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Volumn 91, Issue 2, 2013, Pages 59-66

Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin

Author keywords

Cholesterol; Hemolysis; Oligomerization; Pyolysin

Indexed keywords

C-TERMINAL DOMAINS; HEMOLYSIS; HEMOLYTIC ACTIVITY; MEMBRANE BINDING; MEMBRANE INSERTION; MONOMER STRUCTURES; PROTEOLYTIC FRAGMENTS; PYOLYSIN;

EID: 84875762324     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/bcb-2012-0065     Document Type: Article
Times cited : (10)

References (24)
  • 1
    • 0033576256 scopus 로고    scopus 로고
    • Streptolysin O: Inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation
    • 10.1021/bi991678y. 10563803
    • Abdel Ghani E.M. Weis S. Walev I. et al. 1999. Streptolysin O: inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation. Biochemistry, 38: 15204-15211. 10.1021/bi991678y. 10563803.
    • (1999) Biochemistry , vol.38 , pp. 15204-15211
    • Abdel Ghani, E.M.1    Weis, S.2    Walev, I.3
  • 2
    • 0030920430 scopus 로고    scopus 로고
    • The Arcanobacterium (Actinomyces) pyogenes hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family
    • 9324258
    • Billington S.J. Jost B.H. Cuevas W.A. et al. 1997. The Arcanobacterium (Actinomyces) pyogenes hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family. J. Bacteriol. 179: 6100-6106. 9324258.
    • (1997) J. Bacteriol , vol.179 , pp. 6100-6106
    • Billington, S.J.1    Jost, B.H.2    Cuevas, W.A.3
  • 3
    • 0016715847 scopus 로고
    • Effect of streptolysin O on erythrocyte membranes, liposomes, and lipid dispersions
    • 10.1083/jcb.67.1.160. doi:1176529
    • Duncan J.L. Schlegel R. 1975. Effect of streptolysin O on erythrocyte membranes, liposomes, and lipid dispersions. A protein-cholesterol interaction. J. Cell Biol. 67: 160-174. 10.1083/jcb.67.1.160. doi:1176529.
    • (1975) A Protein-cholesterol Interaction. J. Cell Biol , vol.67 , pp. 160-174
    • Duncan, J.L.1    Schlegel, R.2
  • 4
    • 0031927661 scopus 로고    scopus 로고
    • Cholesterol-Streptolysin O Interaction: An em Study of Wild-Type and Mutant Streptolysin O. J Struct
    • 10.1006/jsbi.1998/3989. 9705878
    • Harris J.R. Adrian M. Bhakdi S. et al. 1998. Cholesterol-Streptolysin O Interaction: An EM Study of Wild-Type and Mutant Streptolysin O. J Struct. Biol. 121: 343-355. 10.1006/jsbi.1998/3989. 9705878.
    • (1998) Biol , vol.121 , pp. 343-355
    • Harris, J.R.1    Adrian, M.2    Bhakdi, S.3
  • 5
    • 78649908803 scopus 로고    scopus 로고
    • Cholesterol microcrystals and cochleate cylinders: Attachment of pyolysin oligomers and domain 4
    • 10.1016/j.jsb.2010.07.010. 20682347
    • Harris J.R. Lewis R.J. Baik C. et al. 2011. Cholesterol microcrystals and cochleate cylinders: attachment of pyolysin oligomers and domain 4. J. Struct. Biol. 173: 38-45. 10.1016/j.jsb.2010.07.010. 20682347.
    • (2011) J. Struct. Biol , vol.173 , pp. 38-45
    • Harris, J.R.1    Lewis, R.J.2    Baik, C.3
  • 6
    • 77952302993 scopus 로고    scopus 로고
    • The Cholesterol-Dependent Cytolysin Family of Gram-Positive Bacterial Toxins
    • 10.1007/978-90-481-8622-8-20. 20213558
    • Heuck A. Moe P. Johnson B. 2010. The Cholesterol-Dependent Cytolysin Family of Gram-Positive Bacterial Toxins. Subcell. Biochem. 51: 551-577. 10.1007/978-90-481-8622-8-20. 20213558.
    • (2010) Subcell. Biochem , vol.51 , pp. 551-577
    • Heuck, A.1    Moe, P.2    Johnson, B.3
  • 7
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulphide trapping synchonizes the insertion of the transmembrane beta-sheet from a pre-pore intermediate
    • 11102453
    • Hotze E. Wilson-Kubalek E. Rossjohn J. et al. 2001. Arresting pore formation of a cholesterol-dependent cytolysin by disulphide trapping synchonizes the insertion of the transmembrane beta-sheet from a pre-pore intermediate. J. Biol. Chem. 276: 8261-8268. 11102453.
    • (2001) J. Biol. Chem , vol.276 , pp. 8261-8268
    • Hotze, E.1    Wilson-Kubalek, E.2    Rossjohn, J.3
  • 8
    • 0033972716 scopus 로고    scopus 로고
    • Genetic and biochemical properties of a hemolysin (pyolysin) produced by a swine isolate of Arcanobacterium (Actinomyces) pyogenes
    • 10711593
    • Ikegami M. Hashimoto N. Kaidoh T. et al. 2000. Genetic and biochemical properties of a hemolysin (pyolysin) produced by a swine isolate of Arcanobacterium (Actinomyces) pyogenes. Microbiol Immunol 44: 1-7. 10711593.
    • (2000) Microbiol Immunol , vol.44 , pp. 1-7
    • Ikegami, M.1    Hashimoto, N.2    Kaidoh, T.3
  • 9
    • 0023656177 scopus 로고
    • Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens
    • 10.1111/j.1432-1033.1987.tb13355.x. 2888650
    • Iwamoto M. Ohno-Iwashita Y. Ando S. 1987. Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens. Eur. J. Biochem. 167: 425-430. 10.1111/j.1432-1033.1987.tb13355.x. 2888650.
    • (1987) Eur. J. Biochem , vol.167 , pp. 425-430
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 10
    • 0025244264 scopus 로고
    • Effect of isolated C-terminal fragment of theta-toxin (perfringolysin O) on toxin assembly and membrane lysis
    • 10.1111/j.1432-1033.1990.tb19422.x. 2253619
    • Iwamoto M. Ohno-Iwashita Y. Ando S. 1990. Effect of isolated C-terminal fragment of theta-toxin (perfringolysin O) on toxin assembly and membrane lysis. Eur. J. Biochem. 194: 25-31. 10.1111/j.1432-1033.1990.tb19422.x. 2253619.
    • (1990) Eur. J. Biochem , vol.194 , pp. 25-31
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 11
    • 84855690465 scopus 로고    scopus 로고
    • Prediction of protein secondary structure from circular dichroism using theoretically derived spectra
    • 10.1002/prot.23188. 22095872
    • Louis-Jeune C. Andrade-Navarro M.A. Perez-Iratxeta C. 2011. Prediction of protein secondary structure from circular dichroism using theoretically derived spectra. Proteins. In press. 10.1002/prot.23188. 22095872.
    • (2011) Proteins. in Press
    • Louis-Jeune, C.1    Andrade-Navarro, M.A.2    Perez-Iratxeta, C.3
  • 12
    • 0025045387 scopus 로고
    • Characteristics of self-quenching of the fluorescence of lipid-conjugated rhodamine in membranes
    • 2380172
    • MacDonald R.I. 1990. Characteristics of self-quenching of the fluorescence of lipid-conjugated rhodamine in membranes. J. Biol. Chem. 265: 13533-13539. 2380172.
    • (1990) J. Biol. Chem , vol.265 , pp. 13533-13539
    • Macdonald, R.I.1
  • 13
    • 0032536856 scopus 로고    scopus 로고
    • Assembly mechanism of the oligomeric streptolysin O pore: The early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization
    • 10.1093/emboj/17.6.1598. 9501081
    • Palmer M. Harris R. Freytag C. et al. 1998. Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization. EMBO J. 17: 1598-1605. 10.1093/emboj/17.6.1598. 9501081.
    • (1998) EMBO J , vol.17 , pp. 1598-1605
    • Palmer, M.1    Harris, R.2    Freytag, C.3
  • 14
    • 0029909653 scopus 로고    scopus 로고
    • Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis
    • 8900142
    • Palmer M. Saweljew P. Vulicevic I. et al. 1996. Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis. J. Biol. Chem. 271: 26664-26667. 8900142.
    • (1996) J. Biol. Chem , vol.271 , pp. 26664-26667
    • Palmer, M.1    Saweljew, P.2    Vulicevic, I.3
  • 15
    • 0029032460 scopus 로고
    • Kinetics of streptolysin O self-assembly
    • 10.1111/j.1432-1033.1995.tb20711.x. 7635150
    • Palmer M. Valeva A. Kehoe M. et al. 1995. Kinetics of streptolysin O self-assembly. Eur. J. Biochem. 231: 388-395. 10.1111/j.1432-1033.1995.tb20711. x. 7635150.
    • (1995) Eur. J. Biochem , vol.231 , pp. 388-395
    • Palmer, M.1    Valeva, A.2    Kehoe, M.3
  • 17
    • 14144251524 scopus 로고    scopus 로고
    • Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin
    • 10.1073/pnas.0403229101. 15637162
    • Polekhina G. Giddings K.S. Tweten R.K. et al. 2005. Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin. Proc. Natl. Acad. Sci. U.S.A. 102: 600-605. 10.1073/pnas. 0403229101. 15637162.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 600-605
    • Polekhina, G.1    Giddings, K.S.2    Tweten, R.K.3
  • 18
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • 10.1016/S0092-8674(00)80251-2. 9182756
    • Rossjohn J. Feil S. McKinstry W. et al. 1997. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell, 89: 685-692. 10.1016/S0092-8674(00)80251-2. 9182756.
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.2    McKinstry, W.3
  • 19
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • 10555145
    • Shatursky O. Heuck A. Shepard L. et al. 1999. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins. Cell, 99: 293-299. 10555145.
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1    Heuck, A.2    Shepard, L.3
  • 20
    • 84875800645 scopus 로고    scopus 로고
    • Perfringolysin O: An alpha-helical to beta-sheet transition identified by fluorescence spectroscopy
    • 9772185
    • Shepard L. Hueck A. Hamman B. et al. 1998. Perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy. Biochemistry 37, 293-299. 9772185.
    • (1998) Biochemistry , vol.37 , pp. 293-299
    • Shepard, L.1    Hueck, A.2    Hamman, B.3
  • 21
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • 10.1016/j.cell.2005.02.033. 15851031
    • Tilley S.J. Orlova E.V. Gilbert R.J.C. et al. 2005. Structural basis of pore formation by the bacterial toxin pneumolysin. Cell, 121: 247-256. 10.1016/j.cell.2005.02.033. 15851031.
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Gilbert, R.J.C.3
  • 22
    • 0025821214 scopus 로고
    • Isolation of a tryptic fragment from Clostridium perfringens theta-toxin that contains sites for membrane binding and self-aggregation
    • 2061320
    • Tweten R.K. Harris R.W. Sims P.J. 1991. Isolation of a tryptic fragment from Clostridium perfringens theta-toxin that contains sites for membrane binding and self-aggregation. J. Biol. Chem. 266: 12449-12454. 2061320.
    • (1991) J. Biol. Chem , vol.266 , pp. 12449-12454
    • Tweten, R.K.1    Harris, R.W.2    Sims, P.J.3
  • 23
    • 0035830656 scopus 로고    scopus 로고
    • Streptolysin O: The C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oligomerization
    • 10.1016/S0005-2736(00)00360-6. 11342166
    • Weis S. Palmer M. 2001. Streptolysin O: the C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oligomerization. Biochim. Biophys. Acta, 1510: 292-299. 10.1016/S0005-2736(00)00360-6. 11342166.
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 292-299
    • Weis, S.1    Palmer, M.2
  • 24
    • 0028295796 scopus 로고
    • Resonance energy transfer: Methods and applications
    • 10.1006/abio.1994.1134. 8053542
    • Wu P. Brand L. 1994. Resonance energy transfer: methods and applications. Anal. Biochem. 218, 1-13. 10.1006/abio.1994.1134. 8053542.
    • (1994) Anal. Biochem , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.