Spatial attributes of the four-helix bundle group of bacteriocins – The high-resolution structure of BacSp222 in solution
MetadataShow full item record
AbstractBacSp222 is a multifunctional bacteriocin produced by Staphylococcus pseudintermedius strain 222, an opportunistic pathogen of domestic animals. At micromolar concentrations, BacSp222 kills Gram-positive bacteria and is cytotoxic toward mammalian cells, while at nanomolar doses, it acts as an immunomodulatory factor, enhancing nitric oxide release in macrophage-like cell lines. The bacteriocin is a cationic, N-terminally formylated, 50-amino-acid-long linear peptide that is rich in tryptophan residues.In this study, the solution structure of BacSp222 was determined and compared to the currently known structures of similar bacteriocins. BacSp222 was isolated from a liquid culture medium in a uniformly 13C- and 15N-labeled form, and NMR data were collected. The structure was calculated based on NMR-derived constraints and consists of a rigid and tightly packed globular bundle of four alpha-helices separated by three short turns.Although the amino acid sequence of BacSp222 has no significant similarity to any known peptide or protein, a 3D structure similarity search indicates a close relation to other four-helix bundle-motif bacteriocins, such as aureocin A53, lacticin Q and enterocins 7A/7B. Assuming similar functions, biology, structure and physicochemical properties, we propose to distinguish the four-helix bundle bacteriocins as a new Type A in subclass IId of bacteriocins, containing linear, non-pediocin-like peptides.
CitationNowakowski M, Jaremko Ł, Wladyka B, Dubin G, Ejchart A, et al. (2017) Spatial attributes of the four-helix bundle group of bacteriocins – The high-resolution structure of BacSp222 in solution. International Journal of Biological Macromolecules. Available: http://dx.doi.org/10.1016/j.ijbiomac.2017.10.158.
SponsorsThe authors greatly appreciate the valuable advice concerning interpretation of the results provided by Dr. Anna Bujacz. The study was supported in part by a grant (to PM) financed by the National Science Centre (Kraków, Poland) according to decision No. DEC-2013/11/B/NZ6/00409. MN would like to thank the National Science Centre for support with SONATA BIS 2 (2012/07/E/ST4/01386). The Faculty of Biochemistry, Biophysics and Biotechnology of Jagiellonian University in Krakow is a partner of the Leading National Research Center (KNOW) supported by the Ministry of Science and Higher Education (Warszawa, Poland).
- A peptide factor secreted by Staphylococcus pseudintermedius exhibits properties of both bacteriocins and virulence factors.
- Authors: Wladyka B, Piejko M, Bzowska M, Pieta P, Krzysik M, Mazurek Ł, Guevara-Lora I, Bukowski M, Sabat AJ, Friedrich AW, Bonar E, Międzobrodzki J, Dubin A, Mak P
- Issue date: 2015 Sep 28
- Nuclear Magnetic Resonance Solution Structures of Lacticin Q and Aureocin A53 Reveal a Structural Motif Conserved among Leaderless Bacteriocins with Broad-Spectrum Activity.
- Authors: Acedo JZ, van Belkum MJ, Lohans CT, Towle KM, Miskolzie M, Vederas JC
- Issue date: 2016 Feb 2
- Structural analysis and characterization of lacticin Q, a novel bacteriocin belonging to a new family of unmodified bacteriocins of gram-positive bacteria.
- Authors: Fujita K, Ichimasa S, Zendo T, Koga S, Yoneyama F, Nakayama J, Sonomoto K
- Issue date: 2007 May
- Solution structures of the linear leaderless bacteriocins enterocin 7A and 7B resemble carnocyclin A, a circular antimicrobial peptide.
- Authors: Lohans CT, Towle KM, Miskolzie M, McKay RT, van Belkum MJ, McMullen LM, Vederas JC
- Issue date: 2013 Jun 11
- Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus.
- Authors: Netz DJ, Pohl R, Beck-Sickinger AG, Selmer T, Pierik AJ, Bastos Mdo C, Sahl HG
- Issue date: 2002 Jun 7