Identification of an antimicrobial peptide from human methionine sulfoxide reductase B3

Title
Identification of an antimicrobial peptide from human methionine sulfoxide reductase B3
Author(s)
김화영김용준[김용준]곽근희[곽근희]이추희
Keywords
MECHANISM; MAMMALS; LIVER
Issue Date
201110
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Citation
BMB REPORTS, v.44, no.10, pp.669 - 673
Abstract
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 Arg- and Pro-rich region and a potential hydrophobic a-helical segment that contains 4 cysteine residues. The potential a-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. colt, Klebsiella pneumoniae, and Salmonella paratyphi, but had no bactericidal activity against Gram-positive Staphylococcus aureus. [BMB reports 2011; 44(10): 669-673]
URI
http://hdl.handle.net/YU.REPOSITORY/24435http://dx.doi.org/10.5483/BMBRep.2011.44.10.669
ISSN
1976-6696
Appears in Collections:
의과대학 > 생화학.분자생물학교실 > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE