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Volumn 72, Issue , 2017, Pages 101-116

Staphylococcus aureus pore-forming toxins: The interface of pathogen and host complexity

Author keywords

Alpha toxin; Hemolysin; Leukocidin; Pore forming toxins; S. aureus vaccines and therapeutics; Staphylococcus aureus

Indexed keywords

ADAM10 ENDOPEPTIDASE; BACTERIAL TOXIN; BETA CYCLODEXTRIN DERIVATIVE; CAVEOLIN; CD11B ANTIGEN; CELL SURFACE RECEPTOR; CHEMOKINE RECEPTOR CCR1; CHEMOKINE RECEPTOR CCR2; CHEMOKINE RECEPTOR CCR5; PANTON VALENTINE LEUKOCIDIN; BACTERIAL PROTEIN; LEUKOCIDIN;

EID: 85018405739     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2017.04.003     Document Type: Review
Times cited : (161)

References (209)
  • 1
    • 0042879872 scopus 로고    scopus 로고
    • Molecular features of the cytolytic pore-forming bacterial protein toxins
    • Alouf, J.E., Molecular features of the cytolytic pore-forming bacterial protein toxins. Folia Microbiol. (Praha) 48:1 (2003), 5–16.
    • (2003) Folia Microbiol. (Praha) , vol.48 , Issue.1 , pp. 5-16
    • Alouf, J.E.1
  • 2
    • 84866418820 scopus 로고    scopus 로고
    • Pathogenic pore-forming proteins: function and host response
    • Bischofberger, M., Iacovache, I., van der Goot, F.G., Pathogenic pore-forming proteins: function and host response. Cell Host Microbe 12:3 (2012), 266–275.
    • (2012) Cell Host Microbe , vol.12 , Issue.3 , pp. 266-275
    • Bischofberger, M.1    Iacovache, I.2    van der Goot, F.G.3
  • 3
    • 84955193035 scopus 로고    scopus 로고
    • Pore-forming toxins: ancient, but never really out of fashion
    • Dal Peraro, M., van der Goot, F.G., Pore-forming toxins: ancient, but never really out of fashion. Nat. Rev. Microbiol. 14:2 (2016), 77–92.
    • (2016) Nat. Rev. Microbiol. , vol.14 , Issue.2 , pp. 77-92
    • Dal Peraro, M.1    van der Goot, F.G.2
  • 4
    • 84879131303 scopus 로고    scopus 로고
    • Staphylococcus aureus α-toxin: nearly a century of intrigue
    • Berube, B., Wardenburg, J., Staphylococcus aureus α-toxin: nearly a century of intrigue. Toxins 5:6 (2013), 1140–1166.
    • (2013) Toxins , vol.5 , Issue.6 , pp. 1140-1166
    • Berube, B.1    Wardenburg, J.2
  • 5
    • 84893778159 scopus 로고    scopus 로고
    • Staphylococcus aureus: a pathogen with still unresolved issues
    • Rasigade, J.P., Vandenesch, F., Staphylococcus aureus: a pathogen with still unresolved issues. Infect. Genet. Evol. 21 (2014), 510–514.
    • (2014) Infect. Genet. Evol. , vol.21 , pp. 510-514
    • Rasigade, J.P.1    Vandenesch, F.2
  • 6
    • 84930239306 scopus 로고    scopus 로고
    • Staphylococcus aureus infections: epidemiology, pathophysiology, clinical manifestations, and management
    • Tong, S.Y., Davis, J.S., Eichenberger, E., Holland, T.L., Fowler, V.G. Jr., Staphylococcus aureus infections: epidemiology, pathophysiology, clinical manifestations, and management. Clin. Microbiol. Rev. 28:3 (2015), 603–661.
    • (2015) Clin. Microbiol. Rev. , vol.28 , Issue.3 , pp. 603-661
    • Tong, S.Y.1    Davis, J.S.2    Eichenberger, E.3    Holland, T.L.4    Fowler, V.G.5
  • 7
    • 84901058157 scopus 로고    scopus 로고
    • The bicomponent pore-forming leucocidins of Staphylococcus aureus
    • Alonzo, F. 3rd, Torres, V.J., The bicomponent pore-forming leucocidins of Staphylococcus aureus. Microbiol. Mol. Biol. Rev. 78:2 (2014), 199–230.
    • (2014) Microbiol. Mol. Biol. Rev. , vol.78 , Issue.2 , pp. 199-230
    • Alonzo, F.1    Torres, V.J.2
  • 8
    • 80053971276 scopus 로고    scopus 로고
    • A Staphylococcus aureus pore-forming toxin subverts the activity of ADAM10 to cause lethal infection in mice
    • Inoshima, I., Inoshima, N., Wilke, G.A., Powers, M.E., Frank, K.M., Wang, Y., Bubeck Wardenburg, J., A Staphylococcus aureus pore-forming toxin subverts the activity of ADAM10 to cause lethal infection in mice. Nat. Med. 17:10 (2011), 1310–1314.
    • (2011) Nat. Med. , vol.17 , Issue.10 , pp. 1310-1314
    • Inoshima, I.1    Inoshima, N.2    Wilke, G.A.3    Powers, M.E.4    Frank, K.M.5    Wang, Y.6    Bubeck Wardenburg, J.7
  • 10
    • 84855808422 scopus 로고    scopus 로고
    • Staphylococcus aureus leucocidin ED contributes to systemic infection by targeting neutrophils and promoting bacterial growth in vivo
    • Alonzo, F. 3rd, Benson, M.A., Chen, J., Novick, R.P., Shopsin, B., Torres, V.J., Staphylococcus aureus leucocidin ED contributes to systemic infection by targeting neutrophils and promoting bacterial growth in vivo. Mol. Microbiol. 83:2 (2012), 423–435.
    • (2012) Mol. Microbiol. , vol.83 , Issue.2 , pp. 423-435
    • Alonzo, F.1    Benson, M.A.2    Chen, J.3    Novick, R.P.4    Shopsin, B.5    Torres, V.J.6
  • 13
  • 16
    • 84892955809 scopus 로고
    • The exotoxins of Staphylococcus pyogenes aureus
    • Burnet, F.M., The exotoxins of Staphylococcus pyogenes aureus. J. Pathol. Bacteriol. 32 (1929), 717–734.
    • (1929) J. Pathol. Bacteriol. , vol.32 , pp. 717-734
    • Burnet, F.M.1
  • 17
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus aureus
    • Bhakdi, S., Tranum-Jensen, J., Alpha-toxin of Staphylococcus aureus. Microbiol. Rev. 55:4 (1991), 733–751.
    • (1991) Microbiol. Rev. , vol.55 , Issue.4 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 18
    • 0001135703 scopus 로고
    • Staphylococcal toxins and antitoxins
    • Glenny, A.T., Stevens, M.F., Staphylococcal toxins and antitoxins. J. Pathol. Bacteriol. 90:2 (1935), 201–210.
    • (1935) J. Pathol. Bacteriol. , vol.90 , Issue.2 , pp. 201-210
    • Glenny, A.T.1    Stevens, M.F.2
  • 19
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M.R., Shustak, C., Cheley, S., Bayley, H., Gouaux, J.E., Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274:5294 (1996), 1859–1865.
    • (1996) Science , vol.274 , Issue.5294 , pp. 1859-1865
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 20
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: a heptameric transmembrane pore
    • Gouaux, J.E.O., Braha, M.R., Hobaugh, L., Song, S., Cheley, C., Shustak Bayley, H., Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl. Acad. Sci. U. S. A. 91:26 (1994), 12828–12831.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , Issue.26 , pp. 12828-12831
    • Gouaux, J.E.O.1    Braha, M.R.2    Hobaugh, L.3    Song, S.4    Cheley, C.5    Shustak Bayley, H.6
  • 21
    • 48749105757 scopus 로고    scopus 로고
    • Comparison of virulence in community-associated methicillin-resistant Staphylococcus aureus pulsotypes USA300 and USA400 in a rat model of pneumonia
    • Montgomery, C.P., Boyle-Vavra, S., Adem, P.V., Lee, J.C., Husain, A.N., Clasen, J., Daum, R.S., Comparison of virulence in community-associated methicillin-resistant Staphylococcus aureus pulsotypes USA300 and USA400 in a rat model of pneumonia. J. Infect. Dis. 198:4 (2008), 561–570.
    • (2008) J. Infect. Dis. , vol.198 , Issue.4 , pp. 561-570
    • Montgomery, C.P.1    Boyle-Vavra, S.2    Adem, P.V.3    Lee, J.C.4    Husain, A.N.5    Clasen, J.6    Daum, R.S.7
  • 23
    • 36849064891 scopus 로고    scopus 로고
    • Poring over pores: α-hemolysin and Panton-Valentine leukocidin in Staphylococcus aureus pneumonia
    • Bubeck Wardenburg, J.T., Bae, M., Otto, F.R., Deleo Schneewind, O., Poring over pores: α-hemolysin and Panton-Valentine leukocidin in Staphylococcus aureus pneumonia. Nat. Med. 13:12 (2007), 1405–1406.
    • (2007) Nat. Med. , vol.13 , Issue.12 , pp. 1405-1406
    • Bubeck Wardenburg, J.T.1    Bae, M.2    Otto, F.R.3    Deleo Schneewind, O.4
  • 24
    • 84904479787 scopus 로고    scopus 로고
    • Insights into alpha-hemolysin (Hla) evolution and expression among Staphylococcus aureus clones with hospital and community origin
    • Tavares, A., Nielsen, J.B., Boye, K., Rohde, S., Paulo, A.C., Westh, H., Schonning, K., de Lencastre, H., Miragaia, M., Insights into alpha-hemolysin (Hla) evolution and expression among Staphylococcus aureus clones with hospital and community origin. PLoS One, 9(7), 2014, e98634.
    • (2014) PLoS One , vol.9 , Issue.7 , pp. e98634
    • Tavares, A.1    Nielsen, J.B.2    Boye, K.3    Rohde, S.4    Paulo, A.C.5    Westh, H.6    Schonning, K.7    de Lencastre, H.8    Miragaia, M.9
  • 26
    • 0027180031 scopus 로고
    • Synthesis of staphylococcal virulence factors is controlled by a regulatory RNA molecule
    • Novick, R.P., Ross, H.F., Projan, S.J., Kornblum, J., Kreiswirth, B.N., Moghazeh, S., Synthesis of staphylococcal virulence factors is controlled by a regulatory RNA molecule. EMBO J. 12:10 (1993), 3967–3975.
    • (1993) EMBO J. , vol.12 , Issue.10 , pp. 3967-3975
    • Novick, R.P.1    Ross, H.F.2    Projan, S.J.3    Kornblum, J.4    Kreiswirth, B.N.5    Moghazeh, S.6
  • 27
    • 0026638833 scopus 로고
    • Regulation of exoprotein expression in Staphylococcus aureus by a locus (sar) distinct from agr
    • Cheung, A.L., Koomey, J.M., Butler, C.A., Projan, S.J., Fischetti, V.A., Regulation of exoprotein expression in Staphylococcus aureus by a locus (sar) distinct from agr. Proc. Natl. Acad. Sci. U. S. A. 89:14 (1992), 6462–6466.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , Issue.14 , pp. 6462-6466
    • Cheung, A.L.1    Koomey, J.M.2    Butler, C.A.3    Projan, S.J.4    Fischetti, V.A.5
  • 28
    • 0031739401 scopus 로고    scopus 로고
    • SarA level is a determinant of agr activation in Staphylococcus aureus
    • Chien, Y., Manna, A., Cheung, A.L., SarA level is a determinant of agr activation in Staphylococcus aureus. Mol. Microbiol. 30:5 (1998), 991–1001.
    • (1998) Mol. Microbiol. , vol.30 , Issue.5 , pp. 991-1001
    • Chien, Y.1    Manna, A.2    Cheung, A.L.3
  • 29
    • 0030850117 scopus 로고    scopus 로고
    • The sae locus of Staphylococcus aureus controls exoprotein synthesis at the transcriptional level
    • Giraudo, A.T., Cheung, A.L., Nagel, R., The sae locus of Staphylococcus aureus controls exoprotein synthesis at the transcriptional level. Arch. Microbiol. 168 (1997), 53–58.
    • (1997) Arch. Microbiol. , vol.168 , pp. 53-58
    • Giraudo, A.T.1    Cheung, A.L.2    Nagel, R.3
  • 30
    • 0142106391 scopus 로고    scopus 로고
    • The staphylococcal saeRS system coordinates environmental signals with agr quorum sensing
    • Novick, R.P., Jiang, D., The staphylococcal saeRS system coordinates environmental signals with agr quorum sensing. Microbiology 149:Pt. 10 (2003), 2709–2717.
    • (2003) Microbiology , vol.149 , pp. 2709-2717
    • Novick, R.P.1    Jiang, D.2
  • 31
    • 78649918595 scopus 로고    scopus 로고
    • Importance of the global regulators Agr and SaeRS in the pathogenesis of CA-MRSA USA300 infection
    • Montgomery, C.P., Boyle-Vavra, S., Daum, R.S., Importance of the global regulators Agr and SaeRS in the pathogenesis of CA-MRSA USA300 infection. PLoS One, 5(12), 2010, e15177.
    • (2010) PLoS One , vol.5 , Issue.12 , pp. e15177
    • Montgomery, C.P.1    Boyle-Vavra, S.2    Daum, R.S.3
  • 32
    • 84863922855 scopus 로고    scopus 로고
    • ADAM10 mediates vascular injury induced by Staphylococcus aureus α-hemolysin
    • Powers, M.E., Kim, H.K., Wang, Y., Bubeck Wardenburg, J., ADAM10 mediates vascular injury induced by Staphylococcus aureus α-hemolysin. J. Infect. Dis. 206:3 (2012), 352–356.
    • (2012) J. Infect. Dis. , vol.206 , Issue.3 , pp. 352-356
    • Powers, M.E.1    Kim, H.K.2    Wang, Y.3    Bubeck Wardenburg, J.4
  • 33
    • 0023518575 scopus 로고
    • Virulence of protein A-deficient and alpha-toxin-deficient mutants of Staphylococcus aureus isolated by allele replacement
    • Patel, A.H., Nowlan, P., Weavers, E.D., Foster, T., Virulence of protein A-deficient and alpha-toxin-deficient mutants of Staphylococcus aureus isolated by allele replacement. Infect. Immun. 55:12 (1987), 3103–3110.
    • (1987) Infect. Immun. , vol.55 , Issue.12 , pp. 3103-3110
    • Patel, A.H.1    Nowlan, P.2    Weavers, E.D.3    Foster, T.4
  • 35
    • 84862804469 scopus 로고    scopus 로고
    • Genetic requirement for ADAM10 in severe Staphylococcus aureus skin infection
    • Inoshima, N., Wang, Y., Bubeck Wardenburg, J., Genetic requirement for ADAM10 in severe Staphylococcus aureus skin infection. J. Invest. Dermatol. 132:5 (2012), 1513–1516.
    • (2012) J. Invest. Dermatol. , vol.132 , Issue.5 , pp. 1513-1516
    • Inoshima, N.1    Wang, Y.2    Bubeck Wardenburg, J.3
  • 36
    • 0024341103 scopus 로고
    • Roles of alpha-toxin and beta-toxin in virulence of Staphylococcus aureus for the mouse mammary gland
    • Bramley, A.J., Patel, A.H., O'Reilly, M., Foster, R., Foster, T.J., Roles of alpha-toxin and beta-toxin in virulence of Staphylococcus aureus for the mouse mammary gland. Infect. Immun. 57:8 (1989), 2489–2494.
    • (1989) Infect. Immun. , vol.57 , Issue.8 , pp. 2489-2494
    • Bramley, A.J.1    Patel, A.H.2    O'Reilly, M.3    Foster, R.4    Foster, T.J.5
  • 38
    • 0032858909 scopus 로고    scopus 로고
    • Alpha-toxin damages the air-blood barrier of the lung in a rat model of Staphylococcus aureus-induced pneumonia
    • McElroy, M.C., Harty, H.R., Hosford, G.E., Boylan, G.M., Pittet, J.F., Foster, T.J., Alpha-toxin damages the air-blood barrier of the lung in a rat model of Staphylococcus aureus-induced pneumonia. Infect. Immun. 67:10 (1999), 5541–5544.
    • (1999) Infect. Immun. , vol.67 , Issue.10 , pp. 5541-5544
    • McElroy, M.C.1    Harty, H.R.2    Hosford, G.E.3    Boylan, G.M.4    Pittet, J.F.5    Foster, T.J.6
  • 39
    • 33846814907 scopus 로고    scopus 로고
    • Surface proteins and exotoxins are required for the pathogenesis of Staphylococcus aureus pneumonia
    • Bubeck Wardenburg, J., Patel, R.J., Schneewind, O., Surface proteins and exotoxins are required for the pathogenesis of Staphylococcus aureus pneumonia. Infect. Immun. 75:2 (2007), 1040–1044.
    • (2007) Infect. Immun. , vol.75 , Issue.2 , pp. 1040-1044
    • Bubeck Wardenburg, J.1    Patel, R.J.2    Schneewind, O.3
  • 40
    • 0001049555 scopus 로고
    • Étude sur le mecanisme de la virulence du Staphylocoque pyogene
    • van de Velde, H., Étude sur le mecanisme de la virulence du Staphylocoque pyogene. Cellule 10 (1894), 401–410.
    • (1894) Cellule , vol.10 , pp. 401-410
    • van de Velde, H.1
  • 41
    • 84886774286 scopus 로고
    • Studies of hemolytic staphylococci: hemolyticactivity— biochemical reactions—serologic reactions
    • Julianelle, L.A., Studies of hemolytic staphylococci: hemolyticactivity— biochemical reactions—serologic reactions. J. Infect. Dis. 31 (1922), 256–284.
    • (1922) J. Infect. Dis. , vol.31 , pp. 256-284
    • Julianelle, L.A.1
  • 42
    • 50249218564 scopus 로고
    • Staphylococcal toxin
    • Panton, P.N., Valentine, F.C.O., Staphylococcal toxin. Lancet 1:5662 (1932), 506–508.
    • (1932) Lancet , vol.1 , Issue.5662 , pp. 506-508
    • Panton, P.N.1    Valentine, F.C.O.2
  • 43
    • 84874768319 scopus 로고    scopus 로고
    • Bacterial survival amidst an immune onslaught: the contribution of the Staphylococcus aureus leukotoxins
    • Alonzo, F. 3rd, Torres, V.J., Bacterial survival amidst an immune onslaught: the contribution of the Staphylococcus aureus leukotoxins. PLoS Pathog., 9(2), 2013, e1003143.
    • (2013) PLoS Pathog. , vol.9 , Issue.2 , pp. e1003143
    • Alonzo, F.1    Torres, V.J.2
  • 44
    • 84886079502 scopus 로고    scopus 로고
    • Staphylococcus aureus leukotoxin ED targets the chemokine receptors CXCR1 and CXCR2 to kill leukocytes and promote infection
    • Reyes-Robles, T., Alonzo, F. 3rd, Kozhaya, L., Lacy, D.B., Unutmaz, D., Torres, V.J., Staphylococcus aureus leukotoxin ED targets the chemokine receptors CXCR1 and CXCR2 to kill leukocytes and promote infection. Cell Host Microbe 14:4 (2013), 453–459.
    • (2013) Cell Host Microbe , vol.14 , Issue.4 , pp. 453-459
    • Reyes-Robles, T.1    Alonzo, F.2    Kozhaya, L.3    Lacy, D.B.4    Unutmaz, D.5    Torres, V.J.6
  • 45
    • 84879518407 scopus 로고    scopus 로고
    • Staphylococcus aureus LukAB cytotoxin kills human neutrophils by targeting the CD11b subunit of the integrin Mac-1
    • DuMont, A.L., Yoong, P., Day, C.J., Alonzo, F. 3rd, McDonald, W.H., Jennings, M.P., Torres, V.J., Staphylococcus aureus LukAB cytotoxin kills human neutrophils by targeting the CD11b subunit of the integrin Mac-1. Proc. Natl. Acad. Sci. U. S. A. 110:26 (2013), 10794–10799.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , Issue.26 , pp. 10794-10799
    • DuMont, A.L.1    Yoong, P.2    Day, C.J.3    Alonzo, F.4    McDonald, W.H.5    Jennings, M.P.6    Torres, V.J.7
  • 46
    • 0027459158 scopus 로고
    • The gamma-hemolysin locus of Staphylococcus aureus comprises three linked genes, two of which are identical to the genes for the F and S components of leukocidin
    • Cooney, J.Z., Kienle, T.J., Foster O'Toole, P.W., The gamma-hemolysin locus of Staphylococcus aureus comprises three linked genes, two of which are identical to the genes for the F and S components of leukocidin. Infect. Immun. 61:2 (1993), 768–771.
    • (1993) Infect. Immun. , vol.61 , Issue.2 , pp. 768-771
    • Cooney, J.Z.1    Kienle, T.J.2    Foster O'Toole, P.W.3
  • 47
    • 0005569278 scopus 로고
    • Fractionation of a leucocidin from Staphylococcus aureus
    • Woodin, A.M., Fractionation of a leucocidin from Staphylococcus aureus. Biochem. J. 73:225–237 (1959), 225–237.
    • (1959) Biochem. J. , vol.73 , Issue.225-237 , pp. 225-237
    • Woodin, A.M.1
  • 48
    • 0033125070 scopus 로고    scopus 로고
    • Assembly of Staphylococcus aureus leukocidin into a pore-forming ring-shaped oligomer on human polymorphonuclear leukocytes and rabbit erythrocytes
    • Sugawara, N., Tomita, T., Sato, T., Kamio, Y., Assembly of Staphylococcus aureus leukocidin into a pore-forming ring-shaped oligomer on human polymorphonuclear leukocytes and rabbit erythrocytes. Biosci. Biotechnol. Biochem. 63:5 (1999), 884–891.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , Issue.5 , pp. 884-891
    • Sugawara, N.1    Tomita, T.2    Sato, T.3    Kamio, Y.4
  • 49
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • Olson, R., Nariya, H., Yokota, K., Kamio, Y., Gouaux, E., Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat. Struct. Biol. 6:2 (1999), 134–140.
    • (1999) Nat. Struct. Biol. , vol.6 , Issue.2 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 50
    • 0036716731 scopus 로고    scopus 로고
    • Stochastic assembly of two-component staphylococcal γ-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3
    • Sugawara-Tomita, N.T., Tomita Kamio, Y., Stochastic assembly of two-component staphylococcal γ-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3. J. Bacteriol. 184:17 (2002), 4747–4756.
    • (2002) J. Bacteriol. , vol.184 , Issue.17 , pp. 4747-4756
    • Sugawara-Tomita, N.T.1    Tomita Kamio, Y.2
  • 51
    • 0036128759 scopus 로고    scopus 로고
    • Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore
    • Miles, G., Movileanu, L., Bayley, H., Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore. Protein Sci. 11:4 (2002), 894–902.
    • (2002) Protein Sci. , vol.11 , Issue.4 , pp. 894-902
    • Miles, G.1    Movileanu, L.2    Bayley, H.3
  • 54
    • 0031148369 scopus 로고    scopus 로고
    • Sequential binding of Staphylococcal γ-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface
    • Kaneko, J.T., Ozawa, T., Tomita Kamio, Y., Sequential binding of Staphylococcal γ-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface. Biosci. Biotechnol. Biochem. 61:5 (1997), 846–851.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , Issue.5 , pp. 846-851
    • Kaneko, J.T.1    Ozawa, T.2    Tomita Kamio, Y.3
  • 56
    • 77955399259 scopus 로고    scopus 로고
    • Identification of a novel Staphylococcus aureus two-component leukotoxin using cell surface proteomics
    • Ventura, C.L., Malachowa, N., Hammer, C.H., Nardone, G.A., Robinson, M.A., Kobayashi, S.D., DeLeo, F.R., Identification of a novel Staphylococcus aureus two-component leukotoxin using cell surface proteomics. PLoS One, 5(7), 2010, e11634.
    • (2010) PLoS One , vol.5 , Issue.7 , pp. e11634
    • Ventura, C.L.1    Malachowa, N.2    Hammer, C.H.3    Nardone, G.A.4    Robinson, M.A.5    Kobayashi, S.D.6    DeLeo, F.R.7
  • 57
    • 0031266137 scopus 로고    scopus 로고
    • Panton-valentine leukocidin genes in a phage-like particle isolated from mitomycin C-treated Staphylococcus aureus V8 (ATCC 49775)
    • Kaneko, J., Kimura, T., Kawakami, Y., Tomita, T., Kamio, Y., Panton-valentine leukocidin genes in a phage-like particle isolated from mitomycin C-treated Staphylococcus aureus V8 (ATCC 49775). Biosci. Biotechnol. Biochem. 61:11 (1997), 1960–1962.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , Issue.11 , pp. 1960-1962
    • Kaneko, J.1    Kimura, T.2    Kawakami, Y.3    Tomita, T.4    Kamio, Y.5
  • 58
    • 0032541129 scopus 로고    scopus 로고
    • Complete nucleotide sequence and molecular characterization of the temperate staphylococcal bacteriophage φPVL carrying Panton-Valentine leukocidin genes
    • Kaneko, J.T., Kimura, S., Narita, T., Tomita Kamio, Y., Complete nucleotide sequence and molecular characterization of the temperate staphylococcal bacteriophage φPVL carrying Panton-Valentine leukocidin genes. Gene 215:1 (1998), 57–67.
    • (1998) Gene , vol.215 , Issue.1 , pp. 57-67
    • Kaneko, J.T.1    Kimura, S.2    Narita, T.3    Tomita Kamio, Y.4
  • 60
    • 79951481523 scopus 로고    scopus 로고
    • Distinct bacteriophages encoding Panton-Valentine leukocidin (PVL) among international methicillin-resistant Staphylococcus aureus clones harboring PVL
    • Boakes, E., Kearns, A.M., Ganner, M., Perry, C., Hill, R.L., Ellington, M.J., Distinct bacteriophages encoding Panton-Valentine leukocidin (PVL) among international methicillin-resistant Staphylococcus aureus clones harboring PVL. J. Clin. Microbiol. 49:2 (2011), 684–692.
    • (2011) J. Clin. Microbiol. , vol.49 , Issue.2 , pp. 684-692
    • Boakes, E.1    Kearns, A.M.2    Ganner, M.3    Perry, C.4    Hill, R.L.5    Ellington, M.J.6
  • 65
    • 84871055980 scopus 로고    scopus 로고
    • The role of the Panton-Valentine leucocidin toxin in staphylococcal disease: a systematic review and meta-analysis
    • Shallcross, L.J., Fragaszy, E., Johnson, A.M., Hayward, A.C., The role of the Panton-Valentine leucocidin toxin in staphylococcal disease: a systematic review and meta-analysis. Lancet Inf. Dis. 13:1 (2013), 43–54.
    • (2013) Lancet Inf. Dis. , vol.13 , Issue.1 , pp. 43-54
    • Shallcross, L.J.1    Fragaszy, E.2    Johnson, A.M.3    Hayward, A.C.4
  • 66
    • 0033496604 scopus 로고    scopus 로고
    • Involvement of Panton-Valentine leukocidin-producing Staphylococcus aureus in primary skin infections and pneumonia
    • Lina, G., Piemont, Y., Godail-Gamot, F., Bes, M., Peter, M.O., Gauduchon, V., Vandenesch, F., Etienne, J., Involvement of Panton-Valentine leukocidin-producing Staphylococcus aureus in primary skin infections and pneumonia. Clin. Infect. Dis. 29:5 (1999), 1128–1132.
    • (1999) Clin. Infect. Dis. , vol.29 , Issue.5 , pp. 1128-1132
    • Lina, G.1    Piemont, Y.2    Godail-Gamot, F.3    Bes, M.4    Peter, M.O.5    Gauduchon, V.6    Vandenesch, F.7    Etienne, J.8
  • 67
    • 0037006653 scopus 로고    scopus 로고
    • Association between Staphylococcus aureus strains carrying gene for Panton-Valentine leukocidin and highly lethal necrotising pneumonia in young immunocompetent patients
    • Gillet, Y., Issartel, B., Vanhems, P., Fournet, J.-C., Lina, G., Bes, M., Vandenesch, F., Piémont, Y., Brousse, N., Floret, D., Etienne, J., Association between Staphylococcus aureus strains carrying gene for Panton-Valentine leukocidin and highly lethal necrotising pneumonia in young immunocompetent patients. Lancet 359:9308 (2002), 753–759.
    • (2002) Lancet , vol.359 , Issue.9308 , pp. 753-759
    • Gillet, Y.1    Issartel, B.2    Vanhems, P.3    Fournet, J.-C.4    Lina, G.5    Bes, M.6    Vandenesch, F.7    Piémont, Y.8    Brousse, N.9    Floret, D.10    Etienne, J.11
  • 68
    • 0027427479 scopus 로고
    • Pore formation by a two-component leukocidin from Staphylococcus aureus within the membrane of human polymorphonuclear leukocytes
    • Finck-Barbacon, V., Duportail, G., Meunier, O., Colin, D.A., Pore formation by a two-component leukocidin from Staphylococcus aureus within the membrane of human polymorphonuclear leukocytes. Biochim. Biophys. Acta 1182:1993 (1993), 275–282.
    • (1993) Biochim. Biophys. Acta , vol.1182 , Issue.1993 , pp. 275-282
    • Finck-Barbacon, V.1    Duportail, G.2    Meunier, O.3    Colin, D.A.4
  • 71
    • 54749153168 scopus 로고    scopus 로고
    • Panton-Valentine leukocidin is not a virulence determinant in murine models of community-associated methicillin-resistant Staphylococcus aureus disease
    • Bubeck Wardenburg, J., Palazzolo-Ballance, A.M., Otto, M., Schneewind, O., DeLeo, F.R., Panton-Valentine leukocidin is not a virulence determinant in murine models of community-associated methicillin-resistant Staphylococcus aureus disease. J. Infect. Dis. 198:8 (2008), 1166–1170.
    • (2008) J. Infect. Dis. , vol.198 , Issue.8 , pp. 1166-1170
    • Bubeck Wardenburg, J.1    Palazzolo-Ballance, A.M.2    Otto, M.3    Schneewind, O.4    DeLeo, F.R.5
  • 73
    • 84864823086 scopus 로고    scopus 로고
    • Immune-activating properties of Panton-Valentine leukocidin improve the outcome in a model of methicillin-resistant Staphylococcus aureus pneumonia
    • Yoong, P., Pier, G.B., Immune-activating properties of Panton-Valentine leukocidin improve the outcome in a model of methicillin-resistant Staphylococcus aureus pneumonia. Infect. Immun. 80:8 (2012), 2894–2904.
    • (2012) Infect. Immun. , vol.80 , Issue.8 , pp. 2894-2904
    • Yoong, P.1    Pier, G.B.2
  • 78
    • 0029149555 scopus 로고
    • Panton-Valentine leucocidin and gamma-hemolysin from Staphylococcus aureus ATCC 49775 are encoded by distinct genetic loci and have different biological activities
    • Prevost, G., Cribier, B., Couppie, P., Petiau, P., Supersac, G., Finck-Barbacon, V., Monteil, H., Piemont, Y., 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), 1995.
    • (1995) Infect. Immun. , vol.63 , Issue.10
    • Prevost, G.1    Cribier, B.2    Couppie, P.3    Petiau, P.4    Supersac, G.5    Finck-Barbacon, V.6    Monteil, H.7    Piemont, Y.8
  • 79
    • 80051769392 scopus 로고
    • Separation of gamma hemolysin from Staphylococcus aureus Smith 5R
    • Mollby, R., Wadstrom, T., Separation of gamma hemolysin from Staphylococcus aureus Smith 5R. Infect. Immun. 3:4 (1971), 633–635.
    • (1971) Infect. Immun. , vol.3 , Issue.4 , pp. 633-635
    • Mollby, R.1    Wadstrom, T.2
  • 80
    • 0017264247 scopus 로고
    • Production and purification of the gamma haemolysin of Staphylococcus aureus ‘Smith 5R’
    • Fackrell, H.B., Wiseman, G.M., Production and purification of the gamma haemolysin of Staphylococcus aureus ‘Smith 5R’. J. Gen. Microbiol. 92:1 (1976), 1–10.
    • (1976) J. Gen. Microbiol. , vol.92 , Issue.1 , pp. 1-10
    • Fackrell, H.B.1    Wiseman, G.M.2
  • 81
    • 0017252176 scopus 로고
    • Properties of the gamma haemolysin of Staphylococcus aureus ‘Smith 5R’
    • Fackrell, H.B., Wiseman, G.M., Properties of the gamma haemolysin of Staphylococcus aureus ‘Smith 5R’. J. Gen. Microbiol. 92:1 (1976), 11–24.
    • (1976) J. Gen. Microbiol. , vol.92 , Issue.1 , pp. 11-24
    • Fackrell, H.B.1    Wiseman, G.M.2
  • 82
    • 0027510074 scopus 로고
    • Sequencing of leucocidin R from Staphylococcus aureus P83 suggests that staphylococcal leucocidins and gamma-hemolysin are members of a single, two-component family of toxins
    • Supersac, G.G., Prevost Piemont, Y., Sequencing of leucocidin R from Staphylococcus aureus P83 suggests that staphylococcal leucocidins and gamma-hemolysin are members of a single, two-component family of toxins. Infect. Immun. 61:2 (1993), 580–587.
    • (1993) Infect. Immun. , vol.61 , Issue.2 , pp. 580-587
    • Supersac, G.G.1    Prevost Piemont, Y.2
  • 83
    • 0019130154 scopus 로고
    • Crystallization and properties of staphylococcal leukocidin
    • Noda, M., Hirayama, T., Kato, I., Matsuda, F., Crystallization and properties of staphylococcal leukocidin. Biochim. Biophys. Acta 633:1 (1980), 33–44.
    • (1980) Biochim. Biophys. Acta , vol.633 , Issue.1 , pp. 33-44
    • Noda, M.1    Hirayama, T.2    Kato, I.3    Matsuda, F.4
  • 84
    • 14944373762 scopus 로고    scopus 로고
    • Cytotoxin and pyrogenic toxin superantigen gene profiles of Staphylococcus aureus associated with subclinical mastitis in dairy cows and relationships with macrorestriction genomic profiles
    • Fueyo, J.M., Mendoza, M.C., Rodicio, M.R., Muniz, J., Alvarez, M.A., Martin, M.C., Cytotoxin and pyrogenic toxin superantigen gene profiles of Staphylococcus aureus associated with subclinical mastitis in dairy cows and relationships with macrorestriction genomic profiles. J. Clin. Microbiol. 43:3 (2005), 1278–1284.
    • (2005) J. Clin. Microbiol. , vol.43 , Issue.3 , pp. 1278-1284
    • Fueyo, J.M.1    Mendoza, M.C.2    Rodicio, M.R.3    Muniz, J.4    Alvarez, M.A.5    Martin, M.C.6
  • 85
    • 0033053177 scopus 로고    scopus 로고
    • Alpha-toxin and gamma-toxin jointly promote Staphylococcus aureus virulence in murine septic arthritis
    • Nilsson, I.M., Hartford, O., Foster, T., Tarkowski, A., Alpha-toxin and gamma-toxin jointly promote Staphylococcus aureus virulence in murine septic arthritis. Infect. Immun. 67:3 (1999), 1045–1049.
    • (1999) Infect. Immun. , vol.67 , Issue.3 , pp. 1045-1049
    • Nilsson, I.M.1    Hartford, O.2    Foster, T.3    Tarkowski, A.4
  • 86
    • 0037242676 scopus 로고    scopus 로고
    • Purification, cloning and characterization of variant LukE-LukD with strong leukocidal activity of staphylococcal bi-component leukotoxin family
    • Morinaga, N.Y., Kaihou Noda, M., Purification, cloning and characterization of variant LukE-LukD with strong leukocidal activity of staphylococcal bi-component leukotoxin family. Microbiol. Immunol. 47:1 (2003), 81–90.
    • (2003) Microbiol. Immunol. , vol.47 , Issue.1 , pp. 81-90
    • Morinaga, N.Y.1    Kaihou Noda, M.2
  • 88
    • 84943580452 scopus 로고    scopus 로고
    • Molecular characteristics and virulence factors in methicillin-susceptible, resistant, and heterogeneous vancomycin-intermediate Staphylococcus aureus from central-southern China
    • Liu, C., Chen, Z.J., Sun, Z., Feng, X., Zou, M., Cao, W., Wang, S., Zeng, J., Wang, Y., Sun, M., Molecular characteristics and virulence factors in methicillin-susceptible, resistant, and heterogeneous vancomycin-intermediate Staphylococcus aureus from central-southern China. J. Microbiol. Immunol. Infect. 48:5 (2015), 490–496.
    • (2015) J. Microbiol. Immunol. Infect. , vol.48 , Issue.5 , pp. 490-496
    • Liu, C.1    Chen, Z.J.2    Sun, Z.3    Feng, X.4    Zou, M.5    Cao, W.6    Wang, S.7    Zeng, J.8    Wang, Y.9    Sun, M.10
  • 89
    • 34848813797 scopus 로고    scopus 로고
    • Virulence genes of bovine Staphylococcus aureus from persistent and nonpersistent intramammary infections with different clinical characteristics
    • Haveri, M., Roslof, A., Rantala, L., Pyorala, S., Virulence genes of bovine Staphylococcus aureus from persistent and nonpersistent intramammary infections with different clinical characteristics. J. Appl. Microbiol. 103:4 (2007), 993–1000.
    • (2007) J. Appl. Microbiol. , vol.103 , Issue.4 , pp. 993-1000
    • Haveri, M.1    Roslof, A.2    Rantala, L.3    Pyorala, S.4
  • 90
    • 84941992866 scopus 로고    scopus 로고
    • Prevalence and molecular characteristics of methicillin-resistant Staphylococcus aureus among skin and soft tissue infections in an emergency department in Guyana
    • Dozois, A., Thomsen, I., Jimenez-Truque, N., Soper, N., Pearson, A., Mohamed-Rambaran, P., Dettorre, K.B., Creech, C.B., Wright, S.W., Prevalence and molecular characteristics of methicillin-resistant Staphylococcus aureus among skin and soft tissue infections in an emergency department in Guyana. Emerg. Med. J. 32:10 (2015), 800–803.
    • (2015) Emerg. Med. J. , vol.32 , Issue.10 , pp. 800-803
    • Dozois, A.1    Thomsen, I.2    Jimenez-Truque, N.3    Soper, N.4    Pearson, A.5    Mohamed-Rambaran, P.6    Dettorre, K.B.7    Creech, C.B.8    Wright, S.W.9
  • 91
    • 84894270046 scopus 로고    scopus 로고
    • Children with invasive Staphylococcus aureus disease exhibit a potently neutralizing antibody response to the cytotoxin LukAB
    • Thomsen, I.P., Dumont, A.L., James, D.B., Yoong, P., Saville, B.R., Soper, N., Torres, V.J., Creech, C.B., Children with invasive Staphylococcus aureus disease exhibit a potently neutralizing antibody response to the cytotoxin LukAB. Infect. Immun. 82:3 (2014), 1234–1242.
    • (2014) Infect. Immun. , vol.82 , Issue.3 , pp. 1234-1242
    • Thomsen, I.P.1    Dumont, A.L.2    James, D.B.3    Yoong, P.4    Saville, B.R.5    Soper, N.6    Torres, V.J.7    Creech, C.B.8
  • 92
    • 84936769144 scopus 로고    scopus 로고
    • Staphylococcus aureus Leukocidin A/B (LukAB) kills human monocytes via host NLRP3 and ASC when extracellular, but not intracellular
    • Melehani, J.H., James, D.B., DuMont, A.L., Torres, V.J., Duncan, J.A., Staphylococcus aureus Leukocidin A/B (LukAB) kills human monocytes via host NLRP3 and ASC when extracellular, but not intracellular. PLoS Pathog., 11(6), 2015, e1004970.
    • (2015) PLoS Pathog. , vol.11 , Issue.6 , pp. e1004970
    • Melehani, J.H.1    James, D.B.2    DuMont, A.L.3    Torres, V.J.4    Duncan, J.A.5
  • 96
    • 0037341574 scopus 로고    scopus 로고
    • Leucotoxic activities of Staphylococcus aureus strains isolated from cows, ewes, and goats with mastitis: importance of LukM/LukF’-PV leukotoxin
    • Rainard, P.J.C., Corrales, M.B., Barrio, T., Cochard Poutrel, B., Leucotoxic activities of Staphylococcus aureus strains isolated from cows, ewes, and goats with mastitis: importance of LukM/LukF’-PV leukotoxin. Clin. Vaccine Immunol. 10:2 (2003), 272–277.
    • (2003) Clin. Vaccine Immunol. , vol.10 , Issue.2 , pp. 272-277
    • Rainard, P.J.C.1    Corrales, M.B.2    Barrio, T.3    Cochard Poutrel, B.4
  • 97
    • 84865034511 scopus 로고    scopus 로고
    • Leukocidin genes lukF-P83 and lukM are associated with Staphylococcus aureus clonal complexes 151, 479 and 133 isolated from bovine udder infections in Thuringia, Germany
    • Schlotter, K., Ehricht, R., Hotzel, H., Monecke, S., Pfeffer, M., Donat, K., Leukocidin genes lukF-P83 and lukM are associated with Staphylococcus aureus clonal complexes 151, 479 and 133 isolated from bovine udder infections in Thuringia, Germany. Vet. Res., 43, 2012, 42.
    • (2012) Vet. Res. , vol.43 , pp. 42
    • Schlotter, K.1    Ehricht, R.2    Hotzel, H.3    Monecke, S.4    Pfeffer, M.5    Donat, K.6
  • 98
    • 84857326507 scopus 로고    scopus 로고
    • Invited review: mastitis in dairy heifers: nature of the disease, potential impact, prevention, and control
    • De Vliegher, S.L.K., Fox, S., Piepers, S., McDougall Barkema, H.W., Invited review: mastitis in dairy heifers: nature of the disease, potential impact, prevention, and control. J. Dairy Sci. 95:3 (2012), 1025–1040.
    • (2012) J. Dairy Sci. , vol.95 , Issue.3 , pp. 1025-1040
    • De Vliegher, S.L.K.1    Fox, S.2    Piepers, S.3    McDougall Barkema, H.W.4
  • 99
    • 24644432505 scopus 로고    scopus 로고
    • Leukotoxin family genes in Staphylococcus aureus isolated from domestic animals and prevalence of lukM-lukF-PV genes by bacteriophages in bovine isolates
    • Yamada, T., Tochimaru, N., Nakasuji, S., Hata, E., Kobayashi, H., Eguchi, M., Kaneko, J., Kamio, Y., Kaidoh, T., Takeuchi, S., Leukotoxin family genes in Staphylococcus aureus isolated from domestic animals and prevalence of lukM-lukF-PV genes by bacteriophages in bovine isolates. Vet. Microbiol. 110:1–2 (2005), 97–103.
    • (2005) Vet. Microbiol. , vol.110 , Issue.1-2 , pp. 97-103
    • Yamada, T.1    Tochimaru, N.2    Nakasuji, S.3    Hata, E.4    Kobayashi, H.5    Eguchi, M.6    Kaneko, J.7    Kamio, Y.8    Kaidoh, T.9    Takeuchi, S.10
  • 100
    • 33748363682 scopus 로고    scopus 로고
    • LukM/LukF’-PV is the most active Staphylococcus aureus leukotoxin on bovine neutrophils
    • Barrio, M.B., Rainard, P., Prevost, G., LukM/LukF’-PV is the most active Staphylococcus aureus leukotoxin on bovine neutrophils. Microbes Infect. 8:8 (2006), 2068–2074.
    • (2006) Microbes Infect. , vol.8 , Issue.8 , pp. 2068-2074
    • Barrio, M.B.1    Rainard, P.2    Prevost, G.3
  • 101
    • 0014261629 scopus 로고
    • Interaction of Staphylococcal α-toxin wth artifical and natural membranes
    • Freer, J.H.J.P., Arbuthnott Bernheimer, A.W., Interaction of Staphylococcal α-toxin wth artifical and natural membranes. J. Bacteriol. 95:3 (1968), 1153–1168.
    • (1968) J. Bacteriol. , vol.95 , Issue.3 , pp. 1153-1168
    • Freer, J.H.J.P.1    Arbuthnott Bernheimer, A.W.2
  • 102
    • 0023237149 scopus 로고
    • Membrane-damaging action of staphylococcal α-toxin on phospholipid cholesterol liposomes
    • Watanabe, M.T., Tomita Yasuda, T., Membrane-damaging action of staphylococcal α-toxin on phospholipid cholesterol liposomes. Biochim. Biophys. Acta 898:3 (1987), 257–265.
    • (1987) Biochim. Biophys. Acta , vol.898 , Issue.3 , pp. 257-265
    • Watanabe, M.T.1    Tomita Yasuda, T.2
  • 103
    • 33748751596 scopus 로고    scopus 로고
    • Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore
    • Valeva, A., Hellmann, N., Walev, I., Strand, D., Plate, M., Boukhallouk, F., Brack, A., Hanada, K., Decker, H., Bhakdi, S., Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore. J. Biol. Chem. 281:36 (2006), 26014–26021.
    • (2006) J. Biol. Chem. , vol.281 , Issue.36 , pp. 26014-26021
    • Valeva, A.1    Hellmann, N.2    Walev, I.3    Strand, D.4    Plate, M.5    Boukhallouk, F.6    Brack, A.7    Hanada, K.8    Decker, H.9    Bhakdi, S.10
  • 104
    • 2442650172 scopus 로고    scopus 로고
    • High resolution crystallographic studies of α-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: implication for understanding protein-lipid interactions
    • Galdiero, S., Gouaux, E., High resolution crystallographic studies of α-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: implication for understanding protein-lipid interactions. Protein Sci. 13:6 (2004), 1503–1511.
    • (2004) Protein Sci. , vol.13 , Issue.6 , pp. 1503-1511
    • Galdiero, S.1    Gouaux, E.2
  • 105
    • 0015953374 scopus 로고
    • Biological properties of staphylococcal α-toxin
    • Cassidy, P., Six, H.E., Harshman, S., Biological properties of staphylococcal α-toxin. Biochim. Biophys. Acta 332 (1974), 413–423.
    • (1974) Biochim. Biophys. Acta , vol.332 , pp. 413-423
    • Cassidy, P.1    Six, H.E.2    Harshman, S.3
  • 106
    • 0019004431 scopus 로고
    • Rabbit erythrocyte band 3: a receptor for staphylococcal alpha toxin
    • Maharaj, I., Fackrell, H.B., Rabbit erythrocyte band 3: a receptor for staphylococcal alpha toxin. Can. J. Microbiol. 26:4 (1980), 524–531.
    • (1980) Can. J. Microbiol. , vol.26 , Issue.4 , pp. 524-531
    • Maharaj, I.1    Fackrell, H.B.2
  • 107
    • 0017153612 scopus 로고
    • 125I-labeled α-toxin to rabbit erythrocytes
    • 125I-labeled α-toxin to rabbit erythrocytes. Biochemistry 15:11 (1976), 2348–2355.
    • (1976) Biochemistry , vol.15 , Issue.11 , pp. 2348-2355
    • Cassidy, P.1    Harshman, S.2
  • 108
    • 0025947639 scopus 로고
    • Staphylococcus aureus α-toxin: dual mechanism of binding to target cells
    • Hildebrand, A.M., Pohl Bhakdi, S., Staphylococcus aureus α-toxin: dual mechanism of binding to target cells. J. Biol. Chem. 266:26 (1991), 17195–17200.
    • (1991) J. Biol. Chem. , vol.266 , Issue.26 , pp. 17195-17200
    • Hildebrand, A.M.1    Pohl Bhakdi, S.2
  • 110
    • 34548790062 scopus 로고    scopus 로고
    • Aromatic residues of Caveolin-1 binding motif of α-hemolysin are essential for membrane penetration
    • Pany, S., Krishnasastry, M.V., Aromatic residues of Caveolin-1 binding motif of α-hemolysin are essential for membrane penetration. Biochem. Biophys. Res. Commun. 363:1 (2007), 197–202.
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , Issue.1 , pp. 197-202
    • Pany, S.1    Krishnasastry, M.V.2
  • 112
    • 5444262529 scopus 로고    scopus 로고
    • Functional form of Caveolin-1 is necessary for the assembly of α-hemolysin
    • Vijayvargia, R., Suresh, C.G., Krishnasastry, M.V., Functional form of Caveolin-1 is necessary for the assembly of α-hemolysin. Biochem. Biophys. Res. Commun. 324:3 (2004), 1130–1136.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , Issue.3 , pp. 1130-1136
    • Vijayvargia, R.1    Suresh, C.G.2    Krishnasastry, M.V.3
  • 113
    • 77955783248 scopus 로고    scopus 로고
    • Role of a disintegrin and metalloprotease 10 in Staphylococcus aureus α-hemolysin-mediated cellular injury
    • Wilke, G.A., Bubeck Wardenburg, J., Role of a disintegrin and metalloprotease 10 in Staphylococcus aureus α-hemolysin-mediated cellular injury. Proc. Natl. Acad. Sci. U. S. A. 107:30 (2010), 13473–13478.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.30 , pp. 13473-13478
    • Wilke, G.A.1    Bubeck Wardenburg, J.2
  • 115
    • 84963815220 scopus 로고    scopus 로고
    • Genome-wide CRISPR screen reveals novel host factors required for Staphylococcus aureus α-hemolysin-mediated toxicity
    • Virreira Winter, S., Zychlinsky, A., Bardoel, B.W., Genome-wide CRISPR screen reveals novel host factors required for Staphylococcus aureus α-hemolysin-mediated toxicity. Sci. Rep., 6, 2016, 24242.
    • (2016) Sci. Rep. , vol.6 , pp. 24242
    • Virreira Winter, S.1    Zychlinsky, A.2    Bardoel, B.W.3
  • 118
    • 84978144802 scopus 로고    scopus 로고
    • ADAM10-dependent signaling through Notch1 and Notch4 controls development of organ-specific vascular beds
    • Alabi, R.O., Glomski, K., Haxaire, C., Weskamp, G., Monette, S., Blobel, C.P., ADAM10-dependent signaling through Notch1 and Notch4 controls development of organ-specific vascular beds. Circ. Res. 119:4 (2016), 519–531.
    • (2016) Circ. Res. , vol.119 , Issue.4 , pp. 519-531
    • Alabi, R.O.1    Glomski, K.2    Haxaire, C.3    Weskamp, G.4    Monette, S.5    Blobel, C.P.6
  • 119
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • Hattori, M., Osterfield, M., Flanagan, J.G., Regulated cleavage of a contact-mediated axon repellent. Science 289:5483 (2000), 1360–1365.
    • (2000) Science , vol.289 , Issue.5483 , pp. 1360-1365
    • Hattori, M.1    Osterfield, M.2    Flanagan, J.G.3
  • 120
    • 0343196671 scopus 로고    scopus 로고
    • Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
    • Pan, D., Rubin, G.M., Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90:2 (1997), 271–280.
    • (1997) Cell , vol.90 , Issue.2 , pp. 271-280
    • Pan, D.1    Rubin, G.M.2
  • 122
    • 0036152681 scopus 로고    scopus 로고
    • Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells
    • Lemjabbar, H., Basbaum, C., Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells. Nat. Med. 8:1 (2002), 41–46.
    • (2002) Nat. Med. , vol.8 , Issue.1 , pp. 41-46
    • Lemjabbar, H.1    Basbaum, C.2
  • 123
    • 45149117638 scopus 로고    scopus 로고
    • ADAM10 regulates endothelial permeability and T-Cell transmigration by proteolysis of vascular endothelial cadherin
    • Schulz, B., Pruessmeyer, J., Maretzky, T., Ludwig, A., Blobel, C.P., Saftig, P., Reiss, K., ADAM10 regulates endothelial permeability and T-Cell transmigration by proteolysis of vascular endothelial cadherin. Circ. Res. 102:10 (2008), 1192–1201.
    • (2008) Circ. Res. , vol.102 , Issue.10 , pp. 1192-1201
    • Schulz, B.1    Pruessmeyer, J.2    Maretzky, T.3    Ludwig, A.4    Blobel, C.P.5    Saftig, P.6    Reiss, K.7
  • 125
    • 84950246980 scopus 로고    scopus 로고
    • TspanC8 tetraspanins differentially regulate the cleavage of ADAM10 substrates, Notch activation and ADAM10 membrane compartmentalization
    • Jouannet, S., Saint-Pol, J., Fernandez, L., Nguyen, V., Charrin, S., Boucheix, C., Brou, C., Milhiet, P.E., Rubinstein, E., TspanC8 tetraspanins differentially regulate the cleavage of ADAM10 substrates, Notch activation and ADAM10 membrane compartmentalization. Cell. Mol. Life Sci. 73:9 (2016), 1895–1915.
    • (2016) Cell. Mol. Life Sci. , vol.73 , Issue.9 , pp. 1895-1915
    • Jouannet, S.1    Saint-Pol, J.2    Fernandez, L.3    Nguyen, V.4    Charrin, S.5    Boucheix, C.6    Brou, C.7    Milhiet, P.E.8    Rubinstein, E.9
  • 126
    • 84966293694 scopus 로고    scopus 로고
    • TspanC8 tetraspanins and a disintegrin and metalloprotease 10 (ADAM10) interact via their extracellular regions: evidence for distinct binding mechanisms for different TspanC8 proteins
    • Noy, P.J., Yang, J., Reyat, J.S., Matthews, A.L., Charlton, A.E., Furmston, J., Rogers, D.A., Rainger, G.E., Tomlinson, M.G., TspanC8 tetraspanins and a disintegrin and metalloprotease 10 (ADAM10) interact via their extracellular regions: evidence for distinct binding mechanisms for different TspanC8 proteins. J. Biol. Chem. 291:7 (2016), 3145–3157.
    • (2016) J. Biol. Chem. , vol.291 , Issue.7 , pp. 3145-3157
    • Noy, P.J.1    Yang, J.2    Reyat, J.S.3    Matthews, A.L.4    Charlton, A.E.5    Furmston, J.6    Rogers, D.A.7    Rainger, G.E.8    Tomlinson, M.G.9
  • 129
    • 15444371289 scopus 로고    scopus 로고
    • ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and β-catenin nuclear signalling
    • Reiss, K.T., Maretzky, A., Ludwig, Tousseyn, T., de Strooper, B.D., Hartmann, P., Saftig, ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and β-catenin nuclear signalling. EMBO J. 24:4 (2005), 742–752.
    • (2005) EMBO J. , vol.24 , Issue.4 , pp. 742-752
    • Reiss, K.T.1    Maretzky, A.2    Ludwig3    Tousseyn, T.4    de Strooper, B.D.5    Hartmann, P.6    Saftig7
  • 130
    • 12544257436 scopus 로고    scopus 로고
    • ADAM10 mediates ectodomain shedding of the betacellulin precursor activated by p-aminophenylmercuric acetate and extracellular calcium influx
    • Sanderson, M.P., Erickson, S.N., Gough, P.J., Garton, K.J., Wille, P.T., Raines, E.W., Dunbar, A.J., Dempsey, P.J., ADAM10 mediates ectodomain shedding of the betacellulin precursor activated by p-aminophenylmercuric acetate and extracellular calcium influx. J. Biol. Chem. 280:3 (2005), 1826–1837.
    • (2005) J. Biol. Chem. , vol.280 , Issue.3 , pp. 1826-1837
    • Sanderson, M.P.1    Erickson, S.N.2    Gough, P.J.3    Garton, K.J.4    Wille, P.T.5    Raines, E.W.6    Dunbar, A.J.7    Dempsey, P.J.8
  • 131
  • 132
    • 0030018156 scopus 로고    scopus 로고
    • CC. CKR5: a RANTES, MIP-1α MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib, G.C., Combadiere, C.C., Broder, Y., Feng, P.E., Kennedy, P.M., Murphy, E.A., Berger, CC. CKR5: a RANTES, MIP-1α MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1. Science 272:5270 (1996), 1955–1958.
    • (1996) Science , vol.272 , Issue.5270 , pp. 1955-1958
    • Alkhatib, G.C.1    Combadiere, C.C.2    Broder, Y.3    Feng, P.E.4    Kennedy, P.M.5    Murphy, E.A.6    Berger7
  • 133
    • 20044390745 scopus 로고    scopus 로고
    • Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC)
    • Choe, H., Moore, M.J., Owens, C.M., Wright, P.L., Vasilieva, N., Li, W., Singh, A.P., Shakri, R., Chitnis, C.E., Farzan, M., Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC). Mol. Microbiol. 55:5 (2005), 1413–1422.
    • (2005) Mol. Microbiol. , vol.55 , Issue.5 , pp. 1413-1422
    • Choe, H.1    Moore, M.J.2    Owens, C.M.3    Wright, P.L.4    Vasilieva, N.5    Li, W.6    Singh, A.P.7    Shakri, R.8    Chitnis, C.E.9    Farzan, M.10
  • 135
    • 84875988747 scopus 로고    scopus 로고
    • Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1)
    • Tan, J.H., Ludeman, J.P., Wedderburn, J., Canals, M., Hall, P., Butler, S.J., Taleski, D., Christopoulos, A., Hickey, M.J., Payne, R.J., Stone, M.J., Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1). J. Biol. Chem. 288:14 (2013), 10024–10034.
    • (2013) J. Biol. Chem. , vol.288 , Issue.14 , pp. 10024-10034
    • Tan, J.H.1    Ludeman, J.P.2    Wedderburn, J.3    Canals, M.4    Hall, P.5    Butler, S.J.6    Taleski, D.7    Christopoulos, A.8    Hickey, M.J.9    Payne, R.J.10    Stone, M.J.11
  • 136
    • 84895123623 scopus 로고    scopus 로고
    • The structural role of receptor tyrosine sulfation in chemokine recognition
    • Ludeman, J.P., Stone, M.J., The structural role of receptor tyrosine sulfation in chemokine recognition. Br. J. Pharmacol. 171:5 (2014), 1167–1179.
    • (2014) Br. J. Pharmacol. , vol.171 , Issue.5 , pp. 1167-1179
    • Ludeman, J.P.1    Stone, M.J.2
  • 137
    • 0028928890 scopus 로고
    • Genomic organization of the glycoprotein D gene: Duffy blood group Fya/Fyb alloantigen system is associated with a polymorphism at the 44-amino acid residue
    • Iwamoto, S., Omi, T., Kajii, E., Ikemoto, S., Genomic organization of the glycoprotein D gene: Duffy blood group Fya/Fyb alloantigen system is associated with a polymorphism at the 44-amino acid residue. Blood 85:3 (1995), 622–626.
    • (1995) Blood , vol.85 , Issue.3 , pp. 622-626
    • Iwamoto, S.1    Omi, T.2    Kajii, E.3    Ikemoto, S.4
  • 138
    • 0029001881 scopus 로고
    • Disruption of a GATA motif in the Duffy gene promoter abolishes erythroid gene expression in Duffy-negative individuals
    • Tournamille, C., Colin, Y., Cartron, J.P., Le Van Kim, C., Disruption of a GATA motif in the Duffy gene promoter abolishes erythroid gene expression in Duffy-negative individuals. Nat. Genet. 10:2 (1995), 224–228.
    • (1995) Nat. Genet. , vol.10 , Issue.2 , pp. 224-228
    • Tournamille, C.1    Colin, Y.2    Cartron, J.P.3    Le Van Kim, C.4
  • 140
    • 3543117686 scopus 로고    scopus 로고
    • Arg89Cys substitution results in very low membrane expression of the Duffy antigen/receptor for chemokines in Fyx individuals
    • Tournamille, C., Le Van Kim, C.P., Gane, Le Pennec, P.Y.F., Roubinet, J., Babinet, J.P., Carton, Y., Colin, Arg89Cys substitution results in very low membrane expression of the Duffy antigen/receptor for chemokines in Fyx individuals. Blood 92:6 (1998), 2147–2156.
    • (1998) Blood , vol.92 , Issue.6 , pp. 2147-2156
    • Tournamille, C.1    Le Van Kim, C.P.2    Gane3    Le Pennec, P.Y.F.4    Roubinet, J.5    Babinet, J.P.6    Carton, Y.7    Colin8
  • 144
    • 0019840267 scopus 로고
    • Effect of staphylococcal leukocidin on mouse leukocyte system
    • Grojec, P., Jeljaszewicz, J., Effect of staphylococcal leukocidin on mouse leukocyte system. Zentralbl. Bakteriol. Mikrobiol. Hyg. 250 (1981), 446–455.
    • (1981) Zentralbl. Bakteriol. Mikrobiol. Hyg. , vol.250 , pp. 446-455
    • Grojec, P.1    Jeljaszewicz, J.2
  • 145
    • 84939534435 scopus 로고    scopus 로고
    • Staphylococcus aureus infection in humanized mice: a new model to study pathogenicity associated with human immune response
    • Knop, J., Hanses, F., Leist, T., Archin, N.M., Buchholz, S., Glasner, J., Gessner, A., Wege, A.K., Staphylococcus aureus infection in humanized mice: a new model to study pathogenicity associated with human immune response. J. Infect. Dis. 212:3 (2015), 435–444.
    • (2015) J. Infect. Dis. , vol.212 , Issue.3 , pp. 435-444
    • Knop, J.1    Hanses, F.2    Leist, T.3    Archin, N.M.4    Buchholz, S.5    Glasner, J.6    Gessner, A.7    Wege, A.K.8
  • 146
    • 85021989813 scopus 로고    scopus 로고
    • Humanized mice exhibit increased susceptibility to Staphylococcus aureus pneumonia
    • Prince, A., Wang, H., Kitur, K., Parker, D., Humanized mice exhibit increased susceptibility to Staphylococcus aureus pneumonia. J. Infect. Dis., 2016, 10.1093/infdis/jiw425.
    • (2016) J. Infect. Dis.
    • Prince, A.1    Wang, H.2    Kitur, K.3    Parker, D.4
  • 148
    • 0035080948 scopus 로고    scopus 로고
    • Flow cytometric determination of Panton-Valentine leucocidin S component binding
    • Gauduchon, V., Werner, S., Prevost, G., Monteil, H., Colin, D.A., Flow cytometric determination of Panton-Valentine leucocidin S component binding. Infect. Immun. 69:4 (2001), 2390–2395.
    • (2001) Infect. Immun. , vol.69 , Issue.4 , pp. 2390-2395
    • Gauduchon, V.1    Werner, S.2    Prevost, G.3    Monteil, H.4    Colin, D.A.5
  • 149
    • 0021944908 scopus 로고
    • Staphylococcal α-toxin-induced PGI2 production in endothelial cells: role of calcium
    • Suttorp, N., Seeger, W., Dewein, E., Bhakdi, S., Roka, L., Staphylococcal α-toxin-induced PGI2 production in endothelial cells: role of calcium. Am. J. Physiol. 248:1 (Pt. 1) (1985), C127–C134.
    • (1985) Am. J. Physiol. , vol.248 , Issue.1 (Pt. 1) , pp. C127-C134
    • Suttorp, N.1    Seeger, W.2    Dewein, E.3    Bhakdi, S.4    Roka, L.5
  • 151
    • 0028324930 scopus 로고
    • Novel path to apoptosis: small transmembrane pores created by staphylococcal alpha-toxin in T lymphocytes evoke internucleosomal DNA degradation
    • Jonas, D., Walev, I., Berger, T., Liebetrau, M., Palmer, M., Bhakdi, S., Novel path to apoptosis: small transmembrane pores created by staphylococcal alpha-toxin in T lymphocytes evoke internucleosomal DNA degradation. Infect. Immun. 62:4 (1994), 1304–1312.
    • (1994) Infect. Immun. , vol.62 , Issue.4 , pp. 1304-1312
    • Jonas, D.1    Walev, I.2    Berger, T.3    Liebetrau, M.4    Palmer, M.5    Bhakdi, S.6
  • 152
    • 0020041511 scopus 로고
    • Mode of action of staphylococcal leukocidin: effects of the S and F components on the activities of membrane-associated enzymes of rabbit polymorphonuclear leukocytes
    • Noda, M., Kato, I., Hirayama, T., Matsuda, F., Mode of action of staphylococcal leukocidin: effects of the S and F components on the activities of membrane-associated enzymes of rabbit polymorphonuclear leukocytes. Infect. Immun. 35:1 (1982), 38–45.
    • (1982) Infect. Immun. , vol.35 , Issue.1 , pp. 38-45
    • Noda, M.1    Kato, I.2    Hirayama, T.3    Matsuda, F.4
  • 153
    • 84987762163 scopus 로고    scopus 로고
    • Staphylococcus aureus α-toxin-mediated cation entry depolarizes membrane potential and activates p38 MAP kinase in airway epithelial cells
    • Eiffler, I., Behnke, J., Ziesemer, S., Muller, C., Hildebrandt, J.P., Staphylococcus aureus α-toxin-mediated cation entry depolarizes membrane potential and activates p38 MAP kinase in airway epithelial cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 311:3 (2016), L676–685.
    • (2016) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.311 , Issue.3 , pp. L676-685
    • Eiffler, I.1    Behnke, J.2    Ziesemer, S.3    Muller, C.4    Hildebrandt, J.P.5
  • 154
    • 64249158831 scopus 로고    scopus 로고
    • Virulence factors of Staphylococcus aureus induce Erk-MAP kinase activation and c-Fos expression in S9 and 16HBE14o- human airway epithelial cells
    • Below, S., Konkel, A., Zeeck, C., Muller, C., Kohler, C., Engelmann, S., Hildebrandt, J.P., Virulence factors of Staphylococcus aureus induce Erk-MAP kinase activation and c-Fos expression in S9 and 16HBE14o- human airway epithelial cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 296:3 (2009), L470–9.
    • (2009) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.296 , Issue.3 , pp. L470-9
    • Below, S.1    Konkel, A.2    Zeeck, C.3    Muller, C.4    Kohler, C.5    Engelmann, S.6    Hildebrandt, J.P.7
  • 155
    • 64749091309 scopus 로고    scopus 로고
    • Antimicrobial mechanisms of phagocytes and bacterial evasion strategies
    • Flannagan, R.S., Cosio, G., Grinstein, S., Antimicrobial mechanisms of phagocytes and bacterial evasion strategies. Nat. Rev. Microbiol. 7:5 (2009), 355–366.
    • (2009) Nat. Rev. Microbiol. , vol.7 , Issue.5 , pp. 355-366
    • Flannagan, R.S.1    Cosio, G.2    Grinstein, S.3
  • 156
    • 77953893605 scopus 로고    scopus 로고
    • Listeria monocytogenes internalin and E-cadherin: from bench to bedside
    • Bonazzi, M., Lecuit, M., Cossart, P., Listeria monocytogenes internalin and E-cadherin: from bench to bedside. Cold Spring Harb. Perspect. Biol., 1(4), 2009, a003087.
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1 , Issue.4 , pp. a003087
    • Bonazzi, M.1    Lecuit, M.2    Cossart, P.3
  • 157
    • 84897927940 scopus 로고    scopus 로고
    • Yersina pestis: mechanisms of entry into and resistance to the host cell
    • Ke, Y., Chen, Z., Yang, R., Yersina pestis: mechanisms of entry into and resistance to the host cell. Front. Cell. Infect. Microbiol., 3, 2013, 106.
    • (2013) Front. Cell. Infect. Microbiol. , vol.3 , pp. 106
    • Ke, Y.1    Chen, Z.2    Yang, R.3
  • 158
    • 84940121894 scopus 로고    scopus 로고
    • CD36 is essential for regulation of the host innate response to Staphylococcus aureus α-toxin-mediated dermonecrosis
    • Castleman, M.J., Febbraio, M., Hall, P.R., CD36 is essential for regulation of the host innate response to Staphylococcus aureus α-toxin-mediated dermonecrosis. J. Immunol. 195:5 (2015), 2294–2302.
    • (2015) J. Immunol. , vol.195 , Issue.5 , pp. 2294-2302
    • Castleman, M.J.1    Febbraio, M.2    Hall, P.R.3
  • 161
    • 0024421764 scopus 로고
    • Release of interleukin-1β associated with potent cytocidal action of staphylococcal alpha-toxin on human monocytes
    • Bhakdi, S.M., Muhly, S., Korom Hugo, F., Release of interleukin-1β associated with potent cytocidal action of staphylococcal alpha-toxin on human monocytes. Infect. Immun. 57:11 (1989), 3512–3519.
    • (1989) Infect. Immun. , vol.57 , Issue.11 , pp. 3512-3519
    • Bhakdi, S.M.1    Muhly, S.2    Korom Hugo, F.3
  • 165
    • 84906939947 scopus 로고    scopus 로고
    • J Bubeck Wardenburg, Tissue-specific patterning of host innate immune responses by Staphylococcus aureus α-toxin
    • Becker, R.E., Berube, B.J., Sampedro, G.R., DeDent, A.C., J Bubeck Wardenburg, Tissue-specific patterning of host innate immune responses by Staphylococcus aureus α-toxin. J. Innate Immun. 6:5 (2014), 619–631.
    • (2014) J. Innate Immun. , vol.6 , Issue.5 , pp. 619-631
    • Becker, R.E.1    Berube, B.J.2    Sampedro, G.R.3    DeDent, A.C.4
  • 168
    • 0028134652 scopus 로고
    • GTP-binding proteins are involved in the modulated activity of human neutrophils treated with the Panton-Valentine leukocidin from Staphylococcus aureus
    • Hensler, T., Koller, M., Prevost, G., Piemont, Y., Konig, W., GTP-binding proteins are involved in the modulated activity of human neutrophils treated with the Panton-Valentine leukocidin from Staphylococcus aureus. Infect. Immun. 62:12 (1994), 5281–5289.
    • (1994) Infect. Immun. , vol.62 , Issue.12 , pp. 5281-5289
    • Hensler, T.1    Koller, M.2    Prevost, G.3    Piemont, Y.4    Konig, W.5
  • 170
    • 0037973528 scopus 로고    scopus 로고
    • Control of the oxidative burst of human neutrophils by staphylococcal leukotoxins
    • Colin, D.A., Monteil, H., Control of the oxidative burst of human neutrophils by staphylococcal leukotoxins. Infect. Immun. 71:7 (2003), 3724–3729.
    • (2003) Infect. Immun. , vol.71 , Issue.7 , pp. 3724-3729
    • Colin, D.A.1    Monteil, H.2
  • 171
    • 76649119813 scopus 로고    scopus 로고
    • Antibody-mediated enhancement of community-acquired methicillin-resistant Staphylococcus aureus infection
    • Yoong, P., Pier, G.B., Antibody-mediated enhancement of community-acquired methicillin-resistant Staphylococcus aureus infection. Proc. Natl. Acad. Sci. U. S. A. 107:5 (2010), 2241–2246.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.5 , pp. 2241-2246
    • Yoong, P.1    Pier, G.B.2
  • 172
    • 84962710220 scopus 로고    scopus 로고
    • The interplay between regulated necrosis and bacterial infection
    • Bleriot, C., Lecuit, M., The interplay between regulated necrosis and bacterial infection. Cell. Mol. Life Sci. 73:11–12 (2016), 2369–2378.
    • (2016) Cell. Mol. Life Sci. , vol.73 , Issue.11-12 , pp. 2369-2378
    • Bleriot, C.1    Lecuit, M.2
  • 173
    • 84962861111 scopus 로고    scopus 로고
    • The intersection of cell death and inflammasome activation
    • Vince, J.E., Silke, J., The intersection of cell death and inflammasome activation. Cell. Mol. Life Sci. 73:11–12 (2016), 2349–2367.
    • (2016) Cell. Mol. Life Sci. , vol.73 , Issue.11-12 , pp. 2349-2367
    • Vince, J.E.1    Silke, J.2
  • 177
    • 48849090895 scopus 로고    scopus 로고
    • The expression of alpha-haemolysin is required for Staphylococcus aureus phagosomal escape after internalization in CFT-1 cells
    • Jarry, T.M., Memmi, G., Cheung, A.L., The expression of alpha-haemolysin is required for Staphylococcus aureus phagosomal escape after internalization in CFT-1 cells. Cell. Microbiol. 10:9 (2008), 1801–1814.
    • (2008) Cell. Microbiol. , vol.10 , Issue.9 , pp. 1801-1814
    • Jarry, T.M.1    Memmi, G.2    Cheung, A.L.3
  • 179
    • 84891506872 scopus 로고    scopus 로고
    • Panton-Valentine leukocidin facilitates the escape of Staphylococcus aureus from human keratinocyte endosomes and induces apoptosis
    • Chi, C.Y., Lin, C.C., Liao, I.C., Yao, Y.C., Shen, F.C., Liu, C.C., Lin, C.F., Panton-Valentine leukocidin facilitates the escape of Staphylococcus aureus from human keratinocyte endosomes and induces apoptosis. J. Infect. Dis. 209:2 (2014), 224–235.
    • (2014) J. Infect. Dis. , vol.209 , Issue.2 , pp. 224-235
    • Chi, C.Y.1    Lin, C.C.2    Liao, I.C.3    Yao, Y.C.4    Shen, F.C.5    Liu, C.C.6    Lin, C.F.7
  • 180
    • 84961282143 scopus 로고    scopus 로고
    • Influence of Sae-regulated and Agr-regulated factors on the escape of Staphylococcus aureus from human macrophages
    • Munzenmayer, L., Geiger, T., Daiber, E., Schulte, B., Autenrieth, S.E., Fraunholz, M., Wolz, C., Influence of Sae-regulated and Agr-regulated factors on the escape of Staphylococcus aureus from human macrophages. Cell. Microbiol. 18:8 (2016), 1172–1183.
    • (2016) Cell. Microbiol. , vol.18 , Issue.8 , pp. 1172-1183
    • Munzenmayer, L.1    Geiger, T.2    Daiber, E.3    Schulte, B.4    Autenrieth, S.E.5    Fraunholz, M.6    Wolz, C.7
  • 181
    • 84890417859 scopus 로고    scopus 로고
    • Staphylococcus aureus leukotoxin GH promotes formation of neutrophil extracellular traps
    • Malachowa, N., Kobayashi, S.D., Freedman, B., Dorward, D.W., DeLeo, F.R., Staphylococcus aureus leukotoxin GH promotes formation of neutrophil extracellular traps. J. Immunol. 191:12 (2013), 6022–6029.
    • (2013) J. Immunol. , vol.191 , Issue.12 , pp. 6022-6029
    • Malachowa, N.1    Kobayashi, S.D.2    Freedman, B.3    Dorward, D.W.4    DeLeo, F.R.5
  • 182
    • 38349110486 scopus 로고    scopus 로고
    • Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles
    • Birmingham, C.L., Canadien, V., Kaniuk, N.A., Steinberg, B.E., Higgins, D.E., Brumell, J.H., Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles. Nature 451:7176 (2008), 350–354.
    • (2008) Nature , vol.451 , Issue.7176 , pp. 350-354
    • Birmingham, C.L.1    Canadien, V.2    Kaniuk, N.A.3    Steinberg, B.E.4    Higgins, D.E.5    Brumell, J.H.6
  • 184
  • 185
    • 84953281503 scopus 로고    scopus 로고
    • -Hemolysin enhances Staphylococcus aureus internalization and survival within mast cells by modulating the expression of (1 integrin
    • Goldmann, O.L., Tuchscherr, M., Rohde Medina, E., -Hemolysin enhances Staphylococcus aureus internalization and survival within mast cells by modulating the expression of (1 integrin. Cell. Microbiol. 18:6 (2016), 807–819.
    • (2016) Cell. Microbiol. , vol.18 , Issue.6 , pp. 807-819
    • Goldmann, O.L.1    Tuchscherr, M.2    Rohde Medina, E.3
  • 186
    • 0032037616 scopus 로고    scopus 로고
    • Macrophage receptors for Mycobacterium tuberculosis
    • Ernst, J.D., Macrophage receptors for Mycobacterium tuberculosis. Infect. Immun. 66:4 (1998), 1277–1281.
    • (1998) Infect. Immun. , vol.66 , Issue.4 , pp. 1277-1281
    • Ernst, J.D.1
  • 187
    • 34848908962 scopus 로고    scopus 로고
    • Fimbrial proteins of Porphyromonas gingivalis mediate in vivo virulence and exploit TLR2 and Complement Receptor 3 to persist in macrophages
    • Wang, M.M.A.K., Shakhatreh, D., James, S., Liang, Si Nishiyama, F., Yoshimura, D.R., Demuth, Hajishengallis, G., Fimbrial proteins of Porphyromonas gingivalis mediate in vivo virulence and exploit TLR2 and Complement Receptor 3 to persist in macrophages. J. Immunol. 179:4 (2007), 2349–2358.
    • (2007) J. Immunol. , vol.179 , Issue.4 , pp. 2349-2358
    • Wang, M.M.A.K.1    Shakhatreh, D.2    James, S.3    Liang4    Si Nishiyama, F.5    Yoshimura, D.R.6    Demuth7    Hajishengallis, G.8
  • 188
    • 84861177209 scopus 로고    scopus 로고
    • Staphylococcus aureus alpha-toxin perturbs the barrier function in Caco-2 epithelial cell monolayers by altering junctional integrity
    • Kwak, Y.K.E., Vikstrom, K.E., Magnusson, Vecsey-Semjen, B., Colque-Navarro, P.R., Mollby, The, Staphylococcus aureus alpha-toxin perturbs the barrier function in Caco-2 epithelial cell monolayers by altering junctional integrity. Infect. Immun. 80:5 (2012), 1670–1680.
    • (2012) Infect. Immun. , vol.80 , Issue.5 , pp. 1670-1680
    • Kwak, Y.K.E.1    Vikstrom, K.E.2    Magnusson3    Vecsey-Semjen, B.4    Colque-Navarro, P.R.5    Mollby6    The7
  • 190
    • 0033827609 scopus 로고    scopus 로고
    • Variable expressions of Staphylococcus aureus bicomponent leucotoxins semiquantified by competitive reverse transcription-PCR
    • Bronner, S., Stoessel, P., Gravet, A., Monteil, H., Prevost, G., Variable expressions of Staphylococcus aureus bicomponent leucotoxins semiquantified by competitive reverse transcription-PCR. Appl. Environ. Microbiol. 66:9 (2000), 3931–3938.
    • (2000) Appl. Environ. Microbiol. , vol.66 , Issue.9 , pp. 3931-3938
    • Bronner, S.1    Stoessel, P.2    Gravet, A.3    Monteil, H.4    Prevost, G.5
  • 192
    • 58849131103 scopus 로고    scopus 로고
    • Virulence gene expression in human community-acquired Staphylococcus aureus infection
    • Loughman, J.A., Fritz, S.A., Storch, G.A., Hunstad, D.A., Virulence gene expression in human community-acquired Staphylococcus aureus infection. J. Infect. Dis. 199:3 (2009), 294–301.
    • (2009) J. Infect. Dis. , vol.199 , Issue.3 , pp. 294-301
    • Loughman, J.A.1    Fritz, S.A.2    Storch, G.A.3    Hunstad, D.A.4
  • 195
  • 197
    • 79961009646 scopus 로고    scopus 로고
    • Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures
    • Glomski, K., Monette, S., Manova, K., De Strooper, B., Saftig, P., Blobel, C.P., Deletion of Adam10 in endothelial cells leads to defects in organ-specific vascular structures. Blood 118:4 (2011), 1163–1174.
    • (2011) Blood , vol.118 , Issue.4 , pp. 1163-1174
    • Glomski, K.1    Monette, S.2    Manova, K.3    De Strooper, B.4    Saftig, P.5    Blobel, C.P.6
  • 199
    • 84900541092 scopus 로고    scopus 로고
    • α-Hemolysin, not Panton-Valentine leukocidin, impacts rabbit mortality from severe sepsis with methicillin-resistant Staphylococcus aureus osteomyelitis
    • Cremieux, A.C., Saleh-Mghir, A.C., Danel, F., Couzon, O., Dumitrescu, T., Lilin, C., Perronne, J., Etienne, G., Lina, Vandenesch, F., α-Hemolysin, not Panton-Valentine leukocidin, impacts rabbit mortality from severe sepsis with methicillin-resistant Staphylococcus aureus osteomyelitis. J. Infect. Dis. 209:11 (2014), 1773–1780.
    • (2014) J. Infect. Dis. , vol.209 , Issue.11 , pp. 1773-1780
    • Cremieux, A.C.1    Saleh-Mghir, A.C.2    Danel, F.3    Couzon, O.4    Dumitrescu, T.5    Lilin, C.6    Perronne, J.7    Etienne, G.8    Lina9    Vandenesch, F.10
  • 201
    • 84983488777 scopus 로고    scopus 로고
    • Synergistic action of Staphylococcus aureus alpha-toxin on platelets and myeloid lineage cells contributes to lethal sepsis
    • Powers, M.E., Becker, R.E., Sailer, A., Turner, J.R., Bubeck Wardenburg, J., Synergistic action of Staphylococcus aureus alpha-toxin on platelets and myeloid lineage cells contributes to lethal sepsis. Cell Host Microbe 17:6 (2015), 775–787.
    • (2015) Cell Host Microbe , vol.17 , Issue.6 , pp. 775-787
    • Powers, M.E.1    Becker, R.E.2    Sailer, A.3    Turner, J.R.4    Bubeck Wardenburg, J.5
  • 203
    • 67650079244 scopus 로고    scopus 로고
    • Anti-alpha-hemolysin monoclonal antibodies mediate protection against Staphylococcus aureus pneumonia
    • Ragle, B.E., Bubeck Wardenburg, J., Anti-alpha-hemolysin monoclonal antibodies mediate protection against Staphylococcus aureus pneumonia. Infect. Immun. 77:7 (2009), 2712–2718.
    • (2009) Infect. Immun. , vol.77 , Issue.7 , pp. 2712-2718
    • Ragle, B.E.1    Bubeck Wardenburg, J.2
  • 204
    • 73849113321 scopus 로고    scopus 로고
    • Prevention and treatment of Staphylococcus aureus pneumonia with a β-cyclodextrin derivative
    • Ragle, B.E., Karginov, V.A., Bubeck Wardenburg, J., Prevention and treatment of Staphylococcus aureus pneumonia with a β-cyclodextrin derivative. Antimicrob. Agents Chemother. 54:1 (2010), 298–304.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.1 , pp. 298-304
    • Ragle, B.E.1    Karginov, V.A.2    Bubeck Wardenburg, J.3
  • 205
    • 84992365476 scopus 로고    scopus 로고
    • Improved protection in a rabbit model of community-associated methicillin-resistant Staphylococcus aureus necrotizing pneumonia upon neutralization of leukocidins in addition to α-hemolysin
    • Diep, B.A., Le, V.T., Visram, Z.C., Rouha, H., Stulik, L., Dip, E.C., Nagy, G., Nagy, E., Improved protection in a rabbit model of community-associated methicillin-resistant Staphylococcus aureus necrotizing pneumonia upon neutralization of leukocidins in addition to α-hemolysin. Antimicrob. Agents Chemother. 60:10 (2016), 6333–6340.
    • (2016) Antimicrob. Agents Chemother. , vol.60 , Issue.10 , pp. 6333-6340
    • Diep, B.A.1    Le, V.T.2    Visram, Z.C.3    Rouha, H.4    Stulik, L.5    Dip, E.C.6    Nagy, G.7    Nagy, E.8


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