Spatial attributes of the four-helix bundle group of bacteriocins – The high-resolution structure of BacSp222 in solution

Michał Nowakowski, Lukasz Jaremko, Benedykt Wladyka, Grzegorz Dubin, Andrzej Ejchart, Paweł Mak

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

BacSp222 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.
Original languageEnglish (US)
Pages (from-to)2715-2724
Number of pages10
JournalInternational Journal of Biological Macromolecules
Volume107
DOIs
StatePublished - Nov 1 2017

Fingerprint

Dive into the research topics of 'Spatial attributes of the four-helix bundle group of bacteriocins – The high-resolution structure of BacSp222 in solution'. Together they form a unique fingerprint.

Cite this