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TitleChimeric mutants of staphylococcal hemolysin, which act as both one-component and two-component hemolysin, created by grafting the stem domain.
Journal, issue, pagesFEBS J, Vol. 289, Issue 12, Page 3505-3520, Year 2022
Publish dateFeb 16, 2022
AuthorsNouran Ghanem / Natsuki Kanagami / Takashi Matsui / Kein Takeda / Jun Kaneko / Yasuyuki Shiraishi / Christian A Choe / Tomomi Uchikubo-Kamo / Mikako Shirouzu / Tsubasa Hashimoto / Tomohisa Ogawa / Tomoaki Matsuura / Po-Ssu Huang / Takeshi Yokoyama / Yoshikazu Tanaka /
PubMed AbstractStaphylococcus aureus expresses several hemolytic pore-forming toxins (PFTs), which are all commonly composed of three domains: cap, rim and stem. PFTs are expressed as soluble monomers and assemble ...Staphylococcus aureus expresses several hemolytic pore-forming toxins (PFTs), which are all commonly composed of three domains: cap, rim and stem. PFTs are expressed as soluble monomers and assemble to form a transmembrane β-barrel pore in the erythrocyte cell membrane. The stem domain undergoes dramatic conformational changes to form a pore. Staphylococcal PFTs are classified into two groups: one-component α-hemolysin (α-HL) and two-component γ-hemolysin (γ-HL). The α-HL forms a homo-heptamer, whereas γ-HL is an octamer composed of F-component (LukF) and S-component (Hlg2). Because PFTs are used as materials for nanopore-based sensors, knowledge of the functional properties of PFTs is used to develop new, engineered PFTs. However, it remains challenging to design PFTs with a β-barrel pore because their formation as transmembrane protein assemblies requires large conformational changes. In the present study, aiming to investigate the design principles of the β-barrel formed as a consequence of the conformational change, chimeric mutants composed of the cap/rim domains of α-HL and the stem of LukF or Hlg2 were prepared. Biochemical characterization and electron microscopy showed that one of them assembles as a heptameric one-component PFT, whereas another participates as both a heptameric one- and heptameric/octameric two-component PFT. All chimeric mutants intrinsically assemble into SDS-resistant oligomers. Based on these observations, the role of the stem domain of these PFTs is discussed. These findings provide clues for the engineering of staphylococcal PFT β-barrels for use in further promising applications.
External linksFEBS J / PubMed:35030303
MethodsEM (single particle)
Resolution11.55 - 16.0 Å
Structure data

EMDB-32064: The oligomerized complex of hemolysin AF3 mutant protomers.
Method: EM (single particle) / Resolution: 16.0 Å

EMDB-32065: The oligomerized complex of AG2 hemolysin mutant protomers
Method: EM (single particle) / Resolution: 11.55 Å

Source
  • Staphylococcus aureus (bacteria)

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