메뉴 건너뛰기




Volumn 111, Issue 49, 2014, Pages E5312-E5320

The cholesterol-dependent cytolysins pneumolysin and streptolysin O require binding to red blood cell glycans for hemolytic activity

Author keywords

Cholesterol dependent cytolysin; Glycan binding; Pneumolysin; Streptococcus pneumoniae; Streptolysin O

Indexed keywords

CARBOHYDRATE; CHOLESTEROL DEPENDENT CYTOLYSIN; CYTOLYSIN; GLYCAN; GLYCOLIPID; LECTIN; MONOCLONAL ANTIBODY; PNEUMOLYSIN; SIALYL LEWIS X ANTIGEN; STREPTOLYSIN O; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CD15 ANTIGEN; LACTO-N-NEOTETRAOSE; OLIGOSACCHARIDE; PLY PROTEIN, STREPTOCOCCUS PNEUMONIAE; POLYSACCHARIDE; PROTEIN BINDING; STREPTOLYSIN;

EID: 84917694808     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1412703111     Document Type: Article
Times cited : (100)

References (48)
  • 1
    • 0027524269 scopus 로고
    • Molecular analysis of the pathogenicity of Streptococcus pneumoniae: The role of pneumococcal proteins
    • Paton JC, Andrew PW, Boulnois GJ, Mitchell TJ (1993) Molecular analysis of the pathogenicity of Streptococcus pneumoniae: The role of pneumococcal proteins. Annu Rev Microbiol 47:89-115.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 89-115
    • Paton, J.C.1    Andrew, P.W.2    Boulnois, G.J.3    Mitchell, T.J.4
  • 2
    • 3543016107 scopus 로고    scopus 로고
    • Membrane-dependent conforma-tional changes initiate cholesterol-dependent cytolysin oligomerization and inter-subunit beta-strand alignment
    • Ramachandran R, Tweten RK, Johnson AE (2004) Membrane-dependent conforma-tional changes initiate cholesterol-dependent cytolysin oligomerization and inter-subunit beta-strand alignment. Nat Struct Mol Biol 11(8):697-705.
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.8 , pp. 697-705
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 3
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An alpha-helical to beta-sheet transition identified by fluorescence spectroscopy
    • Shepard LA, et al. (1998) Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An alpha-helical to beta-sheet transition identified by fluorescence spectroscopy. Biochemistry 37(41):14563-14574.
    • (1998) Biochemistry , vol.37 , Issue.41 , pp. 14563-14574
    • Shepard, L.A.1
  • 4
    • 84862605391 scopus 로고    scopus 로고
    • Packing a punch: The mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins
    • Dunstone MA, Tweten RK (2012) Packing a punch: The mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins. Curr Opin Struct Biol 22(3):342-349.
    • (2012) Curr Opin Struct Biol , vol.22 , Issue.3 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 5
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • Shatursky O, et al. (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins. Cell 99(3):293-299.
    • (1999) Cell , vol.99 , Issue.3 , pp. 293-299
    • Shatursky, O.1
  • 6
    • 0015405486 scopus 로고
    • Some factors influencing the effect of cholesterol on streptolysin O activity
    • Watson KC, Rose TP, Kerr EJ (1972) Some factors influencing the effect of cholesterol on streptolysin O activity. J Clin Pathol 25(10):885-891.
    • (1972) J Clin Pathol , vol.25 , Issue.10 , pp. 885-891
    • Watson, K.C.1    Rose, T.P.2    Kerr, E.J.3
  • 7
    • 0030037296 scopus 로고    scopus 로고
    • Induction of cytokine gene expression by listeriolysin O and roles of macrophages and NK cells
    • Nishibori T, Xiong H, Kawamura I, Arakawa M, Mitsuyama M (1996) Induction of cytokine gene expression by listeriolysin O and roles of macrophages and NK cells. Infect Immun 64(8):3188-3195.
    • (1996) Infect Immun , vol.64 , Issue.8 , pp. 3188-3195
    • Nishibori, T.1    Xiong, H.2    Kawamura, I.3    Arakawa, M.4    Mitsuyama, M.5
  • 8
    • 0027463286 scopus 로고
    • Membrane damage and interleukin-1 production in murine macrophages exposed to listeriolysin O
    • Yoshikawa H, et al. (1993) Membrane damage and interleukin-1 production in murine macrophages exposed to listeriolysin O. Infect Immun 61(4):1334-1339.
    • (1993) Infect Immun , vol.61 , Issue.4 , pp. 1334-1339
    • Yoshikawa, H.1
  • 9
    • 0031776879 scopus 로고    scopus 로고
    • Listeriolysin O: Cholesterol inhibits cytolysis but not binding to cellular membranes
    • Jacobs T, et al. (1998) Listeriolysin O: Cholesterol inhibits cytolysis but not binding to cellular membranes. Mol Microbiol 28(6):1081-1089.
    • (1998) Mol Microbiol , vol.28 , Issue.6 , pp. 1081-1089
    • Jacobs, T.1
  • 10
    • 16544370492 scopus 로고    scopus 로고
    • Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin
    • Giddings KS, Zhao J, Sims PJ, Tweten RK (2004) Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin. Nat Struct Mol Biol 11(12):1173-1178.
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.12 , pp. 1173-1178
    • Giddings, K.S.1    Zhao, J.2    Sims, P.J.3    Tweten, R.K.4
  • 11
    • 0141706347 scopus 로고    scopus 로고
    • Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins
    • Giddings KS, Johnson AE, Tweten RK (2003) Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins. Proc Natl Acad Sci USA 100(20): 11315-11320.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.20 , pp. 11315-11320
    • Giddings, K.S.1    Johnson, A.E.2    Tweten, R.K.3
  • 12
    • 84891372554 scopus 로고    scopus 로고
    • Cell targeting by the Staphylococcus aureus pore-forming toxins: It's not just about lipids
    • DuMont AL, Torres VJ (2014) Cell targeting by the Staphylococcus aureus pore-forming toxins: It's not just about lipids. Trends Microbiol 22(1):21-27.
    • (2014) Trends Microbiol , vol.22 , Issue.1 , pp. 21-27
    • Dumont, A.L.1    Torres, V.J.2
  • 13
    • 84872358998 scopus 로고    scopus 로고
    • Characterization of pneumolysin from Streptococcus pneumoniae, interacting with carbohydrate moiety and cholesterol as a component of cell membrane
    • Lim JE, Park SA, Bong SM, Chi YM, Lee KS (2013) Characterization of pneumolysin from Streptococcus pneumoniae, interacting with carbohydrate moiety and cholesterol as a component of cell membrane. Biochem Biophys Res Commun 430(2): 659-663.
    • (2013) Biochem Biophys Res Commun , vol.430 , Issue.2 , pp. 659-663
    • Lim, J.E.1    Park, S.A.2    Bong, S.M.3    Chi, Y.M.4    Lee, K.S.5
  • 14
    • 2142825136 scopus 로고    scopus 로고
    • The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin
    • Nöllmann M, Gilbert R, Mitchell T, Sferrazza M, Byron O (2004) The role of cholesterol in the activity of pneumolysin, a bacterial protein toxin. Biophys J 86(5):3141-3151.
    • (2004) Biophys J , vol.86 , Issue.5 , pp. 3141-3151
    • Nöllmann, M.1    Gilbert, R.2    Mitchell, T.3    Sferrazza, M.4    Byron, O.5
  • 15
    • 62849083844 scopus 로고    scopus 로고
    • Differential carbohydrate recognition by Campylobacter jejuni strain 11168: Influences of temperature and growth conditions
    • Day CJ, et al. (2009) Differential carbohydrate recognition by Campylobacter jejuni strain 11168: Influences of temperature and growth conditions. PLoS ONE 4(3):e4927.
    • (2009) PLoS ONE , vol.4 , Issue.3 , pp. e4927
    • Day, C.J.1
  • 16
    • 34548497122 scopus 로고    scopus 로고
    • Presence of nonhemolytic pneumolysin in serotypes of Streptococcus pneumoniae associated with disease outbreaks
    • Jefferies JM, et al. (2007) Presence of nonhemolytic pneumolysin in serotypes of Streptococcus pneumoniae associated with disease outbreaks. J Infect Dis 196(6): 936-944.
    • (2007) J Infect Dis , vol.196 , Issue.6 , pp. 936-944
    • Jefferies, J.M.1
  • 17
    • 30744464885 scopus 로고    scopus 로고
    • Identification of invasive serotype 1 pneumococcal isolates that express nonhemolytic pneumolysin
    • Kirkham LA, et al. (2006) Identification of invasive serotype 1 pneumococcal isolates that express nonhemolytic pneumolysin. J Clin Microbiol 44(1):151-159.
    • (2006) J Clin Microbiol , vol.44 , Issue.1 , pp. 151-159
    • Kirkham, L.A.1
  • 18
    • 0030219032 scopus 로고    scopus 로고
    • Sequence variation in the Streptococcus pneumoniae pneumolysin gene affecting haemolytic activity and electro-phoretic mobility of the toxin
    • Lock RA, Zhang QY, Berry AM, Paton JC (1996) Sequence variation in the Streptococcus pneumoniae pneumolysin gene affecting haemolytic activity and electro-phoretic mobility of the toxin. Microb Pathog 21(2):71-83.
    • (1996) Microb Pathog , vol.21 , Issue.2 , pp. 71-83
    • Lock, R.A.1    Zhang, Q.Y.2    Berry, A.M.3    Paton, J.C.4
  • 19
    • 77749292162 scopus 로고    scopus 로고
    • Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
    • Farrand AJ, LaChapelle S, Hotze EM, Johnson AE, Tweten RK (2010) Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sci USA 107(9):4341-4346.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.9 , pp. 4341-4346
    • Farrand, A.J.1    Lachapelle, S.2    Hotze, E.M.3    Johnson, A.E.4    Tweten, R.K.5
  • 20
    • 0025779030 scopus 로고
    • Purification and immunogenicity of genetically obtained pneumolysin toxoids and their conjugation to Streptococcus pneumoniae type 19F polysaccharide
    • Paton JC, et al. (1991) Purification and immunogenicity of genetically obtained pneumolysin toxoids and their conjugation to Streptococcus pneumoniae type 19F polysaccharide. Infect Immun 59(7):2297-2304.
    • (1991) Infect Immun , vol.59 , Issue.7 , pp. 2297-2304
    • Paton, J.C.1
  • 21
    • 80855127655 scopus 로고    scopus 로고
    • Pneumolysin with low hemolytic activity confers an early growth advantage to Streptococcus pneumoniae in the blood
    • Harvey RM, Ogunniyi AD, Chen AY, Paton JC (2011) Pneumolysin with low hemolytic activity confers an early growth advantage to Streptococcus pneumoniae in the blood. Infect Immun 79(10):4122-4130.
    • (2011) Infect Immun , vol.79 , Issue.10 , pp. 4122-4130
    • Harvey, R.M.1    Ogunniyi, A.D.2    Chen, A.Y.3    Paton, J.C.4
  • 22
    • 0014661170 scopus 로고
    • Glycosphingolipids with Lewis blood group activity: Uptake by human erythrocytes
    • Marcus DM, Cass LE (1969) Glycosphingolipids with Lewis blood group activity: Uptake by human erythrocytes. Science 164 (3879):553-555.
    • (1969) Science , vol.164 , Issue.3879 , pp. 553-555
    • Marcus, D.M.1    Cass, L.E.2
  • 23
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22(2): 195-201.
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 24
    • 61449229355 scopus 로고    scopus 로고
    • Protein structure homology modeling using SWISS-MODEL workspace
    • Bordoli L, et al. (2009) Protein structure homology modeling using SWISS-MODEL workspace. Nat Protoc 4(1):1-13.
    • (2009) Nat Protoc , vol.4 , Issue.1 , pp. 1-13
    • Bordoli, L.1
  • 25
    • 84864371562 scopus 로고    scopus 로고
    • Prediction of carbohydrate binding sites on protein surfaces with 3-dimensional probability density distributions of interacting atoms
    • Tsai KC, et al. (2012) Prediction of carbohydrate binding sites on protein surfaces with 3-dimensional probability density distributions of interacting atoms. PLoS ONE 7(7): e40846.
    • (2012) PLoS ONE , vol.7 , Issue.7 , pp. e40846
    • Tsai, K.C.1
  • 26
    • 0025989653 scopus 로고
    • Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumo-niae
    • Boulnois GJ, Paton JC, Mitchell TJ, Andrew PW (1991) Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumo-niae. Mol Microbiol 5(11):2611-2616.
    • (1991) Mol Microbiol , vol.5 , Issue.11 , pp. 2611-2616
    • Boulnois, G.J.1    Paton, J.C.2    Mitchell, T.J.3    Andrew, P.W.4
  • 27
    • 22944433255 scopus 로고    scopus 로고
    • Three-dimensional structures of carbohydrate determinants of Lewis system antigens: Implications for effective antibody targeting of cancer
    • Yuriev E, Farrugia W, Scott AM, Ramsland PA (2005) Three-dimensional structures of carbohydrate determinants of Lewis system antigens: Implications for effective antibody targeting of cancer. Immunol Cell Biol 83(6):709-717.
    • (2005) Immunol Cell Biol , vol.83 , Issue.6 , pp. 709-717
    • Yuriev, E.1    Farrugia, W.2    Scott, A.M.3    Ramsland, P.A.4
  • 28
    • 0021611610 scopus 로고
    • Structure of sialylated fucosyl lactosaminoglycan isolated from human granulocytes
    • Fukuda M, Spooncer E, Oates JE, Dell A, Klock JC (1984) Structure of sialylated fucosyl lactosaminoglycan isolated from human granulocytes. J Biol Chem 259(17): 10925-10935.
    • (1984) J Biol Chem , vol.259 , Issue.17 , pp. 10925-10935
    • Fukuda, M.1    Spooncer, E.2    Oates, J.E.3    Dell, A.4    Klock, J.C.5
  • 29
    • 0021342469 scopus 로고
    • Isolation and characterization of polyfucosylated lactosaminoglycan from human granulocytes
    • Spooncer E, Fukuda M, Klock JC, Oates JE, Dell A (1984) Isolation and characterization of polyfucosylated lactosaminoglycan from human granulocytes. J Biol Chem 259(8): 4792-4801.
    • (1984) J Biol Chem , vol.259 , Issue.8 , pp. 4792-4801
    • Spooncer, E.1    Fukuda, M.2    Klock, J.C.3    Oates, J.E.4    Dell, A.5
  • 30
    • 0028784158 scopus 로고
    • Detection in human blood platelets of sialyl Lewis X gangliosides, potential ligands for CD62 and other selectins
    • Cooling LL, Zhang DS, Walker KE, Koerner TA (1995) Detection in human blood platelets of sialyl Lewis X gangliosides, potential ligands for CD62 and other selectins. Glycobiology 5(6):571-581.
    • (1995) Glycobiology , vol.5 , Issue.6 , pp. 571-581
    • Cooling, L.L.1    Zhang, D.S.2    Walker, K.E.3    Koerner, T.A.4
  • 31
    • 0024353042 scopus 로고
    • Sialyl SSEA-1 antigen as a carbohydrate marker of human natural killer cells and immature lymphoid cells
    • Ohmori K, et al. (1989) Sialyl SSEA-1 antigen as a carbohydrate marker of human natural killer cells and immature lymphoid cells. Blood 74(1):255-261.
    • (1989) Blood , vol.74 , Issue.1 , pp. 255-261
    • Ohmori, K.1
  • 32
    • 0024519822 scopus 로고
    • Adhesion molecules controlling lymphocyte migration
    • Stoolman LM (1989) Adhesion molecules controlling lymphocyte migration. Cell 56(6): 907-910.
    • (1989) Cell , vol.56 , Issue.6 , pp. 907-910
    • Stoolman, L.M.1
  • 33
    • 0027484929 scopus 로고
    • A distinct type of sialyl Lewis X antigen defined by a novel monoclonal antibody is selectively expressed on helper memory T cells
    • Ohmori K, et al. (1993) A distinct type of sialyl Lewis X antigen defined by a novel monoclonal antibody is selectively expressed on helper memory T cells. Blood 82(9): 2797-2805.
    • (1993) Blood , vol.82 , Issue.9 , pp. 2797-2805
    • Ohmori, K.1
  • 34
    • 0030748084 scopus 로고    scopus 로고
    • Selectin-carbohydrate interactions during inflammation and metastasis
    • McEver RP (1997) Selectin-carbohydrate interactions during inflammation and metastasis. Glycoconj J 14(5):585-591.
    • (1997) Glycoconj J , vol.14 , Issue.5 , pp. 585-591
    • McEver, R.P.1
  • 35
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • Lasky LA (1992) Selectins: Interpreters of cell-specific carbohydrate information during inflammation. Science 258 (5084):964-969.
    • (1992) Science , vol.258 , Issue.5084 , pp. 964-969
    • Lasky, L.A.1
  • 36
    • 0028041301 scopus 로고
    • Selectin ligands
    • Varki A (1994) Selectin ligands. Proc Natl Acad Sci USA 91(16):7390-7397.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.16 , pp. 7390-7397
    • Varki, A.1
  • 37
    • 0034671746 scopus 로고    scopus 로고
    • Binding of glyco-sulfopeptides to P-selectin requires stereospecific contributions of individual tyrosine sulfate and sugar residues
    • Leppänen A, White SP, Helin J, McEver RP, Cummings RD (2000) Binding of glyco-sulfopeptides to P-selectin requires stereospecific contributions of individual tyrosine sulfate and sugar residues. J Biol Chem 275(50):39569-39578.
    • (2000) J Biol Chem , vol.275 , Issue.50 , pp. 39569-39578
    • Leppänen, A.1    White, S.P.2    Helin, J.3    McEver, R.P.4    Cummings, R.D.5
  • 38
    • 1942542931 scopus 로고    scopus 로고
    • Ligands for L-selectin: Homing, inflammation, and beyond
    • Rosen SD (2004) Ligands for L-selectin: Homing, inflammation, and beyond. Annu Rev Immunol 22:129-156.
    • (2004) Annu Rev Immunol , vol.22 , pp. 129-156
    • Rosen, S.D.1
  • 39
    • 55749095702 scopus 로고    scopus 로고
    • E-selectin receptors on human leukocytes
    • Nimrichter L, et al. (2008) E-selectin receptors on human leukocytes. Blood 112(9): 3744-3752.
    • (2008) Blood , vol.112 , Issue.9 , pp. 3744-3752
    • Nimrichter, L.1
  • 40
    • 35348954771 scopus 로고    scopus 로고
    • Critical role of mac-1 sialyl lewis x moieties in regulating neutrophil degranulation and transmigration
    • Zen K, Cui LB, Zhang CY, Liu Y (2007) Critical role of mac-1 sialyl lewis x moieties in regulating neutrophil degranulation and transmigration. J Mol Biol 374(1):54-63.
    • (2007) J Mol Biol , vol.374 , Issue.1 , pp. 54-63
    • Zen, K.1    Cui, L.B.2    Zhang, C.Y.3    Liu, Y.4
  • 41
    • 13144275228 scopus 로고    scopus 로고
    • The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae
    • Rossjohn J, et al. (1998) The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae. J Mol Biol 284(2):449-461.
    • (1998) J Mol Biol , vol.284 , Issue.2 , pp. 449-461
    • Rossjohn, J.1
  • 42
    • 0017370479 scopus 로고
    • The reactions of antibodies to paragloboside (lacto-N-neotetraosyl ceramide) with human erythrocytes and lymphocytes
    • Schwarting GA, Marcus DM (1977) The reactions of antibodies to paragloboside (lacto-N-neotetraosyl ceramide) with human erythrocytes and lymphocytes. J Immunol 118(4): 1415-1419.
    • (1977) J Immunol , vol.118 , Issue.4 , pp. 1415-1419
    • Schwarting, G.A.1    Marcus, D.M.2
  • 43
    • 84911972981 scopus 로고    scopus 로고
    • A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O
    • Mozola CC, Magassa N, Caparon MG (2014) A novel cholesterol-insensitive mode of membrane binding promotes cytolysin-mediated translocation by Streptolysin O. Mol Microbiol 94(3):675-687.
    • (2014) Mol Microbiol , vol.94 , Issue.3 , pp. 675-687
    • Mozola, C.C.1    Magassa, N.2    Caparon, M.G.3
  • 44
    • 84907088572 scopus 로고    scopus 로고
    • A galactose-binding lectin isolated from Aplysia kurodai (sea hare) eggs inhibits streptolysin-induced hemolysis
    • Hasan I, et al. (2014) A galactose-binding lectin isolated from Aplysia kurodai (sea hare) eggs inhibits streptolysin-induced hemolysis. Molecules 19(9):13990-14003.
    • (2014) Molecules , vol.19 , Issue.9 , pp. 13990-14003
    • Hasan, I.1
  • 45
    • 84856741481 scopus 로고    scopus 로고
    • Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity
    • Feil SC, et al. (2012) Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity. Structure 20(2):248-258.
    • (2012) Structure , vol.20 , Issue.2 , pp. 248-258
    • Feil, S.C.1
  • 46
    • 84905659601 scopus 로고    scopus 로고
    • The impact of pneumolysin on the macrophage response to Streptococcus pneumoniae is strain-dependent
    • Harvey RM, et al. (2014) The impact of pneumolysin on the macrophage response to Streptococcus pneumoniae is strain-dependent. PLoS ONE 9(8):e103625.
    • (2014) PLoS ONE , vol.9 , Issue.8 , pp. e103625
    • Harvey, R.M.1
  • 48
    • 59449086954 scopus 로고    scopus 로고
    • Streptolysin O promotes group A Streptococcus immune evasion by accelerated macrophage apoptosis
    • Timmer AM, et al. (2009) Streptolysin O promotes group A Streptococcus immune evasion by accelerated macrophage apoptosis. J Biol Chem 284(2):862-871.
    • (2009) J Biol Chem , vol.284 , Issue.2 , pp. 862-871
    • Timmer, A.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.