Dynamic structure of intermedilysin : Analysis of membrane binding region
| Project/Area Number | 15590098 |
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Drug development chemistry
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| Research Institution | Nagoya University |
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Principal Investigator |
OHKURA Kazuto Nagoya University, Grad.Sch.Bioagr.Sci., Assistant Prof., 大学院・生命農学研究科, 助手 (00242850)
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| Co-Investigator(Kenkyū-buntansha) |
HORI Hitoshi Univ.Tokushima, Dep.Biol.Sci.Tech., Fac.Eng., Prof., 工学部, 教授 (90119008)
TSUGE Hideaki Tokushima Bunri Univ., Inst.Health Sci., Prof., 健康科学研究所, 教授 (40299342)
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| Project Period (FY) |
2003 – 2005
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| Project Status |
Completed(Fiscal Year 2005)
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| Budget Amount *help |
¥3,600,000 (Direct Cost : ¥3,600,000)
Fiscal Year 2005 : ¥700,000 (Direct Cost : ¥700,000)
Fiscal Year 2004 : ¥1,000,000 (Direct Cost : ¥1,000,000)
Fiscal Year 2003 : ¥1,900,000 (Direct Cost : ¥1,900,000)
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| Keywords | infection / cytolysin |
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| Research Abstract |
Background : Intermedilysin (ILY) is a human-specific cytolysin secreted from Streptococcus intermedius. In this study, we analyzed the dynamic structure of ILY, Streptolysin O (SLO) and their 12mer substituted mutants during 500ps. Several parameters, such as dipole moment and electrostatic potential, were determined to discuss the molecular mechanism of membrane binding.
Material and Methods : Molecular models of ILY, SLO and their mutants were constructed using InsightII-Discover with the Homology module. Their molecular dynamics were simulated with the Discover3 module, and z-matrix data of the membrane-binding 12mer region were extracted to calculate the MO parameters (i.e. dipole moment, solvation free energy (dGW)).
Results : Cytolysins vibrated like a bow, and the dipole moment direction of ILY 12mer region was different from that of SLO. Certain ILY mutants indicated the SLO-like dipole properties, which had an SLO-type 11mer cysteine motif amino acid sequence. The ILY 11mer region was more hydrophobic than that of SLO, and seemed to easy interact with the cell membrane without cholesterol. The electrostatic potential field distribution of ILY differed from that of SLO, especially in the 11mer region.
Conclusion : In the 11mer region, the dipole moment directions of these cytolysins were constant during molecular movement, and ready to interact with membrane components (i.e. cholesterol, phospholipid) in each style.
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Report
(4results)
Research Products
(21results)
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[Journal Article] The Human-specific Action of Intermedilysin, a Homologue of Streptolysin O, is Dictated by Domain 4 of the Protein2004
Author(s)
Hideaki Nagamune, Kazuto Ohkura, Akiko Sukeno, Graeme Cowan, Timothy J.Mitchell, Wataru Ito, Ooki Ohnishi, Kanako Hattori, Miki Yamato, Katsuhiko Hirota, Yoichiro Miyake, Takuya Maeda, Hiroki Kourai
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Journal Title
Microbiology and Immunology Vol.48-No.9
Pages : 677-692
Description
「研究成果報告書概要(欧文)」より
Related Report
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