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  • Title: Structural analysis of human specific cytolysin intermedilysin aiming application to cancer immunotherapy.
    Author: Ohkura K, Nagamune H, Kourai H.
    Journal: Anticancer Res; 2004; 24(5C):3343-53. PubMed ID: 15515430.
    Abstract:
    BACKGROUND: Intermedilysin (ILY) is a human specific cytolysin secreted by Streptococcus intermedius. In the present study, we performed molecular modeling of ILY and cholesterol-dependent cytolysins (CDCs) (pneumolysin, PLY; listeriolysin O, LLO; streptolysin O, SLO; alveolysin, ALV; suilysin, SLY; pyolysin, PLO) to compare the membrane binding domains including the undecapeptide (11mer) region which is thought to be necessary for the cytolytic activity of CDCs. MATERIALS AND METHODS: The molecular models of cytolysins were constructed using InsightII with Homology module with X-ray data of perfringolysin O (PFO). RESULTS: The ILY molecule was long and rod shaped, and comprised four domains. ILY was shown to possess stereocomplementary surfaces within the molecule and the potential to stack with 8 degrees of curvature leading to a ring cluster of 45 molecules or so in the human erythrocyte cell membranes. CONCLUSION: From the molecular orbital calculations and isostatic potential analysis, we considered that the ILY 11mer region has different features from those of traditional CDCs, and the ILY domain 4 should be very useful to apply the human cell-specific targeting module.
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