메뉴 건너뛰기




Volumn 588, Issue 1, 2014, Pages 35-40

Permeability characteristics of cell-membrane pores induced by ostreolysin A/pleurotolysin B, binary pore-forming proteins from the oyster mushroom

Author keywords

Electrophysiology; Membrane attack complex perforin (MACPF) domain; Pleurotus ostreatus; Pore forming protein

Indexed keywords

CELL PROTEIN; COMPLEMENT MEMBRANE ATTACK COMPLEX; OSTREOLYSIN A; PLEUROTOLYSIN B; UNCLASSIFIED DRUG; EDETIC ACID; FUNGAL PROTEIN; LANTHANUM; MACROGOL 8000; PERFORIN;

EID: 84891028518     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.10.038     Document Type: Article
Times cited : (17)

References (28)
  • 1
    • 3042555480 scopus 로고    scopus 로고
    • Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex
    • T. Tomita, K. Noguchi, H. Mimuro, F. Ukaji, K. Ito, N. Sugawara-Tomita, and Y. Hashimoto Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex J. Biol. Chem. 279 2004 26975 26982
    • (2004) J. Biol. Chem. , vol.279 , pp. 26975-26982
    • Tomita, T.1    Noguchi, K.2    Mimuro, H.3    Ukaji, F.4    Ito, K.5    Sugawara-Tomita, N.6    Hashimoto, Y.7
  • 2
    • 77958479289 scopus 로고    scopus 로고
    • Isolation and characterization of a novel two-component hemolysin, erylysin A and B, from an edible mushroom, Pleurotus eryngii
    • T. Shibata, M. Kudou, Y. Hoshi, A. Kudo, N. Nanashima, and K. Miyairi Isolation and characterization of a novel two-component hemolysin, erylysin A and B, from an edible mushroom, Pleurotus eryngii Toxicon 56 2010 1436 1442
    • (2010) Toxicon , vol.56 , pp. 1436-1442
    • Shibata, T.1    Kudou, M.2    Hoshi, Y.3    Kudo, A.4    Nanashima, N.5    Miyairi, K.6
  • 3
    • 84883238674 scopus 로고    scopus 로고
    • Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B
    • 10.1016/j.biochi.2013.06.012
    • K. Ota, A. Leonardi, M. Mikelj, M. Skočaj, T. Wohlschlager, M. Künzler, M. Aebi, M. Narat, I. Križaj, G. Anderluh, K. Sepčić, and P. Maček Membrane cholesterol and sphingomyelin, and ostreolysin A are obligatory for pore-formation by a MACPF/CDC-like pore-forming protein, pleurotolysin B Biochimie. 95 2013 1855 1864 10.1016/j.biochi.2013.06.012
    • (2013) Biochimie. , vol.95 , pp. 1855-1864
    • Ota, K.1    Leonardi, A.2    Mikelj, M.3    Skočaj, M.4    Wohlschlager, T.5    Künzler, M.6    Aebi, M.7    Narat, M.8    Križaj, I.9    Anderluh, G.10    Sepčić, K.11    Maček, P.12
  • 4
    • 63449118079 scopus 로고    scopus 로고
    • Aegerolysins: Structure, function, and putative biological role
    • S. Berne, L. Lah, and K. Sepčić Aegerolysins: structure, function, and putative biological role Protein Sci. 18 2009 694 706
    • (2009) Protein Sci. , vol.18 , pp. 694-706
    • Berne, S.1    Lah, L.2    Sepčić, K.3
  • 6
    • 0019434060 scopus 로고
    • Kinetics of hemolysis induced by equinatoxin, a cytolytic toxin from the sea anemone Actinia equina. Effect of some ions and pH
    • P. Maček, and D. Lebez Kinetics of hemolysis induced by equinatoxin, a cytolytic toxin from the sea anemone Actinia equina. Effect of some ions and pH Toxicon 19 1981 233 240
    • (1981) Toxicon , vol.19 , pp. 233-240
    • Maček, P.1    Lebez, D.2
  • 7
    • 0027398335 scopus 로고
    • Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes
    • G. Belmonte, C. Pederzolli, P. Maček, and G. Menestrina Pore formation by the sea anemone cytolysin equinatoxin II in red blood cells and model lipid membranes J. Membrane Biol. 131 1993 11 22
    • (1993) J. Membrane Biol. , vol.131 , pp. 11-22
    • Belmonte, G.1    Pederzolli, C.2    Maček, P.3    Menestrina, G.4
  • 9
    • 0023186359 scopus 로고
    • Biophysical analysis of novel transport pathways induced in red blood cell membranes
    • H. Ginsburg, and W.D. Stein Biophysical analysis of novel transport pathways induced in red blood cell membranes J. Membrane Biol. 96 1987 1 10
    • (1987) J. Membrane Biol. , vol.96 , pp. 1-10
    • Ginsburg, H.1    Stein, W.D.2
  • 10
    • 0000576265 scopus 로고
    • Pore size distribution analysis of gel substances by size exclusion chromatography
    • S. Kuga Pore size distribution analysis of gel substances by size exclusion chromatography J. Chromatogr. A 206 1981 449 461
    • (1981) J. Chromatogr. A , vol.206 , pp. 449-461
    • Kuga, S.1
  • 11
    • 0000560829 scopus 로고
    • Filtration, diffusion, and molecular sieving through porous cellulose membranes
    • E.M. Renkin Filtration, diffusion, and molecular sieving through porous cellulose membranes J. Gen. Physiol. 38 1954 225 243
    • (1954) J. Gen. Physiol. , vol.38 , pp. 225-243
    • Renkin, E.M.1
  • 12
    • 0034840842 scopus 로고    scopus 로고
    • Neuroblastoma cell lines - A versatile in vitro model in neurobiology
    • P. Shastry, A. Basu, and M.S. Rajadhyaksha Neuroblastoma cell lines - a versatile in vitro model in neurobiology Int. J. Neurosci. 108 2001 109 126
    • (2001) Int. J. Neurosci. , vol.108 , pp. 109-126
    • Shastry, P.1    Basu, A.2    Rajadhyaksha, M.S.3
  • 13
    • 18144365177 scopus 로고    scopus 로고
    • The use of Chinese hamster ovary (CHO) cells in the study of ion channels
    • N. Gamper, J.D. Stockand, and M.S. Shapiro The use of Chinese hamster ovary (CHO) cells in the study of ion channels J. Pharmacol. Toxicol. Meth. 51 2005 177 185
    • (2005) J. Pharmacol. Toxicol. Meth. , vol.51 , pp. 177-185
    • Gamper, N.1    Stockand, J.D.2    Shapiro, M.S.3
  • 14
    • 0037131367 scopus 로고    scopus 로고
    • Trachynilysin, a neurosecretory protein isolated from stonefish (Synanceia trachynis) venom, forms nonselective pores in the membrane of NG108-15 cells
    • G. Ouanounou, M. Malo, J. Stinnakre, A.S. Kreger, and J. Molgó Trachynilysin, a neurosecretory protein isolated from stonefish (Synanceia trachynis) venom, forms nonselective pores in the membrane of NG108-15 cells J. Biol. Chem. 277 2002 39119 39127
    • (2002) J. Biol. Chem. , vol.277 , pp. 39119-39127
    • Ouanounou, G.1    Malo, M.2    Stinnakre, J.3    Kreger, A.S.4    Molgó, J.5
  • 15
    • 0025996463 scopus 로고
    • Formation of ion-conductiong channels by the membrane attack complex proteins of complement
    • J.W. Shiver, J.R. Dankert, and A.F. Esser Formation of ion-conductiong channels by the membrane attack complex proteins of complement Biophys. J. 60 1991 761 769
    • (1991) Biophys. J. , vol.60 , pp. 761-769
    • Shiver, J.W.1    Dankert, J.R.2    Esser, A.F.3
  • 16
    • 0026695462 scopus 로고
    • Differential sensitivity of pneumolysin-induced channels to gating by divalent-cations
    • Y.E. Korchev, C.L. Bashford, and C.A. Pasternak Differential sensitivity of pneumolysin-induced channels to gating by divalent-cations J. Membrane Biol. 127 1992 195 203
    • (1992) J. Membrane Biol. , vol.127 , pp. 195-203
    • Korchev, Y.E.1    Bashford, C.L.2    Pasternak, C.A.3
  • 17
    • 0029062191 scopus 로고
    • Lytic reaction of in vivo primed peritoneal exudate CTL. Induction of high-conductance single channels in the target cell membrane
    • R. Lavy, Y.H. Mika, D. Rosen, G. Berke, and O. Binah Lytic reaction of in vivo primed peritoneal exudate CTL. Induction of high-conductance single channels in the target cell membrane J. Immunol. 154 1995 5039 5048
    • (1995) J. Immunol. , vol.154 , pp. 5039-5048
    • Lavy, R.1    Mika, Y.H.2    Rosen, D.3    Berke, G.4    Binah, O.5
  • 18
    • 0032007852 scopus 로고    scopus 로고
    • A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers
    • Y.E. Korchev, C.L. Bashford, C. Pederzolli, C.A. Pasternak, P.J. Morgan, P.W. Andrew, and T.J. Mitchell A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers Biochem. J. 329 1998 571 577
    • (1998) Biochem. J. , vol.329 , pp. 571-577
    • Korchev, Y.E.1    Bashford, C.L.2    Pederzolli, C.3    Pasternak, C.A.4    Morgan, P.J.5    Andrew, P.W.6    Mitchell, T.J.7
  • 19
    • 0034702810 scopus 로고    scopus 로고
    • The Mechanism of pore assembly for a cholesterol-dependent cytolysin: Formation of a large prepore complex precedes the insertion of the transmembrane β-hairpins
    • L.A. Shepard, O. Shatursky, A.E. Johnson, and R.K. Tweten The Mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane β-hairpins Biochemistry 39 2000 10284 10293
    • (2000) Biochemistry , vol.39 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 20
    • 0036521875 scopus 로고    scopus 로고
    • CD59 blocks not only the insertion of C9 into MAC but inhibits ion channel formation by homologous C5b-8 as well as C5b-9
    • I. Farkas, L. Baranyi, Y. Ishikawa, N. Okada, C. Bohata, D. Budai, A. Fukuda, M. Imai, and H. Okada CD59 blocks not only the insertion of C9 into MAC but inhibits ion channel formation by homologous C5b-8 as well as C5b-9 J. Physiol.-London 539 2002 537 545
    • (2002) J. Physiol.-London , vol.539 , pp. 537-545
    • Farkas, I.1    Baranyi, L.2    Ishikawa, Y.3    Okada, N.4    Bohata, C.5    Budai, D.6    Fukuda, A.7    Imai, M.8    Okada, H.9
  • 22
    • 47849083269 scopus 로고    scopus 로고
    • Demonstration of a cholesterol-dependent cytolysin in a noninsecticidal Bacillus sphaericus strain and evidence for widespread distribution of the toxin within the species
    • C. From, P.E. Granum, and S.P. Hardy Demonstration of a cholesterol-dependent cytolysin in a noninsecticidal Bacillus sphaericus strain and evidence for widespread distribution of the toxin within the species FEMS Microbiol. Lett. 286 2008 85 92
    • (2008) FEMS Microbiol. Lett. , vol.286 , pp. 85-92
    • From, C.1    Granum, P.E.2    Hardy, S.P.3
  • 23
    • 39749125475 scopus 로고    scopus 로고
    • Pneumolysin generates multiple conductance pores in the membrane of nucleated cells
    • R.G. El-Rachkidy, N.W. Davies, and P.W. Andrew Pneumolysin generates multiple conductance pores in the membrane of nucleated cells Biochem. Biophys. Res. Commun. 368 2008 786 792
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 786-792
    • El-Rachkidy, R.G.1    Davies, N.W.2    Andrew, P.W.3
  • 25
    • 0025282764 scopus 로고
    • Pore-forming toxins: Experiments with S aureus α-toxin, C perfringens θ-toxin and E coli haemolysin in lipid bilayers, liposomes and intact cells
    • G. Menestrina, C.L. Bashford, and C.A. Pasternak Pore-forming toxins: experiments with S. aureus α-toxin, C. perfringens θ-toxin and E. coli haemolysin in lipid bilayers, liposomes and intact cells Toxicon 28 1990 477 491
    • (1990) Toxicon , vol.28 , pp. 477-491
    • Menestrina, G.1    Bashford, C.L.2    Pasternak, C.A.3
  • 26
    • 0021968046 scopus 로고
    • The membrane attack complex of complement - C5b-8 complex as accelerator of C9 polymerization
    • J. Tschopp, E.R. Podack, and H.J. Mullereberhard The membrane attack complex of complement - C5b-8 complex as accelerator of C9 polymerization J. Immunol. 134 1985 495 499
    • (1985) J. Immunol. , vol.134 , pp. 495-499
    • Tschopp, J.1    Podack, E.R.2    Mullereberhard, H.J.3
  • 28
    • 84857650341 scopus 로고    scopus 로고
    • Membrane assembly of the cholesterol-dependent cytolysin pore complex
    • E.M. Hotze, and R.K. Tweten Membrane assembly of the cholesterol- dependent cytolysin pore complex Biochim. Biophys. Acta 1818 2012 1028 1038
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1028-1038
    • Hotze, E.M.1    Tweten, R.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.