Antimicrobial activity of a C-terminal peptide from human extracellular superoxide dismutaseReport as inadecuate




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BMC Research Notes

, 2:136

First Online: 15 July 2009Received: 12 January 2009Accepted: 15 July 2009DOI: 10.1186-1756-0500-2-136

Cite this article as: Pasupuleti, M., Davoudi, M., Malmsten, M. et al. BMC Res Notes 2009 2: 136. doi:10.1186-1756-0500-2-136

Abstract

BackgroundAntimicrobial peptides AMP are important effectors of the innate immune system. Although there is increasing evidence that AMPs influence bacteria in a multitude of ways, bacterial wall rupture plays the pivotal role in the bactericidal action of AMPs. Structurally, AMPs share many similarities with endogenous heparin-binding peptides with respect to secondary structure, cationicity, and amphipathicity.

FindingsIn this study, we show that RQA21 RQAREHSERKKRRRESECKAA, a cationic and hydrophilic heparin-binding peptide corresponding to the C-terminal region of extracellular superoxide dismutase SOD, exerts antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Bacillus subtilis and Candida albicans. The peptide was also found to induce membrane leakage of negatively charged liposomes. However, its antibacterial effects were abrogated in physiological salt conditions as well as in plasma.

ConclusionThe results provide further evidence that heparin-binding peptide regions are multifunctional, but also illustrate that cationicity alone is not sufficient for AMP function at physiological conditions. However, our observation, apart from providing a link between heparin-binding peptides and AMPs, raises the hypothesis that proteolytically generated C-terminal SOD-derived peptides could interact with, and possibly counteract bacteria. Further studies are therefore merited to study a possible role of SOD in host defence.

Electronic supplementary materialThe online version of this article doi:10.1186-1756-0500-2-136 contains supplementary material, which is available to authorized users.

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Author: Mukesh Pasupuleti - Mina Davoudi - Martin Malmsten - Artur Schmidtchen

Source: https://link.springer.com/







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