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Article

Polysialic Acid Modulates the Binding of External Lactoferrin in Neutrophil Extracellular Traps

1
Institute of Reproductive Biology, Leibniz Institute for Farm Animal Biology (FBN), Wilhelm-Stahl-Allee 2, 18196 Dummerstorf, Germany
2
Institute of Biochemistry, Faculty of Medicine, Justus-Liebig-University, Friedrichstr. 24, 35392 Giessen, Germany
3
Institute of Veterinary Physiology and Biochemistry, Justus-Liebig-University Giessen, Frankfurter Str. 100, 35392 Giessen, Germany
*
Author to whom correspondence should be addressed.
Current Address: GIP Gesellschaft für innovative Personalwirtschaftssysteme mbH, Strahlenbergerstr. 112, 63067 Offenbach, Germany.
Biology 2019, 8(2), 20; https://doi.org/10.3390/biology8020020
Received: 29 January 2019 / Revised: 28 February 2019 / Accepted: 21 March 2019 / Published: 28 March 2019
(This article belongs to the Special Issue Neutrophil Extracellular Traps)
Neutrophil extracellular traps (NETs) are formed by neutrophils during inflammation. Among other things, these DNA constructs consist of antimicrobial proteins such as lactoferrin and histones. With these properties, NETs capture and destroy invading microorganisms. The carbohydrate polysialic acid (polySia) interacts with both lactoferrin and histones. Previous experiments demonstrated that, in humans, lactoferrin inhibits the release of NET and that this effect is supported by polySia. In this study, we examined the interplay of lactoferrin and polySia in already-formed NETs from bovine neutrophils. The binding of polySia was considered to occur at the lactoferricin (LFcin)-containing domain of lactoferrin. The interaction with the peptide LFcin was studied in more detail using groups of defined polySia chain lengths, which suggested a chain-length-dependent interaction mechanism with LFcin. The LFcin domain of lactoferrin was found to interact with DNA. Therefore, the possibility that polySia influences the integration of lactoferrin into the DNA-structures of NETs was tested by isolating bovine neutrophils and inducing NETosis. Experiments with NET fibers saturated with lactoferrin demonstrated that polySia initiates the incorporation of external lactoferrin in already-loaded NETs. Thus, polySia may modulate the constituents of NET. View Full-Text
Keywords: polysialic acid; lactoferrin; neutrophil extracellular traps; innate immune system polysialic acid; lactoferrin; neutrophil extracellular traps; innate immune system
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MDPI and ACS Style

Kühnle, A.; Lütteke, T.; Bornhöfft, K.F.; Galuska, S.P. Polysialic Acid Modulates the Binding of External Lactoferrin in Neutrophil Extracellular Traps. Biology 2019, 8, 20. https://doi.org/10.3390/biology8020020

AMA Style

Kühnle A, Lütteke T, Bornhöfft KF, Galuska SP. Polysialic Acid Modulates the Binding of External Lactoferrin in Neutrophil Extracellular Traps. Biology. 2019; 8(2):20. https://doi.org/10.3390/biology8020020

Chicago/Turabian Style

Kühnle, Andrea, Thomas Lütteke, Kim F. Bornhöfft, and Sebastian P. Galuska 2019. "Polysialic Acid Modulates the Binding of External Lactoferrin in Neutrophil Extracellular Traps" Biology 8, no. 2: 20. https://doi.org/10.3390/biology8020020

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