Anionic C-terminal proregion of nematode antimicrobial peptide cecropin P4 precursor inhibits antimicrobial activity of the mature peptide

Bioscience, Biotechnology and Biochemistry

Volumn 72, Issue 12, 2008, Pages 3281-3284

  Ueno, Satoshi ^a,b   Kusaka, Kohtaro ^a   Tamada, Yasushi ^a   Minaba, Masaomi ^a   Zhang, Hong ^a   Wang, Pi Chao ^b   Kato, Yusuke ^a  

^a NATIONAL INSTITUTE OF AGROBIOLOGICAL SCIENCES   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

Antimicrobial peptide; Cecropin; Innate immunity; Nematode; Precursor

Indexed keywords

ANTIMICROBIAL PEPTIDE; CECROPIN; INNATE IMMUNITY; NEMATODE; PRECURSOR;

AMINES;

ANTIINFECTIVE AGENT; CECROPIN; PROTEIN PRECURSOR;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BACTERIUM; CELL MEMBRANE; CHEMISTRY; CYTOLOGY; DRUG ANTAGONISM; DRUG EFFECT; METABOLISM; MOLECULAR GENETICS; NEMATODE; SYNTHESIS;

AMINO ACID SEQUENCE; ANIMALS; ANTI-INFECTIVE AGENTS; BACTERIA; CECROPINS; CELL MEMBRANE; MOLECULAR SEQUENCE DATA; NEMATODA; PROTEIN PRECURSORS;

EID: 58149091271     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.80397     Document Type: Article

References (18)

1. Pillai, A., Ueno, S., Zhang, H., Lee, J. M., and Kato, Y., Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum. Biochem. J., 390, 207-214 (2005).
2. Lee, J. Y., Boman, A., Sun, C. X., Andersson, M., Jornvall, H., Mutt, V., and Boman, H. G., Antibacterial peptides from pig intestine: isolation of a mammalian cecropin. Proc. Natl. Acad. Sci. USA, 86, 9159-9162 (1989).
3. Sipos, D., Andersson, M., and Ehrenberg, A., The structure of the mammalian antibacterial peptide cecropin P1 in solution, determined by proton-NMR. Eur. J. Biochem., 209, 163-169 (1992).
4. Gazit, E., Boman, A., Boman, H. G., and Shai, Y., Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry, 34, 11479-11488 (1995).
5. Steiner, H., Hultmark, D., Engstrom, A., Bennich, H., and Boman, H. G., Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature, 292, 246-248 (1981).
6. Zhao, C., Liaw, L., Lee, I. H., and Lehrer, R. I., cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava. FEBS Lett., 412, 144-148 (1997).
7. Nakayama, K., Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J., 327, 625-635 (1997).
8. Poole, C. B., Jin, J., and McReynolds, L. A., Cloning and biochemical characterization of blisterase, a subtilisin-like convertase from the filarial parasite, Onchocerca volvulus. J. Biol. Chem., 278, 36183-36190 (2003).
9. Boman, H. C., Boman, I. A., Andreu, D., Li, Z. Q., Merrifield, R. B., Schlenstedt, G., and Zimmermann, R., Chemical synthesis and enzymic processing of precursor forms of cecropins A and B. J. Biol. Chem., 264, 5852-5860 (1989).
10. Michaelson, D., Rayner, J., Couto, M., and Ganz, T., Cationic defensins arise from charge-neutralized propeptides: mechanism for avoiding leukocyte autocytotoxicity? J. Leukoc. Biol., 51, 634-639 (1992).
11. Panyutich, A., Shi, J., Boutz, P. L., Zhao, C., and Ganz, T., Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins. Infect. Immun., 65, 978-985 (1997).
12. Moore, A. J., Devine, D. A., and Bibby, M. C., Preliminary experimental anticancer activity of cecropins. Pept. Res., 7, 265-269 (1994).
13. Liu, L., and Ganz, T., The pro-region of human neutrophil defensin contains a motif that is essential for normal subcellular sorting. Blood, 85, 1095-1103 (1995).
14. Zaiou, M., Nizet, V., and Gallo, R. L., Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence. J. Invest. Dermatol., 120, 810-816 (2003).
15. Xiong, Y. Q., Mukhopadhyay, K., Yeaman, M. R., Adler-Moore, J., and Bayer, A. S., Functional interrelationships between cell membrane and cell wall in antimicrobial peptide-mediated killing of Staphylococcus aureus. Antimicrob. Agents Chemother., 49, 3114-3121 (2005).
16. Brogden, K. A., Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol., 3, 238-250 (2005).
17. Kato, Y., Nematode antimicrobial peptides. Curr. Topics Pept. Prot. Res., 8, 1-10 (2007).
18. Zhang, H., Morikawa, K., Ohta, T., and Kato, Y., In vitro resistance to the CSαβ-type antimicrobial peptide ASABF-α is conferred by overexpression of sigma factor sigB in Staphylococcus aureus. J. Antimicrob. Chemother., 55, 686-691 (2005).