Plantaricin A, a peptide pheromone produced by Lactobacillus plantarum, permeabilizes the cell membrane of both normal and cancerous lymphocytes and neuronal cells

Peptides

Volumn 31, Issue 7, 2010, Pages 1237-1244

  Sand, Sverre L ^a   Oppegård, Camilla ^a   Ohara, Shinya ^b   Iijima, Toshio ^b   Naderi, Soheil ^a   Blomhoff, Heidi K ^a   Nissen Meyer, Jon ^a   Sand, Olav ^a  

^a UNIVERSITY OF OSLO   (Norway)

^b TOHOKU UNIVERSITY   (Japan)

Author keywords

Cell lysis; Lactobacillus plantarum; Lymphocytes; Membrane permeabilization; Neuronal cells; Plantaricin A (PlnA)

Indexed keywords

PLANTARICIN A; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTINEOPLASTIC ACTIVITY; ARTICLE; B CELL LEUKEMIA; B LYMPHOCYTE; BRAIN NERVE CELL; CANCER CELL CULTURE; CELL MEMBRANE CONDUCTANCE; CELL PERMEABILIZATION; CELL STRUCTURE; CELL VIABILITY; CONTROLLED STUDY; DRUG SENSITIVITY; DRUG SYNTHESIS; EMBRYO; GLIA CELL; HUMAN; HUMAN CELL; LACTOBACILLUS PLANTARUM; LEUKEMIA CELL LINE; MOUSE; NONHUMAN; PRIORITY JOURNAL; RAT; T CELL LEUKEMIA; T LYMPHOCYTE;

ANIMALS; ANTINEOPLASTIC AGENTS; BACTERIOCINS; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; FLOW CYTOMETRY; HUMANS; JURKAT CELLS; LACTOBACILLUS PLANTARUM; LEUKEMIA; LYMPHOCYTES; MICE; NEURONS; PHEROMONES; RATS;

BACTERIA (MICROORGANISMS); EUKARYOTA; LACTOBACILLUS PLANTARUM; METAZOA; MURINAE; RATTUS;

EID: 77952545034     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2010.04.010     Document Type: Article

References (31)

1. Anderssen E.L., Diep D.B., Nes I.F., Eijsink V.G., and Nissen-Meyer J. Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide bacteriocins, plantaricins EF and JK, and the induction factor plantaricin A. Appl Environ Microbiol 64 (1998) 2269-2272
2. Balasubramanian K., and Schroit A.J. Aminophospholipid asymmetry: a matter of life and death. Annu Rev Physiol 65 (2003) 701-734
3. Boman H.G. Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 13 (1995) 61-92
4. Chen H.M., Leung K.W., Thakur N.N., Tan A., and Jack R.W. Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3. Eur J Biochem 270 (2003) 911-920
5. Chen H.M., Wang W., Smith D., and Chan S.C. Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells. Biochim Biophys Acta 1336 (1997) 171-179
6. Cruciani R.A., Barker J.L., Zasloff M., Chen H.C., and Colamonici O. Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation. PNAS 88 (1991) 3792-3796
7. Diep D.B., Havarstein L.S., and Nes I.F. A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11. Mol Microbiol 18 (1995) 631-639
8. Diep D.B., Havarstein L.S., Nissen-Meyer J., and Nes I.F. The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcription unit as an agr-like regulatory system. Appl Environ Microbiol 60 (1994) 160-166
9. Fimland G., Johnsen L., Dalhus B., and Nissen-Meyer J. Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action. J Pept Sci 11 (2005) 688-696
10. Greene L.A., and Tischler A.S. Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. PNAS 73 (1976) 2424-2428
11. Hancock R.E., and Chapple D.S. Peptide antibiotics. Antimicrob Agents Chemother 43 (1999) 1317-1323
12. Hauge H.H., Mantzilas D., Moll G.N., Konings W.N., Driessen A.J., Eijsink V.G., et al. Plantaricin A is an amphiphilic alpha-helical bacteriocin-like pheromone which exerts antimicrobial and pheromone activities through different mechanisms. Biochemistry 37 (1998) 16026-16032
13. Jacob L., and Zasloff M. Potential therapeutic applications of magainins and other antimicrobial agents of animal origin. Ciba Found Symp 186 (1994) 197-223
14. Klebe R.J., and Ruddle R.H. Neuroblastoma-cell culture analysis of a differentiating stem cell system. J Cell Biol 43 (1969) A69
15. Kristiansen P.E., Fimland G., Mantzilas D., and Nissen-Meyer J. Structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A. J Biol Chem 280 (2005) 22945-22950
16. Lehrer R.I., Lichtenstein A.K., and Ganz T. Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu Rev Immunol 11 (1993) 105-128
17. Leuschner C., and Hansel W. Membrane disrupting lytic peptides for cancer treatments. Curr Pharm Des 10 (2004) 2299-2310
18. Lichtenstein A. Mechanism of mammalian cell lysis mediated by peptide defensins. Evidence for an initial alteration of the plasma membrane. J Clin Invest 88 (1991) 93-100
19. Matsuzaki K. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim Biophys Acta 1376 (1998) 391-400
20. Murphy T.H., Schnaar R.L., and Coyle J.T. Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake. FASEB J 4 (1990) 1624-1633
21. Nissen-Meyer J., and Nes I.F. Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action. Arch Microbiol 167 (1997) 67-77
22. Oren Z., and Shai Y. Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers 47 (1998) 451-463
23. Rasmussen A.M., Smeland E.B., Erikstein B.K., Caignault L., and Funderud S. A new method for detachment of dynabeads from positively selected lymphocytes-B. J Immunol Methods 146 (1992) 195-202
24. Sand S.L., Haug T.M., Nissen-Meyer J., and Sand O. The bacterial peptide pheromone plantaricin A permeabilizes cancerous, but not normal, rat pituitary cells and differentiates between the outer and inner membrane leaflet. J Membr Biol 216 (2007) 61-71
25. Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 66 (2002) 236-248
26. - regulation. J Neurophysiol 81 (1999) 1939-1948
27. Tossi A., Sandri L., and Giangaspero A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
28. Ye J.S., Zheng X.J., Leung K.W., Chen H.M., and Sheu F.S. Induction of transient ion channel-like pores in a cancer cell by antibiotic peptide. J Biochem 136 (2004) 255-259
29. Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. PNAS 84 (1987) 5449-5453
30. Zelezetsky I., Pacor S., Pag U., Papo N., Shai Y., Sahl H.G., et al. Controlled alteration of the shape and conformational stability of alpha-helical cell-lytic peptides: effect on mode of action and cell specificity. Biochem J 390 (2005) 177-188
31. Zhao H., Sood R., Jutila A., Bose S., Fimland G., Nissen-Meyer J., et al. Interaction of the antimicrobial peptide pheromone Plantaricin A with model membranes: implications for a novel mechanism of action. Biochim Biophys Acta 1758 (2006) 1461-1474