Macin family of antimicrobial proteins combines antimicrobial and nerve repair activities

Journal of Biological Chemistry

Volumn 287, Issue 17, 2012, Pages 14246-14258

  Jung, Sascha ^a   Sönnichsen, Frank D ^a   Hung, Chien Wen ^a   Tholey, Andreas ^a   Boidin Wichlacz, Céline ^b,d   Haeusgen, Wiebke ^c   Gelhaus, Christoph ^a   Desel, Christine ^a   Podschun, Rainer ^c   Waetzig, Vicki ^c   Tasiemski, Aurélie ^b,d   Leippe, Matthias ^a   Grötzinger, Joachim ^a  

^a UNIVERSITY OF KIEL   (Germany)

^b UNIV LILLE   (France)

^c UNIVERSITY HOSPITAL SCHLESWIG HOLSTEIN   (Germany)

^d Univ Lille   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BACTERIOLOGY; BIOACTIVITY; CELL MEMBRANES; CELL PROLIFERATION; PROTEINS;

ANTIMICROBIAL PROTEINS; BACILLUS MEGATERIUM; CYTOPLASMIC MEMBRANE; FUNCTIONAL CHARACTERISTICS; GRAM-NEGATIVE BACTERIA; MECHANISTIC MODELING; NEUROBLASTOMA CELLS; SEQUENCE SIMILARITY;

REPAIR;

CENTRAL NERVOUS SYSTEM AGENTS; HYDRAMACIN 1; MACIN; NEUROMACIN; POLYPEPTIDE ANTIBIOTIC AGENT; THEROMACIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIMICROBIAL THERAPY; ARTICLE; BACILLUS MEGATERIUM; BACTERIAL CELL; BIOLOGICAL MODEL; CELL AGGREGATION; CELL MEMBRANE PERMEABILITY; CELL PROLIFERATION; CHANNEL GATING; CHIMERA; CONTROLLED STUDY; DRUG PURIFICATION; DRUG SCREENING; DRUG STRUCTURE; ESCHERICHIA COLI; EX VIVO STUDY; LEECH; NERVE REGENERATION; NEUROBLASTOMA CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; STAPHYLOCOCCUS AUREUS; STRUCTURE ACTIVITY RELATION; SURFACE PROPERTY;

EID: 84859997941     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.336495     Document Type: Article

References (37)

1. Jenssen, H., Hamill, P., and Hancock, R. E. (2006) Peptide antimicrobial agents. Clin. Microbiol. Rev. 19, 491-511 (Pubitemid 44137212)
2. Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389-395
3. Jung, S., Mysliwy, J., Spudy, B., Lorenzen, I., Reiss, K., Gelhaus, C., Podschun, R., Leippe, M., and Grötzinger, J. (2011) Human β-defensin 2 and β-defensin 3 chimeric peptides reveal the structural basis of the pathogen specificity of their parent molecules. Antimicrob. Agents Chemother. 55, 954-960
4. Schwab, U., Gilligan, P., Jaynes, J., and Henke, D. (1999) In vitro activities of designed antimicrobial peptides against multidrug-resistant cystic fibrosis pathogens. Antimicrob. Agents Chemother. 43, 1435-1440 (Pubitemid 29259339)
5. Otero-González, A. J., Magalhães, B. S., Garcia-Villarino, M., López-Abarrategui, C., Sousa, D. A., Dias, S. C., and Franco, O. L. (2010) Antimicrobial peptides from marine invertebrates as a new frontier for microbial infection control. FASEB J. 24, 1320-1334
6. Neonakis, I. K., Spandidos, D. A., and Petinaki, E. (2011) Confronting multidrug-resistant Acinetobacter baumannii: a review. Int. J. Antimicrob. Agents 37, 102-109
7. Wilmes, M., Cammue, B. P., Sahl, H. G., and Thevissen, K. (2011) Antibiotic activities of host defense peptides: more to it than lipid bilayer perturbation. Nat. Prod. Rep. 28, 1350-1358
8. Schikorski, D., Cuvillier-Hot, V., Leippe, M., Boidin-Wichlacz, C., Slomianny, C., Macagno, E., Salzet, M., and Tasiemski, A. (2008) Microbial challenge promotes the regenerative process of the injured central nervous system of the medicinal leech by inducing the synthesis of antimicrobial peptides in neurons and microglia. J. Immunol. 181, 1083-1095
9. Wang, G., Li, X., and Wang, Z. (2009) APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 37, D933-D937
10. Jung, S., Dingley, A. J., Augustin, R., Anton-Erxleben, F., Stanisak, M., Gelhaus, C., Gutsmann, T., Hammer, M. U., Podschun, R., Bonvin, A. M., Leippe, M., Bosch, T. C., and Grötzinger, J. (2009) Hydramacin-1, structure and antibacterial activity of a protein from the basal metazoan Hydra. J. Biol. Chem. 284, 1896-1905
11. Tasiemski, A., Vandenbulcke, F., Mitta, G., Lemoine, J., Lefebvre, C., Sautire, P. E., and Salzet, M. (2004) Molecular characterization of two novel antibacterial peptides inducible upon bacterial challenge in an annelid, the leech Theromyzon tessulatum. J. Biol. Chem. 279, 30973-30982 (Pubitemid 39037756)
12. Dingley, A. J., Lorenzen, I., and Grötzinger, J. (2008) NMR analysis of viral protein structures. Methods Mol. Biol. 451, 441-462
13. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
14. Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278, 313-352
15. Güntert, P. (2004) Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278, 353-378
16. Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223
17. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921
18. Vriend, G. (1990) WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56, 29
19. van Gunsteren, W. F., Billeter, S. R., Eising, A. A., Hünenberger, P. H., Krüger, P., Mark, A. E., Scott, W. R. P., and Tironi, I. G. (1996) Biomolecular Simulation: the GROMOS96 Manual and User Guide, vdf Hochschulverlag AG, Zürich
20. Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55, 29-32
21. Petrey, D., and Honig, B. (2003) GRASP2: visualization, surface properties, and electrostatics of macromolecular structures and sequences. Methods Enzymol. 374, 492-509 (Pubitemid 37531822)
22. Sahly, H., Schubert, S., Harder, J., Rautenberg, P., Ullmann, U., Schröder, J., and Podschun, R. (2003) Burkholderia is highly resistant to human β-defensin 3. Antimicrob. Agents Chemother. 47, 1739-1741 (Pubitemid 36548564)
23. Herbst, R., Ott, C., Jacobs, T., Marti, T., Marciano-Cabral, F., and Leippe, M. (2002) Pore-forming polypeptides of the pathogenic protozoon Naegleria fowleri. J. Biol. Chem. 277, 22353-22360 (Pubitemid 34967203)
24. Leippe, M., Ebel, S., Schoenberger, O. L., Horstmann, R. D., and Müller-Eberhard, H. J. (1991) Pore-forming peptide of pathogenic Entamoeba histolytica. Proc. Natl. Acad. Sci. U.S.A. 88, 7659-7663 (Pubitemid 21915213)
25. Pick, U. (1981) Liposomes with a large trapping capacity prepared by freezing and thawing of sonicated phospholipid mixtures. Arch. Biochem. Biophys. 212, 186-194
26. Tasiemski, A., and Salzet, M. (2010) Leech immunity: from brain to peripheral responses. Adv. Exp. Med. Biol. 708, 80-104
27. Boidin-Wichlacz, C., Vergote, D., Slomianny, C., Jouy, N., Salzet, M., and Tasiemski, A. (2012) Morphological and functional characterization of leech circulating blood cells: role in immunity and neural repair. Cell. Mol. Life Sci., in press
28. Duan, Y., Panoff, J., Burrell, B. D., Sahley, C. L., and Muller, K. J. (2005) Repair and regeneration of functional synaptic connections: cellular and molecular interactions in the leech. Cell. Mol. Neurobiol. 25, 441-450 (Pubitemid 40768444)
29. Schaller, H. C., Hermans-Borgmeyer, I., and Hoffmeister, S. A. (1996) Neuronal control of development in Hydra. Int. J. Dev. Biol. 40, 339 -344
30. Bosch, T. C. (2007) Why polyps regenerate and we don't: towards a cellular and molecular framework for Hydra regeneration. Dev. Biol. 303, 421-433
31. Zucca, M., Scutera, S., and Savoia, D. (2011) New antimicrobial frontiers. Mini Rev. Med. Chem. 11, 888-900
32. Nguyen, L. T., Haney, E. F., and Vogel, H. J. (2011) The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol. 29, 464-472
33. Yang, Y. S., Mitta, G., Chavanieu, A., Calas, B., Sanchez, J. F., Roch, P., and Aumelas, A. (2000) Solution structure and activity of the synthetic fourdisulfide bond Mediterranean mussel defensin (MGD-1). Biochemistry 39, 14436-14447
34. Lay, F. T., Schirra, H. J., Scanlon, M. J., Anderson, M. A., and Craik, D. J. (2003) The three-dimensional solution structure of NaD1, a new floral defensin from Nicotiana alata and its application to a homology model of the crop defense protein alfAFP. J. Mol. Biol. 325, 175-188 (Pubitemid 36153006)
35. Blanc, E., Romi-Lebrun, R., Bornet, O., Nakajima, T., and Darbon, H. (1998) Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels. Biochemistry 37, 12412-12418 (Pubitemid 28427525)
36. Lamberty, M., Caille, A., Landon, C., Tassin-Moindrot, S., Hetru, C., Bulet, P., and Vovelle, F. (2001) Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities. Biochemistry 40, 11995-12003 (Pubitemid 32946541)
37. Cook, W. J., Zell, A., Watt, D. D., and Ealick, S. E. (2002) Structure of variant 2 scorpion toxin from Centruroides sculpturatus Ewing. Protein Sci. 11, 479-486 (Pubitemid 34171253)