Functional analysis of an α-helical antimicrobial peptide derived from a novel mouse defensin-like gene

Biochemical and Biophysical Research Communications

Volumn 398, Issue 4, 2010, Pages 778-784

  Kawaguchi, Akira ^a,b   Suzuki, Tadaki ^a,b   Kimura, Takashi ^a   Sakai, Naoki ^a   Ayabe, Tokiyoshi ^a   Sawa, Hirofumi ^a   Hasegawa, Hideki ^b  

^a HOKKAIDO UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

Author keywords

Antimicrobial peptide; Bactericidal activity; Cationic helical peptide; CD spectroscopy; Defensin

Indexed keywords

BETA DEFENSIN; DODECYL SULFATE SODIUM; K17 PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; AQUEOUS SOLUTION; ARTICLE; BACTERICIDAL ACTIVITY; CIRCULAR DICHROISM; EXON; GENE EXPRESSION; GENE LOCUS; GENE SYNTHESIS; GENOME ANALYSIS; MOUSE; NONHUMAN; OPEN READING FRAME; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; SALMONELLA TYPHIMURIUM; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; ANIMALS; BETA-DEFENSINS; CELL LINE, TUMOR; ERYTHROCYTES; EXONS; HEMOLYSIS; MICE; MICE, INBRED C57BL; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SALMONELLA TYPHIMURIUM; STAPHYLOCOCCUS AUREUS;

BACTERIA (MICROORGANISMS); MAMMALIA; NEGIBACTERIA; POSIBACTERIA; SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM; STAPHYLOCOCCUS AUREUS;

EID: 77955426168     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.07.028     Document Type: Article

References (19)

1. Brogden K. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria. Nat. Rev. Microbiol. 2005, 3:238-250.
2. Andreu D., Rivas L. Animal antimicrobial peptides: an overview. Biopolymers 1998, 47:415-433.
3. Maupetit J., Derreumaux P., Tuffery P. PEP-FOLD: an online resource for de novo peptide structure prediction. Nucleic Acids Res. 2009, 37:W498-W503.
4. Ayabe T., Satchell D., Wilson C., Parks W., Selsted M., Ouellette A. Secretion of microbicidal alpha-defensins by intestinal Paneth cells in response to bacteria. Nat. Immunol. 2000, 1:113-118.
5. Stalker J., Gibbins B., Meidl P., Smith J., Spooner W., Hotz H., Cox A. The Ensembl Web site: mechanics of a genome browser. Genome Res. 2004, 14:951-955.
6. Bals R., Wang X., Meegalla R., Wattler S., Weiner D., Nehls M., Wilson J. Mouse beta-defensin 3 is an inducible antimicrobial peptide expressed in the epithelia of multiple organs. Infect. Immun. 1999, 67:3542-3547.
7. Lehrer R., Ganz T. Defensins of vertebrate animals. Curr. Opin. Immunol. 2002, 14:96-102.
8. Morrison G., Semple C., Kilanowski F., Hill R., Dorin J. Signal sequence conservation and mature peptide divergence within subgroups of the murine beta-defensin gene family. Mol. Biol. Evol. 2003, 20:460-470.
9. Maxwell A., Morrison G., Dorin J. Rapid sequence divergence in mammalian beta-defensins by adaptive evolution. Mol. Immunol. 2003, 40:413-421.
10. Wang G., Li X., Wang Z. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009, 37:D933-D937.
11. Jia H., Wowk S., Schutte B., Lee S., Vivado A., Tack B., Bevins C., McCray P.J. A novel murine beta -defensin expressed in tongue, esophagus, and trachea. J. Biol. Chem. 2000, 275:33314-33320.
12. Morrison G., Rolfe M., Kilanowski F., Cross S., Dorin J. Identification and characterization of a novel murine beta-defensin-related gene. Mamm. Genome 2002, 13:445-451.
13. Diamond G., Jones D., Bevins C. Airway epithelial cells are the site of expression of a mammalian antimicrobial peptide gene. Proc. Natl. Acad. Sci. USA 1993, 90:4596-4600.
14. Tsutsumi-Ishii Y., Nagaoka I. NF-kappa B-mediated transcriptional regulation of human beta-defensin-2 gene following lipopolysaccharide stimulation. J. Leukoc. Biol. 2002, 71:154-162.
15. Tossi A., Tarantino C., Romeo D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. Eur. J. Biochem. 1997, 250:549-558.
16. Saberwal G., Nagaraj R. Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities. Biochim. Biophys. Acta 1994, 1197:109-131.
17. Shin S., Kang J., Jang S., Kim Y., Kim K., Hahm K. Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells. Biochim. Biophys. Acta 2000, 1463:209-218.
18. Dathe M., Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1999, 1462:71-87.
19. Shin S., Lee S., Yang S., Park E., Lee D., Lee M., Eom S., Song W., Kim Y., Hahm K., Kim J. Antibacterial, antitumor and hemolytic activities of alpha-helical antibiotic peptide, P18 and its analogs. J. Pept. Res. 2001, 58:504-514.