(1) Rice, B.L. (2006) Antimicrobial resistance in gram-positive bacteria. Am. J. Infect. Control., 34(5, suppl, 1):S11-19.
(2) Foster, T.J. (2005) Immune evasion by staphylococci. Nat. Rev. Microbiol., 3(12):948-958.
(3) Menestrina, G. (2001) Mode of action of β-barrel pore-forming toxins of the staphylococcal α-hemolysin family. Toxicon., 39(11):1661-1672.
(4) Gouaux, E. (1998) alpha-Hemolysin from Staphylococcus aureus: an archetype of beta-barrel, channel-forming toxins. J. Struct. Biol., 121(2):110-122.
(5) Kamio, Y., Rahman, A., Nariya, H., Ozawa, T., Izaki, K. (1993) The two Staphylococcal bi-component toxins, leukocidin and gamma-hemolysin, share one component in common. FEBS. Lett., 321(1):15-18.
(6) Kaneko, J., Kamio, Y. (2004) Bacterial two-component and hetero-heptameric pore forming cytolytic toxins: Structures, pore- forming mechanism, and organization of the genes. Biosci. Biotechnol. Biochem., 68(5):981-1003.
(7) Prévost, G., Cribier, B., Couppié, P., Petiau, P., Supersac, G., Finck-Barbançon, V., Monteil, H., Piemont, Y. (1995) Panton-Valentine leucocidin and gamma-hemolysin from Staphylococcus aureus ATCC 49775 are encoded by distinct genetic loci and have different biological activities. Infect. Immun., 63(10):4121-4129.
(8) Morinaga, N., Kaihou, Y., Noda, M. (2003). Purification, cloning and characterization of variant LukE-LukD with strong leukocidal activity of staphylococcal bi-component leukotoxin family. Microbiol. Immunol., 47(1):81–90.
(9) Gravet, A., Colin, D.A., Keller, D., Giradot, R., Monteil, H., and Prévost, G. (1998) Characterization of a novel structural member, LukE-LukD, of the bi-component staphylococcal leucotoxins family. FEBS. Lett., 436(2):202-208.
(10) Kaneko, J., Muramoto, K., Kamio, Y. (1997) Gene of LukF-PV-like component of Panton-Valentine leukocidin in Staphylococcus aureus P83 is linked with lukM. Biosci. Biotechnol. Biochem., 61(3):541-544.
(11) Dumont, A.L., Nygaard, T.K., Watkins, R.L., Smith, A., Kozhaya, L., Kreiswirth, B.N., Shopsin, B., Unutmaz, D., Voyich, J.M., Torres, V.J. (2011) Characterization of a new cytotoxin that contributes to Staphylococcus aureus pathogenesis. Mol. Microbiol., 79(3):814-825.
(12) Badarau, A., Rouha, H., Malafa, S., Logan, D.T., Håkansson, M., Stulik, L., Dolezilkova, I., Teubenbacher, A., Gross, K., Maierhofer, B., Weber, S., Jägerhofer, M., Hoffman, D., Nagy, E. (2015) Structure-function analysis of heterodimer formation, oligomerization, and receptor binding of the Staphylococcus aureus bi-component toxin LukGH. J. Biol. Chem., 290(1):142-156.
(13) Koop, G., Vrieling, M., Storisteanu, D.M., Lok, L.S., Monie, T., van Wigcheren, G., Raisen, C., Ba, X., Gleadall, N., Hadjirin, N., Timmerman, A.J., Wagenaar, J.A., Klunder, H.M., Fitzgerald, J.R., Zadoks, R., Paterson, G.K., Torres, C., Waller, A.S., Loeffler, A., Loncaric, I., Hoet, A.E., Bergström, K., De, Martino, L., Pomba, C., de Lencastre, H., Ben Slama, K., Gharsa, H., Richardson, E.J., Chilvers, E.R., de Haas, C., van Kessel, K., van Strijp, J.A., Harrison, E.M., Holmes, M.A. (2017) Identification of LukPQ, a novel, equid-adapted leukocidin of Staphylococcus aureus. Sci. Rep., 7:40660.
(14) Bohack C.A. (2006) Staphylococcus aureus exotoxins. In gram-positive pathogens (Vincent, A., Richard, P., Eds.) ASM Press., pp.464-477.
(15) Spaan, A.N., Van Strijp, J.A.G., Torres, V.J. (2017) Leukocidins: staphylococcal bi‑component pore-forming toxins find their receptors. Nat. Rev. Microbiol., 15(7):435-447.
(16) Yamashita, K., Kawai, Y., Tanaka, Y., Hirano, N., Kaneko, J., Tomita, N., Ohta, M., Kamio, Y., Yao, M., Tanaka, I. (2011) Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-berrel pore formation mechanism by two components. Proc. Natl. Acad. Sci. USA., 108(42):17314-17319.
(17) Song, L., Hobaugh, R, M., Shustak, C., Cheley, S., Bayley, H., Gouaux, J.E. (1996) Structure of staphylococcal α-Hemolysin, a heptameric transmembrane pore. Science., 274(5294):1859-1866.
(18) Olson, R., Nariya, H., Yokota, K., Kamio, Y., Gouaux, E. (1999) Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat. Struct. Biol., 6(2):134-140.
(19) Roblin, P., Guillet, V., Joubert, O., Keller, D., Erard, M., Maveyraud, L., Prévost, G., Mourey, L. (2008) A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of -barrel pore-forming toxins. Proteins., 71(1):485–496.
(20) Monma, N., Nguyen, V.T., Kaneko, J., Higuchi, H., Kamio, Y. (2004) Essential residues, W177 and R198, of LukF for phosphatidylcholine-binding and pore- formation by staphylococcal gamma-hemolysin on human erythrocyte membranes. J. Biochem., 136(4):427-431.
(21) Yamashita, D., Sugawara, T., Takeshita, M., Kaneko, J., Kaneko, Y., Tanaka, I., Tanaka, Y., Yao, M. (2014) Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins. Nat. commun., 5:4897.
(22) Sugawara, T., Yamashita, D., Kato, K., Peng, Z., Ueda, J., Kaneko, J., Kamio, Y., Tanaka, Y., Yao, M. (2015) Structural basis for pore-forming mechanism of staphylococcal α-hemolysin. Toxicon., 108:226-231.
(23) Ozawa, T., Kaneko, J., Kamio, Y. (1995) Essential binding of LukF of Staphylococcal gamma-hemolysin followed by the biding of H gamma Ⅱ for the hemolysis of human erythrocytes. Biosci. Biotechnol. Biochem., 59(6):1181-1183.
(24) Kaneko, J., Ozawa, T., Tomita, T., Kamio, Y. (1997) Sequential binding of staphylococcus gamma-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface. Biosci. Biotechnol. Biochem., 61(5):846-851.
(25) Sugawara-Tomita, N., Tomita, T., Kamio, Y (2002) Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3. J. Bacteriol., 184(17):4747-4756.
(26) Nguyen, V.T., Kamio, Y., Higuchi, H. (2003) Single-molecule imaging of cooperative assembly of gamma-hemolysin on erythrocyte membranes. EMBO. J., 22(19):4968-4979.
(27) Nguyen, A.H., Nguyen, V.T., Kamio, Y., Higuchi, H. (2006) Single-molecule visualization of environment-sensitive fluorophores inserted into cell membranes by staphylococcal gamma-hemolysin. Biochemistry., 45(8):2570-2576.
(28) Tomita, N., Abe, K., Kamio, Y., Ohta, M. (2011) Cluster-forming property correlated with hemolytic activity by staphylococcal -hemolysin transmembrane pores. FEBS. Lett., 585(21):3452–3456.
(29) Cheley, S., Malghani, M.S., Song, L., Hobaugh, M., Gouaux, J.E., Yang, J., Bayley, H. (1997) Spontaneous oligomerization of a staphylococcal alpha-hemolysin conformationally constrained by removal of residues that form the transmembrane beta-barrel. Protein. Eng., 10(12):1433-1443.
(30) Jayasinghe, L., Miles, G., Bayley, H. (2006) Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217. J. Biol. Chem., 281(4):2195-2204.
(31) Kaneko, J., Mascarenas, A.L., Huda, M.N., Tomita, T., Kamio, Y. (1998) An N-terminal region of LukF of staphylococcal leukocidin/gamma-hemolysin crucial for the biological activity of the toxin. Biosci. Biotechnol. Biochem., 62(7):1465-1467.
(32) Takeda, K., Tanaka, Y., Abe, N., Kaneko, J. (2018) Intermolecular ionic interactions serve as a possible switch for stem release in the staphylococcal bi-component toxin for β-barrel pore assembly. Toxicon., 155:43-48.
(33) Inoue, H., Nojima, H., Okayama, H. (1990). High efficiency transformation of Escherichia coli with plasmids. Gene., 96(1):23-28.
(34) Kunkel, T.A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA., 82(2):488-492.
(35) Sugimoto, M., Esaki, N., Tanaka, H., Soda, K. (1989) A simple and efficient method for the oligonucleotide-directed mutagenesis using plasmid DNA template and phosphorothioate-modified nucleotide. Anal. Biochem., 179(2):309-311.
(36) Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature., 227(5259):680-685.
(37) Alsever, J.B., and Ainslie, R.B. (1941) A new method for the preparation of dilute blood plasma and the operation of a complete transfusion service. N.Y. State J. Med., 41:126-131.
(38) 長崎 由依（2014）二成分性膜孔形成毒素 γ-hemolysin のS 成分の活性に関与する因子の探索東北大学修士論文
(39) Nguyen, V.T., Higuchi, H., Kamio, Y. (2002) Controlling pore assembly of staphylococcal gamma-hemolysin by low temperature and by disulphide bond formation in double-cysteine LukF mutants. Mol. Microbiol., 45(6):1485-1498.
(40) Rasband, W.S. (1997-2012) ImageJ, U. S. National Institutes of Health, Bethesda, Maryland, USA. http://imagej.nih.gov/ij/
(41) Schneider, C.A., Rasband, W.S., Eliceiri, K.W. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods., 9(7):671-675.
(42) Welch, B.L. (1947) The generalization of “Student’s” problem when several different population variances are involved. Biometrika., 34(1-2):28-35.
(43) Prevost, G., Bouakham, T., Piemont, Y., Monteil, H. (1995) Characterisation of a synergohymenotropic toxin produced by Staphylococcus intermedius. FEBS. Lett., 376(3):135-140.
(44) Takeda, K., Tanaka, Y., Kaneko, J. (2020) The N-terminal amino-latch region of Hlg2 component of staphylococcal bi-component γ- haemolysin is dispensable for prestem release to form β-barrel pores. J. Biochem., 168(4):349-354.
(45) Wilkins, M.R., Gasteiger, E., Bairoch, A., Sanchez, J.C., Williams, K.L., Appel, R.D., Hochstrasser, D.F. (1999) Protein identification and analysis tools in the ExPASy server. Methods. Mol. Biol., 112:531-552.
(46) De, S., Olson, R. (2011) Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins. Proc. Natl. Acad. Sci. USA., 108(18):7385-7390.
(47) 竹下 珠由 (2014) 黄色ブドウ球菌の二成分性膜孔形成血球崩壊毒素における S 成分の細胞特異性に関与する領域の解析. 東北大学修士論文
(48) Peng, Z., Takeshita, M., Shibata, N., Tada, H., Tanaka, Y., Kaneko, J. (2018) Rim domain loops of staphylococcal β-pore forming bi-component toxin S-components recognize target human erythrocytes in a coordinated manner. J. Biochem., 164(2):93-102.
(49) Seilie, E.S., Bubeck Wardenburg, J. (2017) Staphylococcus aureus pore-forming toxins: The interface of pathogen and host complexity. Semin. Cell. Dev. Biol., 72:101–116.
(50) Peng, Z., Shibata, N., Tada, H., Kaneko, J. (2018) Cytotoxicity analysis of staphylococcal bi-component β-pore forming toxins using the CHO cells expressing human lymphocyte receptor CCR5. Biosci. Biotechnol. Biochem., 82(12):2094-2097.
(51) Vrieling, M., Koymans, K.J., Heesterbeek, D.A., Aerts, P.C., Rutten, V.P., de Haas, C.J., van Kessel, K.P., Koets, A.P., Nijland, R., van Strijp, J.A. (2015) Bovine Staphylococcus aureus secretes the leukocidin LukMF' to kill migrating neutrophils through CCR1. mBio., 6(3):e00335.
(52) Spaan, A.N., Reyes-Robles, T., Badiou, C., Cochet, S., Boguslawski, K.M., Yoong, P., Day, C.J., de Haas, C.J., van Kessel, K.P., Vandenesch, F., Jennings, M.P., Le Van Kim, C., Colin, Y., van Strijp, J.A., Henry, T., Torres, V.J. (2015) Staphylococcus aureus Targets the Duffy Antigen Receptor for Chemokines (DARC) to Lyse Erythrocytes. Cell. Host. Microbe., 18(3):363-370.
(53) Spaan, A.N., Schiepers, A., de Haas, C.J., van Hooijdonk, D.D., Badiou, C., Contamin, H., Vandenesch, F., Lina, G., Gerard, N.P., Gerard, C., van Kessel, K.P., Henry, T., van Strijp, J.A. (2015) Differential Interaction of the Staphylococcal Toxins Panton-Valentine Leukocidin and γ- Hemolysin CB with Human C5a Receptors. J. Immunol., 195(3):1034-1043.
(54) Mumberg, D., Müller, R., Funk, M. (1994) Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic. Acids. Res., 22(25):5767-5768.
(55) Jones, E.W. (1977) Proteinase mutants of Saccharomyces cerevisiae. Genetics., 85(1):23-33.
(56) Gietz, R.D., Woods, R.A. (2002) Transformation of yeast by lithium acetate/single-stranded carrierDNA/polyethylene glycol method. Methods. Enzym., 350:87-96.
(57) Drew, D., Newstead, S., Sonoda, Y., Kim, H., von Heijne, G., Iwata, S. (2008) GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae. Nat. Protoc., 3(5):784-798.
(58) Nossal, N.G., Heppel, L.A. (1966) The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J. Biol. Chem., 241(13):3055-3062.
(59) Shen, S.H., Chrétien, P., Bastien, L., Slilaty, S.N. (1991) Primary sequence of the glucanase gene from Oerskovia xanthineolytica. Expression and purification of the enzyme from Escherichia coli. J. Biol. Chem., 266(2):1058-1063.
(60) Holcomb, C.L., Etcheverry, T., Schekman, R. (1987) Isolation of secretory vesicles from Saccharomyces cerevisiae. Anal. Biochem., 166(2):328-334.
(61) Arnold, C.E., Parekh, R.N., Yang, W., Wittrup, K.D. (1998) Leader peptide efficiency correlates with signal recognition particle dependence in Saccharomyces cerevisiae. Biotechnol. Bioeng., 59(3):286-293.
(62) Shiroishi, M., Tsujimoto, H., Makyio, H., Asada, H., Yurugi-Kobayashi, T., Shimamura, T., Murata, T., Nomura, N., Haga, T., Iwata, S., Kobayashi, T. (2012) Platform for the rapid construction and evaluation of GPCRs for crystallography in Saccharomyces cerevisiae. Microb. Cell. Fact., 11:78.
(63) Indge, K.J. (1968) The effects of various anions and cations on the lysis of yeast protoplasts by osmotic shock. J. Gen. Microbiol., 51(3):425-432.
(64) Mosmann, T. (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods., 65(1-2):55-63.
(65) 彭 昭 (2018) 黄色ブドウ球菌二成分性膜孔形成毒素 LukED の S 成分の細胞特異性に関する解析.東北大学博士論文.
(66) Robertson, N., Rappas, M., Doré, A.S., Brown, J., Bottegoni, G., Koglin, M., Cansfield, J., Jazayeri, A., Cooke, R.M., Marshall, F.H. (2018) Structure of the complement C5a receptor bound to the extra-helical antagonist NDT9513727. Nature., 553(7686):111-114.
(67) Reen, D.J. (1994) Enzyme-linked immunosorbent assay (ELISA). Methods. Mol. Biol., 32:461-466.
(68) Piliarik, M., Vaisocherová, H., Homola, J. (2009) Surface plasmon resonance biosensing. Methods. Mol. Biol., 503:65-88.
(69) Walther, D.M., Rapaport, D., Tommassen, J. (2009) Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence. Cell. Mol. Life Sci., 66(17), 2789-2804.
(70) Misra, R. (2012) Assembly of the β-barrel outer membrane proteins in Gram-negative bacteria, mitochondria, and chloroplasts. ISRN. Mol. Biol., 2012, 708203.
(71) Sklar, J.G., Wu, T., Kahne, D., Silhavy, T.J. (2007) Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes. Dev., 21(19):2473-2484.
(72) Noinaj, N., Gumbart, J.C., Buchanan, S.K. (2016) The β-barrel assembly machinery in motion. Nat. Rev. Microbiol., 15(4):197-204.
(73) Dal Peraro, M., van der Goot, F.G. (2016) Pore-forming toxins: ancient, but never really out of fashion. Nat. Rev. Microbiol., 14(2):77-92.
(74) Nariya, H., Izaki, K., Kamio, Y. (1993) The C-terminal region of the S component of staphylococcal leukocidin is essential for the biological activity of the toxin. FEBS. Lett., 329(1-2):219-222.
(75) Nariya, H., Kamio, Y. (1995) Identification of the essential regions for LukS- and H gamma II-specific functions of staphylococcal leukocidin and gamma-hemolysin. Biosci. Biotechnol. Biochem., 59(8):1603-1604.
(76) Nariya, H., Nishiyama, A., Kamio, Y. (1997) Identification of the minimum segment in which the threonine246 residue is a potential phosphorylated site by protein kinase A for the LukS-specific function of staphylococcal leukocidin. FEBS. Lett., 415(1):96-100.
(77) Nariya, H., Shimatani, A., Tomita, T., Kamio, Y. (1997) Identification of the essential amino acid residues in lukS for the hemolytic activity of staphylococcal leukocidin towards rabbit erythrocytes. Biosci. Biotechnol. Biochem., 61(12):2095-2099.
(78) Nishiyama, A., Nariya, H., Kamio, Y. (1998) Phosphorylation of LukS by protein kinase A is crucial for the LukS-specific function of the staphylococcal leukocidin on human polymorphonuclear leukocytes. Biosci. Biotechnol. Biochem., 62(9):1834-1838.
(79) Yokota, K., Sugawara. N., Nariya, H., Kaneko, J., Tomita, T., Kamio, Y. (1998) Further study on the two pivotal parts of Hlg2 for the full hemolytic activity of staphylococcal gamma-hemolysin. Biosci. Biotechnol. Biochem., 62(9):1745-1750.
(80) Yokota, K., Kamio, Y. (2000) Tyrosine72 residue at the bottom of rim domain in LukF crucial for the sequential binding of the staphylococcal gamma-hemolysin to human erythrocytes. Biosci. Biotechnol. Biochem., 64(12):2744-2747.
(81) Nishiyama, A., Guerra, M.A., Sugawara, N., Yokota, K., Kaneko, J., Kamio, Y. (2002) Identification of serine138 residue in the 4-residue segment K135K136I137S138 of LukS-I component of Staphylococcus intermedius leukocidin crucial for the LukS-I-specific function of staphylococcal leukocidin. Biosci. Biotechnol. Biochem., 66(2):328-335.
(82) 門馬 直太 (2004) 黄色ブドウ球菌のγ-ヘモリジンの血球認識機構に関する研究.東北大学博士論文
(83) Tanaka, Y., Hirano, N., Kaneko, J., Kamio, Y., Yao, M., Tanaka, I. (2011) 2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structure. Protein. Sci., 20(2):448-456.
(84) Jares-Erijman, E.A., Jovin, T.M. (2003) FRET imaging. Nat. Biotechnol., 21(11):1387-1395.
(85) Ghanem, N., Kanagami, N., Matsui, T., Takeda, K., Kaneko, J., Shiraishi, Y., Choe, C.A., Uchikubo-Kamo, T., Shirouzu, M., Hashimoto, T., Ogawa, T., Matsuura, T., Po-Ssu, H., Yokoyama, T., Tanaka, Y. (2022) Chimeric mutants of staphylococcal hemolysin, which act as both one-component and two- component hemolysin, created by grafting the stem domain. FEBS. J., Advance online publication (doi: 10.1111/febs.16354).
(86) 上田 淳基 (2018) 黄色ブドウ球菌膜孔形成毒素のβバレル型膜孔形成機構の解明.東北大学修士論文
(87) 杉浦 慎一郎 (2021) 黄色ブドウ球菌の膜孔形成毒素のβバレル形成に関わる stem 残基の解析.東北大学修士論文
(88) Noda, M., Kato, I., Matsuda, F., Hiratama, T. (1981) Mode of action of staphylococcal leukocidin: relationship between binding of 125I-labeled S and F components of leukocidin to rabbit polymorphonuclear leukocytes and leukocidin activity. Infect. Immun., 34(2):362-367.
(89) Moore, K.L. (2003) The biology and enzymology of protein tyrosine O-sulfation. J. Biol. Chem., 278(27):24243-24246.
(90) Brown, A.J., Dyos, S.L., Whiteway, M.S., White, J.H., Watson, M.A., Marzioch, M., Clare, J.J., Cousens, D.J., Paddon, C., Plumpton, C., Romanos, M.A., Dowell, S.J. (2000) Functional coupling of mammalian receptors to the yeast mating pathway using novel yeast/mammalian G protein alpha-subunit chimeras. Yeast., 16(1):11-22.
(91) Nomiyama, H., Yoshie, O. (2015) Functional roles of evolutionary conserved motifs and residues in vertebrate chemokine receptors. J. Leukoc. Biol., 97(1):39-47.
(92) Howorka, S., Bayley, H. (2002) Probing distance and electrical potential within a protein pore with tethered DNA. Biophys. J., 83(6):3202-3210.
(93) Hu, Z.L., Huo, M.Z., Ying, YL, Long YT. (2021) Biological Nanopore Approach for Single-Molecule Protein Sequencing. Angew. Chem. Int. Ed. Engl., 60(27):14738-14749.
論文の公開元へ
