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TitleStepwise assembly of α-hemolysin from intermediates to the mature pore in native erythrocytes.
Journal, issue, pagesJ Cell Biol, Vol. 225, Issue 3, Year 2026
Publish dateMar 2, 2026
AuthorsArnab Chatterjee / Anupam Roy / Partho Pratim Das / Debajyoti Chakraborty / Bartika Ghoshal / Siddharth Jhunjhunwala / Somnath Dutta /
PubMed AbstractAlpha-hemolysin (α-HL) is a small pore-forming toxin secreted by pathogenic Staphylococcus aureus, inducing cell death process by forming pores in membrane. So far, detergents or artificial lipid ...Alpha-hemolysin (α-HL) is a small pore-forming toxin secreted by pathogenic Staphylococcus aureus, inducing cell death process by forming pores in membrane. So far, detergents or artificial lipid environments have been utilized to characterize the toxin structure. The toxin-induced changes in the membrane, membrane remodeling after toxin treatment, and the role of the toxin during pore formation process remain ambiguous. Thus, understanding pore formation in the cellular environment, including the roles of the plasma membrane and lipid composition, is crucial for drug development. In this study, we captured step-by-step oligomerization of α-HL and membrane rupture of erythrocyte cells using confocal microscopy, cryo-EM imaging, and single-particle analysis. We resolved 3.1-3.8 Å resolution structures of pore, prepore, and immature pore conformations in cellular environment. Furthermore, mass spectrometry analysis demonstrated key erythrocyte lipid components interacting with α-HL. Our findings indicate that shorter or unsaturated lipid chains facilitate pore formation and the role of phosphatidylcholine with varying physical properties in modulating the toxin's activity.
External linksJ Cell Biol / PubMed:41524690 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.8 Å
Structure data

63620

9m4a

EMDB-63620, PDB-9m4a:
Cryo-EM structure of pre-pore state IV of heptameric alpha-hemolysin in the presence of RBC
Method: EM (single particle) / Resolution: 3.46 Å

63626

9m4p

9ufa

EMDB-63626, PDB-9m4p:
Cryo-EM structure of alpha-hemolysin heptameric pore state in the presence of RBC
PDB-9ufa: phosphatidylcholine head group bound alpha-hemolysin heptameric pore structure in the presence of RBC
Method: EM (single particle) / Resolution: 3.1 Å

63781

9mbx

EMDB-63781, PDB-9mbx:
Cryo-EM structure of alpha-hemolysin heptameric pre-pore state III in the presence of RBC
Method: EM (single particle) / Resolution: 3.8 Å

65040

9vfw

EMDB-65040, PDB-9vfw:
Cryo-EM structure of pre-pore state II of heptameric alpha-hemolysin in the presence of RBCs
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-PC:
PHOSPHOCHOLINE

Source
  • staphylococcus aureus (bacteria)
KeywordsTOXIN / small PFT / RBC / pre-pore / PC / PFT

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