number = "6",

}

RIS

TY - JOUR

T1 - Polyphosphates form antigenic complexes with platelet factor 4 (PF4) and enhance PF4-binding to bacteria

AU - Brandt, Sven

AU - Krauel, Krystin

AU - Jaax, Miriam

AU - Renné, Thomas

AU - Helm, Christiane A

AU - Hammerschmidt, Sven

AU - Delcea, Mihaela

AU - Greinacher, Andreas

PY - 2015/11/25

Y1 - 2015/11/25

N2 - Short chain polyphosphates (polyP) are pro-coagulant and pro-inflammatory platelet released inorganic polymers. The platelet chemokine platelet factor 4 (PF4) binds to lipid A on bacteria, inducing an antibody mediated host defense mechanism, which can be misdirected against PF4/heparin complexes leading to the adverse drug reaction heparin-induced thrombocytopenia (HIT). Here, we demonstrate that PF4 complex formation with soluble short chain polyP contributes to host defense mechanisms. Circular dichroism spectroscopy and isothermal titration calorimetry revealed that PF4 changed its structure upon binding to polyP in a similar way as seen in PF4/heparin complexes. Consequently, PF4/polyP complexes exposed neoepitopes to which human anti-PF4/heparin antibodies bound. PolyP enhanced binding of PF4 to Escherichia coli, hereby facilitating bacterial opsonisation and, in the presence of human anti-PF4/polyanion antibodies, phagocytosis. Our study indicates a role of polyP in enhancing PF4-mediated defense mechanisms of innate immunity.

AB - Short chain polyphosphates (polyP) are pro-coagulant and pro-inflammatory platelet released inorganic polymers. The platelet chemokine platelet factor 4 (PF4) binds to lipid A on bacteria, inducing an antibody mediated host defense mechanism, which can be misdirected against PF4/heparin complexes leading to the adverse drug reaction heparin-induced thrombocytopenia (HIT). Here, we demonstrate that PF4 complex formation with soluble short chain polyP contributes to host defense mechanisms. Circular dichroism spectroscopy and isothermal titration calorimetry revealed that PF4 changed its structure upon binding to polyP in a similar way as seen in PF4/heparin complexes. Consequently, PF4/polyP complexes exposed neoepitopes to which human anti-PF4/heparin antibodies bound. PolyP enhanced binding of PF4 to Escherichia coli, hereby facilitating bacterial opsonisation and, in the presence of human anti-PF4/polyanion antibodies, phagocytosis. Our study indicates a role of polyP in enhancing PF4-mediated defense mechanisms of innate immunity.

U2 - 10.1160/TH15-01-0062

DO - 10.1160/TH15-01-0062

M3 - SCORING: Journal article

C2 - 26225544

VL - 114

SP - 1189

EP - 1198

JO - THROMB HAEMOSTASIS

JF - THROMB HAEMOSTASIS

SN - 0340-6245

IS - 6

ER -