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The Bovine Antimicrobial Peptide Lactoferricin Interacts with Polysialic Acid without Loss of Its Antimicrobial Activity against Escherichia coli

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
*
Author to whom correspondence should be addressed.
Animals 2020, 10(1), 1; https://doi.org/10.3390/ani10010001
Received: 6 November 2019 / Revised: 9 December 2019 / Accepted: 15 December 2019 / Published: 18 December 2019
(This article belongs to the Section Animal Physiology)
Bovine milk contains a high concentration of the protein lactoferrin. It is an important antimicrobial biomolecule, which is also present in other bodily fluids like blood and semen. However, not only the intact protein but also its cleavage products have antimicrobial activity. Perhaps, the best-known cleavage product of lactoferrin is the peptide lactoferricin that has significant antimicrobial capacity against a broad range of pathogens such as enterohemorrhagic Escherichia coli (EHEC). Interestingly, lactoferricin can interact with the sugar polymer polysialic acid, which is also present in milk, blood, and semen. In the present study, we tested if the binding to polysialic acid influences the biological activity of bovine lactoferricin. Remarkably, neither different amounts of polysialic acid nor different chain lengths of this sugar polymer influenced the antimicrobial activity of lactoferricin. The ability of polysialic acid to bind and not inactivate lactoferricin may allow the development of novel endogenous and biodegradable polysialylated surfaces and/or hydrogels, which can be loaded with the antimicrobial peptide lactoferricin for biomedical applications in veterinary and human medicine.
The lactoferrin-derived peptide lactoferricin (LFcin) belongs to the family of antimicrobial peptides, and its bovine form has already been successfully applied to counteract enterohemorrhagic Escherichia coli (EHEC) infection. Recently, it was described that LFcin interacts with the sugar polymer polysialic acid (polySia) and that the binding of lactoferrin to polySia is mediated by LFcin, included in the N-terminal domain of lactoferrin. For this reason, the impact of polySia on the antimicrobial activity of bovine LFcin was investigated. Initially, the interaction of LFcin was characterized in more detail by native agarose gel electrophoresis, demonstrating that a chain length of 10 sialic acid residues was necessary to bind LFcin, whereas approximately twice-as-long chains were needed to detect binding of lactoferrin. Remarkably, the binding of polySia showed, independently of the chain length, no impact on the antimicrobial effects of LFcin. Thus, LFcin binds polySia without loss of its protective activity as an antimicrobial peptide. View Full-Text
Keywords: lactoferrin; lactoferricin; polysialic acid; sialic acids; antimicrobial peptides; innate immune system lactoferrin; lactoferricin; polysialic acid; sialic acids; antimicrobial peptides; innate immune system
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MDPI and ACS Style

Kühnle, A.; Galuska, C.E.; Zlatina, K.; Galuska, S.P. The Bovine Antimicrobial Peptide Lactoferricin Interacts with Polysialic Acid without Loss of Its Antimicrobial Activity against Escherichia coli. Animals 2020, 10, 1.

AMA Style

Kühnle A, Galuska CE, Zlatina K, Galuska SP. The Bovine Antimicrobial Peptide Lactoferricin Interacts with Polysialic Acid without Loss of Its Antimicrobial Activity against Escherichia coli. Animals. 2020; 10(1):1.

Chicago/Turabian Style

Kühnle, Andrea; Galuska, Christina E.; Zlatina, Kristina; Galuska, Sebastian P. 2020. "The Bovine Antimicrobial Peptide Lactoferricin Interacts with Polysialic Acid without Loss of Its Antimicrobial Activity against Escherichia coli" Animals 10, no. 1: 1.

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