Plectasin, a fungal defensin, targets the bacterial cell wall precursor lipid II

Science

Volumn 328, Issue 5982, 2010, Pages 1168-1172

  Schneider, Tanja ^a   Kruse, Thomas ^b   Wimmer, Reinhard ^c   Wiedemann, Imke ^a   Sass, Vera ^a   Pag, Ulrike ^a   Jansen, Andrea ^a   Nielsen, Allan K ^d   Mygind, Per H ^d   Raventós, Dorotea S ^d   Neve, Seren ^d   Ravn, Birthe ^d   Bonvin, Alexandre M J J ^e   De Maria, Leonardo ^d   Andersen, Anders S ^b,d   Gammelgaard, Lora K ^d   Sahl, Hans Georg ^a   Kristensen, Hans Henrik ^d  

^a UNIVERSITY OF BONN   (Germany)

^b STATENS SERUM INSTITUT   (Denmark)

^c AALBORG UNIVERSITY   (Denmark)

^d NOVOZYMES A S   (Denmark)

^e UTRECHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; PLECTASIN;

ANTIMICROBIAL ACTIVITY; BACTERIUM; BIOASSAY; FUNGUS; IMMUNITY; LIPID; MEMBRANE; NUCLEAR MAGNETIC RESONANCE; PEPTIDE; PROTEIN; STOICHIOMETRY;

ARTICLE; BACTERIAL CELL WALL; BIOSYNTHESIS; COMPLEX FORMATION; IN VITRO STUDY; LIPOGENESIS; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRECURSOR; PRIORITY JOURNAL; STOICHIOMETRY;

ANTI-BACTERIAL AGENTS; ASCOMYCOTA; BACILLUS SUBTILIS; BINDING SITES; CELL MEMBRANE; CELL WALL; COMPUTER SIMULATION; DEFENSINS; FUNGAL PROTEINS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGONUCLEOTIDE ARRAY SEQUENCE ANALYSIS; PEPTIDES; PROTEIN CONFORMATION; STAPHYLOCOCCUS; URIDINE DIPHOSPHATE N-ACETYLMURAMIC ACID; VANCOMYCIN;

BACTERIA (MICROORGANISMS);

EID: 77952976637     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1185723     Document Type: Article

References (22)

1. P. H. Mygind et al., Nature 437, 975 (2005).
2. D. Andes, W. Craig, L. A. Nielsen, H. H. Kristensen, Antimicrob. Agents Chemother. 53, 3003 (2009).
3. Materials and methods are available as supporting material on Science Online.
4. M. Zasloff, Nature 415, 389 (2002).
5. R. E. Hancock, H. G. Sahl, Nat. Biotechnol. 24, 1551 (2006).
6. B. Hutter et al., Antimicrob. Agents Chemother. 48, 2838 (2004).
7. F. McAleese et al., J. Bacteriol. 188, 1120 (2006).
8. M. Cao, T. Wang, R. Ye, J. D. Helmann, Mol. Microbiol. 45, 1267 (2002).
9. T. Mascher, N. G. Margulis, T. Wang, R. W. Ye, J. D. Helmann, Mol. Microbiol. 50, 1591 (2003).
10. J. van Heijenoort, Microbiol. Mol. Biol. Rev. 71, 620 (2007).
11. T. Schneider et al., Mol. Microbiol. 53, 675 (2004).
12. P. E. Reynolds, Eur. J. Clin. Microbiol. Infect. Dis. 8, 943 (1989).
13. N. E. Allen, T. I. Nicas, FEMS Microbiol. Rev. 26, 511 (2003).
14. H. Brötz et al., Mol. Microbiol. 30, 317 (1998).
15. J. M. Willey, W. A. van der Donk, Annu. Rev. Microbiol. 61, 477 (2007).
16. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
17. G. Jones, P. Willett, R. C. Glen, A. R. Leach, R. Taylor, J. Mol. Biol. 267, 727 (1997).
18. C. Dominguez, R. Boelens, A. M. Bonvin, J. Am. Chem. Soc. 125, 1731 (2003).
19. S. T. Hsu et al., Nat. Struct. Mol. Biol. 11, 963 (2004).
20. H. E. Hasper et al., Science 313, 1636 (2006).
21. E. Breukink, B. de Kruijff, Nat Rev. Drug Discov. 5, 321 (2006).
22. 13C atoms of plectasin have been deposited in the BioMagResBank (accession number 16739).