title: Cluster-forming property correlated with hemolytic activity by staphylococcal γ-hemolysin transmembrane pores.
abstract: Staphylococcal γ-hemolysin (Hlg) is a pore-forming toxin consisting of two separate components, LukF (34kDa) and Hlg2 (32kDa). Here we show that Hlg pores aggregate and form clusters on human erythrocyte membranes in association with increasing hemolytic activity. Quantitative analysis using transmission electron microscopy and image processing revealed that the formation of single pores and clusters is related to the release of potassium ions and of hemoglobin from erythrocytes, respectively. This is the first study to suggest a novel and unique property which can facilitate hemolysis by the cluster formation of Hlg pores.
authors: Institute of Fluid Science, Tohoku University, Sendai, Miyagi, Japan. tomita@ifs.biofluid.tohoku.ac.jp
authors: Noriko
authors: N
authors: Tomita
authors: Kazuyo
authors: K
authors: Abe
authors: Yoshiyuki
authors: Y
authors: Kamio
authors: Makoto
authors: M
authors: Ohta
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism* / Q000382:microbiology / Q000648:ultrastructure; D006454:Hemoglobins / Q000378:metabolism; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000378:metabolism*; D006461:Hemolysis; D006801:Humans; D046529:Microscopy, Electron, Transmission; D016062:Porosity; D011188:Potassium / Q000378:metabolism; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D013211:Staphylococcus aureus / Q000378:metabolism*; D013997:Time Factors
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; D006454:Hemoglobins; D006460:Hemolysin Proteins; C037956:gamma-hemolysin, Staphylococcus aureus; D011188:Potassium