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J. Biol. Chem., Vol. 275, Issue 27, 20374-20381, July 7, 2000
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Thrombocidins, Microbicidal Proteins from Human Blood Platelets, Are C-terminal Deletion Products of CXC Chemokines*

Jeroen KrijgsveldDagger §, Sebastian A. J. ZaatDagger , Jan MeeldijkDagger ||, Peter A. van Veelen**, Gang FangDagger Dagger , Bert PoolmanDagger Dagger , Ernst Brandt§§¶¶, Jan E. Ehlert§§¶¶, Alma J. Kuijpers§||||, Gerard H. M. Engbers||||, Jan Feijen||||, and Jacob DankertDagger

From the Dagger  Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands, the ** Department of Immunohematology and Blood Bank, Leiden University Medical Center, 2333 AA Leiden, The Netherlands, the Dagger Dagger  Department of Microbiology, University of Groningen, 97-51 AA Haren, The Netherlands, the §§ Department of Immunology and Cell Biology, Forschungszentrum Borstel, D-23845 Borstel, Germany, and the |||| Department of Chemical Technology, Institute of Biomedical Technology, University of Twente, 7500 AE Enschede, The Netherlands

Antibacterial proteins are components of the innate immune system found in many organisms and produced by a variety of cell types. Human blood platelets contain a number of antibacterial proteins in their alpha -granules that are released upon thrombin activation. The present study was designed to purify these proteins obtained from human platelets and to characterize them chemically and biologically. Two antibacterial proteins were purified from platelet granules in a two-step protocol using cation exchange chromatography and continuous acid urea polyacrylamide gel electrophoresis and were designated thrombocidin (TC)-1 and TC-2. Characterization of these proteins using mass spectrometry and N-terminal sequencing revealed that TC-1 and TC-2 are variants of the CXC chemokines neutrophil-activating peptide-2 and connective tissue-activating peptide-III, respectively. TC-1 and TC-2 differ from these chemokines by a C-terminal truncation of 2 amino acids. Both TCs, but not neutrophil-activating peptide-2 and connective tissue-activating peptide-III, were bactericidal for Bacillus subtilis, Escherichia coli, Staphylococcus aureus, and Lactococcus lactis and fungicidal for Cryptococcus neoformans. Killing of B. subtilis by either TC appeared to be very rapid. Because TCs were unable to dissipate the membrane potential of L. lactis, the mechanism of TC-mediated killing most probably does not involve pore formation.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by Dutch Organization for Scientific Research (NWO) Grant 902-35-105.

To whom correspondence should be addressed: Academic Medical Center, Dept. of Medical Microbiology, Rm. L1-163, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands. Tel.: 31205664863; Fax: 31206979271; E-mail: S.A.Zaat@amc.uva.nl.

|| Supported by Netherlands Heart Foundation Grant 94.129.

¶¶ Supported in part by the Deutsche Forschungsgemeinschaft, Sonderforschungsbereich 367, Projekt C4.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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