373
Views
14
CrossRef citations to date
0
Altmetric
Original Articles

Complete Covalent Structure of Nisin Q, New Natural Nisin Variant, Containing Post-Translationally Modified Amino Acids

, , , , , & show all
Pages 1750-1755 | Received 25 Jan 2008, Accepted 04 Apr 2008, Published online: 22 May 2014

  • 1) Cotter, P. D., Hill, C., and Ross, R. P., Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol., 3, 777–788 (2005).
  • 2) Xie, L., and van der Donk, W. A., Post-translational modifications during lantibiotic biosynthesis. Curr. Opin. Chem. Biol., 8, 498–507 (2004).
  • 3) Entian, K. D., and de Vos, W. M., Genetics of subtilin and nisin biosyntheses: biosynthesis of lantibiotics. Antonie van Leeuwenhoek, 69, 109–117 (1996).
  • 4) Hsu, S. T., Breukink, E., Tischenko, E., Lutters, M. A., de Kruijff, B., Kaptein, R., Bonvin, A. M., and van Nuland, N. A., The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics. Nat. Struct. Mol. Biol., 11, 963–967 (2004).
  • 5) van de Ven, F. J., van den Hooven, H. W., Konings, R. N., and Hilbers, C. W., NMR studies of lantibiotics. The structure of nisin in aqueous solution. Eur. J. Biochem., 202, 1181–1188 (1991).
  • 6) Freund, S., Jung, G., Gutbrod, O., Folkers, G., Gibbons, W. A., Allgaier, H., and Werner, R., The solution structure of the lantibiotic gallidermin. Biopolymers, 31, 803–811 (1991).
  • 7) Chan, W. C., Bycroft, B. W., Leyland, M. L., Lian, L. Y., Yang, J. C., and Roberts, G. C., Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR. FEBS Lett., 300, 56–62 (1992).
  • 8) van de Kamp, M., Horstink, L. M., van den Hooven, H. W., Konings, R. N., Hilbers, C. W., Frey, A., Sahl, H.-G., Metzger, J. W., and van de Ven, F. J., Sequence analysis by NMR spectroscopy of the peptide lantibiotic epilancin K7 from Staphylococcus epidermidis K7. Eur. J. Biochem., 227, 757–771 (1995).
  • 9) van den Hooven, H. W., Lagerwerf, F. M., Heerma, W., Haverkamp, J., Piard, J. C., Hilbers, C. W., Siezen, R. J., Kuipers, O. P., and Rollema, H. S., The structure of the lantibiotic lacticin 481 produced by Lactococcus lactis: location of the thioether bridges. FEBS Lett., 391, 317–322 (1996).
  • 10) Turner, D. L., Brennan, L., Meyer, H. E., Lohaus, C., Siethoff, C., Costa, H. S., Gonzalez, B., Santos, H., and Suarez, J. E., Solution structure of plantaricin C, a novel lantibiotic. Eur. J. Biochem., 264, 833–839 (1999).
  • 11) Smith, L., Novak, J., Rocca, J., McClung, S., Hillman, J. D., and Edison, A. S., Covalent structure of mutacin 1140 and a novel method for the rapid identification of lantibiotics. Eur. J. Biochem., 267, 6810–6816 (2000).
  • 12) Martin, N. I., Sprules, T., Carpenter, M. R., Cotter, P. D., Hill, C., Ross, R. P., and Vederas, J. C., Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity. Biochemistry, 43, 3049–3056 (2000).
  • 13) Zendo, T., Fukao, M., Ueda, K., Higuchi, T., Nakayama, J., and Sonomoto, K., Identification of the lantibiotic nisin Q, a new natural nisin variant produced by Lactococcus lactis 61-14 isolated from a river in Japan. Biosci. Biotechnol. Biochem., 67, 1616–1619 (2003).
  • 14) Gross, E., and Morell, J. L., The structure of nisin. J. Am. Chem. Soc., 93, 4634–4635 (1971).
  • 15) Mulders, J. W., Boerrigter, I. J., Rollema, H. S., Siezen, R. J., and de Vos, W. M., Identification and characterization of the lantibiotic nisin Z, a natural nisin variant. Eur. J. Biochem., 201, 581–584 (1991).
  • 16) Fujita, K., Ichimasa, S., Zendo, T., Koga, S., Yoneyama, F., Nakayama, J., and Sonomoto, K., Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of gram-positive bacteria. Appl. Environ. Microbiol., 73, 2871–2877 (2007).
  • 17) van De Ven, F. J., and Jung, G., Structures of lantibiotics studied by NMR. Antonie van Leeuwenhoek, 69, 99–107 (1996).
  • 18) Zweier, J. L., Duke, S. S., Kuppusamy, P., Sylvester, J. T., and Gabrielson, E. W., Electron paramagnetic resonance evidence that cellular oxygen toxicity is caused by the generation of superoxide and hydroxyl free radicals. FEBS Lett., 252, 12–16 (1989).
  • 19) Kuipers, O. P., Rollema, H. S., Yap, W. M., Boot, H. J., Siezen, R. J., and de Vos, W. M., Engineering dehydrated amino acid residues in the antimicrobial peptide nisin. J. Biol. Chem., 267, 24340–24346 (1992).
  • 20) Bonelli, R. R., Schneider, T., Sahl, H.-G., and Wiedemann, I., Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies. Antimicrob. Agents Chemother., 50, 1449–1457 (2006).
  • 21) Chan, W. C., Leyland, M., Clark, J., Dodd, H. M., Lian, L. Y., Gasson, M. J., Bycroft, B. W., and Roberts, G. C., Structure-activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin. FEBS Lett., 390, 129–132 (1996).
  • 22) Ottenwalder, B., Kupke, T., Brecht, S., Gnau, V., Metzger, J., Jung, G., and Götz, F., Isolation and characterization of genetically engineered gallidermin and epidermin analogs. Appl. Environ. Microbiol., 61, 3894–3903 (1995).
  • 23) van Kraaij, C., Breukink, E., Rollema, H. S., Bongers, R. S., Kosters, H. A., de Kruijff, B., and Kuipers, O. P., Engineering a disulfide bond and free thiols in the lantibiotic nisin Z. Eur. J. Biochem., 267, 901–909 (2000).
  • 24) Wirawan, R. E., Klesse, N. A., Jack, R. W., and Tagg, T. R., Molecular and genetic characterization of a novel nisin variant produced by Streptococcus uberis. Appl. Environ. Microbiol., 72, 1148–1156 (2006).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.