메뉴 건너뛰기




Volumn 57, Issue 2, 2014, Pages 310-316

Membrane pore formation by human complement: Functional importance of the transmembrane β-hairpin (TMH) segments of C8α and C9

Author keywords

C8; C9; Complement; MACPF; Membrane attack complex; Perfringolysin O

Indexed keywords

CHIMERIC PROTEIN; CLOSTRIDIUM PERFRINGENS TOXIN; COMPLEMENT COMPONENT C8; COMPLEMENT COMPONENT C8ALPHA; COMPLEMENT COMPONENT C9; ENTEROPEPTIDASE; UNCLASSIFIED DRUG;

EID: 84887524393     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2013.10.007     Document Type: Article
Times cited : (7)

References (33)
  • 1
    • 84858967104 scopus 로고    scopus 로고
    • Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC)
    • Aleshin A.E., Schraufstatter I.U., Stec B., Bankston L.A., Liddington R.C., DiScipio R.G. Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC). J. Biol. Chem. 2012, 287:10210-10222.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10210-10222
    • Aleshin, A.E.1    Schraufstatter, I.U.2    Stec, B.3    Bankston, L.A.4    Liddington, R.C.5    DiScipio, R.G.6
  • 2
    • 15444378399 scopus 로고    scopus 로고
    • Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy
    • Dang T.X., Hotze E.M., Rouiller I., Tweten R.K., Wilson-Kubalek E.M. Prepore to pore transition of a cholesterol-dependent cytolysin visualized by electron microscopy. J. Struct. Biol. 2005, 150:100-108.
    • (2005) J. Struct. Biol. , vol.150 , pp. 100-108
    • Dang, T.X.1    Hotze, E.M.2    Rouiller, I.3    Tweten, R.K.4    Wilson-Kubalek, E.M.5
  • 3
    • 0026349236 scopus 로고
    • The relationship between polymerization of complement component C9 and membrane channel formation
    • DiScipio R.G. The relationship between polymerization of complement component C9 and membrane channel formation. J. Immunol. 1991, 147:4239-4247.
    • (1991) J. Immunol. , vol.147 , pp. 4239-4247
    • DiScipio, R.G.1
  • 4
    • 0032868186 scopus 로고    scopus 로고
    • The architectural transition of human complement component C9 to poly (C9)
    • DiScipio R.G., Berlin C. The architectural transition of human complement component C9 to poly (C9). Mol. Immunol. 1999, 36:575-585.
    • (1999) Mol. Immunol. , vol.36 , pp. 575-585
    • DiScipio, R.G.1    Berlin, C.2
  • 5
    • 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 M.A., Tweten R.K. Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins. Curr. Opin. Struct. Biol. 2012, 22:342-349.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 6
    • 0028331322 scopus 로고
    • The membrane attack complex of complement. Assembly, structure and cytotoxic activity
    • Esser A.F. The membrane attack complex of complement. Assembly, structure and cytotoxic activity. Toxicology 1994, 87:229-247.
    • (1994) Toxicology , vol.87 , pp. 229-247
    • Esser, A.F.1
  • 7
    • 34548670476 scopus 로고    scopus 로고
    • Structure of C8α-MACPF reveals mechanism of membrane attack in complement immune defense
    • Hadders M.A., Beringer D.X., Gros P. Structure of C8α-MACPF reveals mechanism of membrane attack in complement immune defense. Science 2007, 317:1552-1554.
    • (2007) Science , vol.317 , pp. 1552-1554
    • Hadders, M.A.1    Beringer, D.X.2    Gros, P.3
  • 8
    • 0029060839 scopus 로고
    • Structure of the human C7 gene and comparison with the C6, C8A, C8B, and C9 genes
    • Hobart M.J., Fernie B.A., DiScipio R.G. Structure of the human C7 gene and comparison with the C6, C8A, C8B, and C9 genes. J. Immunol. 1995, 154:5188-5194.
    • (1995) J. Immunol. , vol.154 , pp. 5188-5194
    • Hobart, M.J.1    Fernie, B.A.2    DiScipio, R.G.3
  • 9
    • 84857650341 scopus 로고    scopus 로고
    • Membrane assembly of the cholesterol-dependent cytolysin pore complex
    • Hotze E.M., Tweten R.K. Membrane assembly of the cholesterol-dependent cytolysin pore complex. Biochim. Biophys. Acta 2012, 1818:1028-1038.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1028-1038
    • Hotze, E.M.1    Tweten, R.K.2
  • 10
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate
    • Hotze E.M., Wilson-Kubalek E.M., Rossjohn J., Parker M.W., Johnson A.E., Tweten R.K. Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate. J. Biol. Chem. 2001, 276:8261-8268.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8261-8268
    • Hotze, E.M.1    Wilson-Kubalek, E.M.2    Rossjohn, J.3    Parker, M.W.4    Johnson, A.E.5    Tweten, R.K.6
  • 11
    • 0037192791 scopus 로고    scopus 로고
    • Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin
    • Hotze E.M., Heuck A.P., Czajkowsky D.M., Shao Z., Johnson A.E., Tweten R.K. Monomer-monomer interactions drive the prepore to pore conversion of a beta-barrel-forming cholesterol-dependent cytolysin. J. Biol. Chem. 2002, 277:11597-11605.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11597-11605
    • Hotze, E.M.1    Heuck, A.P.2    Czajkowsky, D.M.3    Shao, Z.4    Johnson, A.E.5    Tweten, R.K.6
  • 12
    • 0020366320 scopus 로고
    • Photolabeling of a hydrophobic domain of the ninth component of human complement
    • Ishida B., Wisnieski B.J., Lavine C.H., Esser A.F. Photolabeling of a hydrophobic domain of the ninth component of human complement. J. Biol. Chem. 1982, 257:10551-10553.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10551-10553
    • Ishida, B.1    Wisnieski, B.J.2    Lavine, C.H.3    Esser, A.F.4
  • 14
    • 79955953166 scopus 로고    scopus 로고
    • Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement
    • Lovelace L.L., Cooper C.L., Sodetz J.M., Lebioda L. Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement. J. Biol. Chem. 2011, 286:17585-17592.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17585-17592
    • Lovelace, L.L.1    Cooper, C.L.2    Sodetz, J.M.3    Lebioda, L.4
  • 15
    • 0023890664 scopus 로고
    • Molecular organization and function of the complement system
    • Müller-Eberhard H.J. Molecular organization and function of the complement system. Annu. Rev. Biochem. 1988, 57:321-347.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 321-347
    • Müller-Eberhard, H.J.1
  • 16
    • 0023664828 scopus 로고
    • The eighth component of human complement: evidence that it is an oligomeric serum protein assembled from products of three different genes
    • Ng S.C., Rao A.G., Howard O.M., Sodetz J.M. The eighth component of human complement: evidence that it is an oligomeric serum protein assembled from products of three different genes. Biochemistry 1987, 26:5229-5233.
    • (1987) Biochemistry , vol.26 , pp. 5229-5233
    • Ng, S.C.1    Rao, A.G.2    Howard, O.M.3    Sodetz, J.M.4
  • 17
    • 0024995537 scopus 로고
    • Localization and molecular modelling of the membrane-inserted domain of the ninth component of human complement and perforin
    • Peitsch M.C., Amiguet P., Guy R., Brunner J., Maizel J.V., Tschopp J. Localization and molecular modelling of the membrane-inserted domain of the ninth component of human complement and perforin. Mol. Immunol. 1990, 27:589-602.
    • (1990) Mol. Immunol. , vol.27 , pp. 589-602
    • Peitsch, M.C.1    Amiguet, P.2    Guy, R.3    Brunner, J.4    Maizel, J.V.5    Tschopp, J.6
  • 18
    • 34247577498 scopus 로고    scopus 로고
    • Delivering the kiss of death: progress on understanding how perforin works
    • Pipkin M.E., Lieberman J. Delivering the kiss of death: progress on understanding how perforin works. Curr. Opin. Immunol. 2007, 19:301-308.
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 301-308
    • Pipkin, M.E.1    Lieberman, J.2
  • 19
    • 0002706313 scopus 로고    scopus 로고
    • Proteins of the membrane attack complex
    • Marcel Dekker, New York, J.E. Volanakis, M.M. Frank (Eds.)
    • Plumb M.E., Sodetz J.M. Proteins of the membrane attack complex. The Human Complement System in Health and Disease 1998, 119-148. Marcel Dekker, New York. J.E. Volanakis, M.M. Frank (Eds.).
    • (1998) The Human Complement System in Health and Disease , pp. 119-148
    • Plumb, M.E.1    Sodetz, J.M.2
  • 20
    • 0033576666 scopus 로고    scopus 로고
    • Chlamydial homologues of the MACPF (MAC/perforin) domain
    • Ponting C.P. Chlamydial homologues of the MACPF (MAC/perforin) domain. Curr. Biol. 1999, 9:R911-R913.
    • (1999) Curr. Biol. , vol.9
    • Ponting, C.P.1
  • 21
    • 3543016107 scopus 로고    scopus 로고
    • Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment
    • Ramachandran R., Tweten R.K., Johnson A.E. Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment. Nat. Struct. Mol. Biol. 2004, 11:697-705.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 697-705
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 23
    • 77950626562 scopus 로고    scopus 로고
    • Topology of the membrane-bound form of complement protein C9 probed by glycosylation mapping, anti-peptide antibody binding, and disulfide modification
    • Rossi V., Wang Y., Esser A.F. Topology of the membrane-bound form of complement protein C9 probed by glycosylation mapping, anti-peptide antibody binding, and disulfide modification. Mol. Immunol. 2010, 47:1553-1560.
    • (2010) Mol. Immunol. , vol.47 , pp. 1553-1560
    • Rossi, V.1    Wang, Y.2    Esser, A.F.3
  • 24
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins
    • Shatursky O., Heuck A.P., Shepard L.A., Rossjohn J., Parker M.W., Johnson A.E., Tweten R.K. The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 1999, 99:293-299.
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 25
    • 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 L.A., Heuck A.P., Hamman B.D., Rossjohn J., Parker M.W., Ryan K.R., Johnson A.E., Tweten R.K. 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 1998, 37:14563-14574.
    • (1998) Biochemistry , vol.37 , pp. 14563-14574
    • Shepard, L.A.1    Heuck, A.P.2    Hamman, B.D.3    Rossjohn, J.4    Parker, M.W.5    Ryan, K.R.6    Johnson, A.E.7    Tweten, R.K.8
  • 26
    • 0034702810 scopus 로고    scopus 로고
    • The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins
    • Shepard L.A., Shatursky O., Johnson A.E., Tweten R.K. The mechanism of pore assembly for a cholesterol-dependent cytolysin: formation of a large prepore complex precedes the insertion of the transmembrane beta-hairpins. Biochemistry 2000, 39:10284-10293.
    • (2000) Biochemistry , vol.39 , pp. 10284-10293
    • Shepard, L.A.1    Shatursky, O.2    Johnson, A.E.3    Tweten, R.K.4
  • 27
    • 33645971303 scopus 로고    scopus 로고
    • Functional studies of the MACPF domain of human complement protein C8alpha reveal sites for simultaneous binding of C8beta, C8gamma, and C9
    • Slade D.J., Chiswell B., Sodetz J.M. Functional studies of the MACPF domain of human complement protein C8alpha reveal sites for simultaneous binding of C8beta, C8gamma, and C9. Biochemistry 2006, 45:5290-5296.
    • (2006) Biochemistry , vol.45 , pp. 5290-5296
    • Slade, D.J.1    Chiswell, B.2    Sodetz, J.M.3
  • 28
    • 43049094015 scopus 로고    scopus 로고
    • Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit
    • Slade D.J., Lovelace L.L., Chruszcz M., Minor W., Lebioda L., Sodetz J.M. Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit. J. Mol. Biol. 2008, 379:331-342.
    • (2008) J. Mol. Biol. , vol.379 , pp. 331-342
    • Slade, D.J.1    Lovelace, L.L.2    Chruszcz, M.3    Minor, W.4    Lebioda, L.5    Sodetz, J.M.6
  • 29
    • 0019297965 scopus 로고
    • The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure
    • Steckel E.W., York R.G., Monahan J.B., Sodetz J.M. The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure. J. Biol. Chem. 1980, 255:11997-12005.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11997-12005
    • Steckel, E.W.1    York, R.G.2    Monahan, J.B.3    Sodetz, J.M.4
  • 30
    • 0020623026 scopus 로고
    • Evidence of direct insertion of terminal complement proteins into cell membrane bilayers during cytolysis. Labeling by a photosensitive membrane probe reveals a major role for the eighth and ninth components
    • Steckel E.W., Welbaum B.E., Sodetz J.M. Evidence of direct insertion of terminal complement proteins into cell membrane bilayers during cytolysis. Labeling by a photosensitive membrane probe reveals a major role for the eighth and ninth components. J. Biol. Chem. 1983, 258:4318-4324.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4318-4324
    • Steckel, E.W.1    Welbaum, B.E.2    Sodetz, J.M.3
  • 31
    • 0023816534 scopus 로고
    • Cloning and expression in Escherichia coli of the perfringolysin O (theta-toxin) gene from Clostridium perfringens and characterization of the gene product
    • Tweten R.K. Cloning and expression in Escherichia coli of the perfringolysin O (theta-toxin) gene from Clostridium perfringens and characterization of the gene product. Infect. Immun. 1988, 56:3228-3234.
    • (1988) Infect. Immun. , vol.56 , pp. 3228-3234
    • Tweten, R.K.1
  • 32
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • Tweten R.K. Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect. Immun. 2005, 73:6199-6209.
    • (2005) Infect. Immun. , vol.73 , pp. 6199-6209
    • Tweten, R.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.