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KMID : 0624620110440100669
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BMB Reports
2011 Volume.44 No. 10 p.669 ~ p.673
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Identification of an antimicrobial peptide from human methionine sulfoxide reductase B3
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Kim Yong-Joon
Kwak Geun-Hee
Lee Chu-Hee
Kim Hwa-Young
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Abstract
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Human methionine sulfoxide reductase B3A (hMsrB3A) is an endoplasmic reticulum (ER) reductase that catalyzes the stereospecific reduction of methionine-R-sulfoxide to methionine in proteins. In this work, we identified an antimicrobial peptide from hMsrB3A protein. The N-terminal ER-targeting signal peptide (amino acids 1-31) conferred an antimicrobial effect in Escherichia coli cells. Sequence and structural analyses showed that the overall positively charged ER signal peptide had an Argand Pro-rich region and a potential hydrophobic α-helical segment that contains 4 cysteine residues. The potential α-helical region was essential for the antimicrobial activity within E. coli cells. A synthetic peptide, comprised of 2-26 amino acids of the signal peptide, was effective at killing Gram-negative E. coli, Klebsiella pneumoniae, and Salmonella paratyphi, but had no bactericidal activity against Gram-positive Staphylococcus aureus.
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KEYWORD
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Antimicrobial peptide, Endoplasmic reticulum signal peptide, Methionine sulfoxide reductase, MsrB3
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