Identification of an antimicrobial peptide from human methionine sulfoxide reductase B3.
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.
Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu, Korea.
Yongjoon
Y
Kim
Geun-Hee
GH
Kwak
Chuhee
C
Lee
Hwa-Young
HY
Kim
D000890:Anti-Infective Agents / Q000737:chemistry / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D006090:Gram-Negative Bacteria / Q000187:drug effects*; D006094:Gram-Positive Bacteria / Q000187:drug effects*; D006801:Humans; D051150:Methionine Sulfoxide Reductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008826:Microbial Sensitivity Tests; D008958:Models, Molecular; D011487:Protein Conformation; D021382:Protein Sorting Signals / Q000235:genetics*
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D021382:Protein Sorting Signals; D051150:Methionine Sulfoxide Reductases; C524352:MSRB3 protein, human