Macin Family of Antimicrobial Proteins Combines Antimicrobial and Nerve Repair Activities

Jung, Sascha, Sönnichsen, Frank, Hung, Chien - Wen, Tholey, Andreas, Boidin-Wichlacz, C., Haeusgen, Wiebke, Gelhaus, Christoph , Desel, Christine , Podschun, Rainer , Waetzig, Vicki, Tasiemski, A., Leippe, Matthias and Grotzinger, Joachim (2012) Macin Family of Antimicrobial Proteins Combines Antimicrobial and Nerve Repair Activities Journal of Biological Chemistry, 287 (17). pp. 14246-14258.

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The tertiary structures of theromacin and neuromacin confirmed the macin protein family as a self-contained family of antimicrobial proteins within the superfamily of scorpion toxinlike proteins. The macins, which also comprise hydramacin-1, are antimicrobially active against Gram-positive and Gram-negative bacteria. Despite high sequence identity, the three proteins showed distinct differences with respect to their biological activity. Neuromacin exhibited a significantly stronger capacity to permeabilize the cytoplasmic membrane of Bacillus megaterium than theromacin and hydramacin-1. Accordingly, it is the only macin that displays pore-forming activity and that was potently active against Staphylococcus aureus. Moreover, neuromacin and hydramacin-1 led to an aggregation of bacterial cells that was not observed with theromacin. Analysis of the molecular surface properties of macins allowed confirmation of the barnacle model as the mechanistic model for the aggregation effect. Besides being antimicrobially active, neuromacin and theromacin, in contrast to hydramacin-1, were able to enhance the repair of leech nerves ex vivo. Notably, all three macins enhanced the viability of murine neuroblastoma cells, extending their functional characteristics. As neuromacin appears to be both a functional and structural chimera of hydramacin-1 and theromacin, the putative structural correlate responsible for the nerve repair capacity in leech was located to a cluster of six amino acid residues using the sequence similarity of surface-exposed regions.

Document Type: Article
Additional Information: Univ Kiel, Inst Biochem, D-24098 Kiel, Germany. Univ Kiel, Otto Diels Inst Organ Chem, D-24098 Kiel, Germany. Univ Kiel, Inst Zool, D-24098 Kiel, Germany. Univ Kiel, Inst Expt Med, Div Systemat Proteome Res, D-24105 Kiel, Germany. Univ Lille 1, CNRS FRE2933, Lab Neuroimmunol & Neurochim Evolut, F-59655 Villeneuve Dascq, France. Univ Hosp Schleswig Holstein, Inst Expt & Clin Pharmacol, D-24105 Kiel, Germany. Univ Hosp Schleswig Holstein, Inst Infect Med, D-24105 Kiel, Germany. Grotzinger, J (reprint author), Univ Kiel, Inst Biochem, Olshausenstr 40, D-24098 Kiel, Germany.
Keywords: macromolecular structures peptides leech system antibacterial regeneration challenge resistant defensin program
Research affiliation: Kiel University > Kiel Marine Science
Kiel University
OceanRep > The Future Ocean - Cluster of Excellence
Refereed: Yes
ISSN: 0021-9258
Projects: Future Ocean
Date Deposited: 14 May 2014 09:59
Last Modified: 02 Feb 2018 09:32

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