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Volumn 109, Issue 44, 2012, Pages

Triggering the measles virus membrane fusion machinery

Author keywords

Paramyxovirus entry; Protein refolding; Virus envelope glycoproteins

Indexed keywords

ALANINE; DIMER; HYBRID PROTEIN; TETRAMER;

EID: 84868147366     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1210925109     Document Type: Article
Times cited : (58)

References (43)
  • 1
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: Lessons from paramyxovirus F
    • Lamb RA, Jardetzky TS (2007) Structural basis of viral invasion: Lessons from paramyxovirus F. Curr Opin Struct Biol 17:427-436.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 2
    • 0031303377 scopus 로고    scopus 로고
    • Functional chimeric HN glycoproteins derived from Newcastle disease virus and human parainfluenza virus-3
    • Deng R, Mirza AM, Mahon PJ, Iorio RM (1997) Functional chimeric HN glycoproteins derived from Newcastle disease virus and human parainfluenza virus-3. Arch Virol Suppl 13:115-130.
    • (1997) Arch Virol Suppl , vol.13 , pp. 115-130
    • Deng, R.1    Mirza, A.M.2    Mahon, P.J.3    Iorio, R.M.4
  • 3
    • 0029006480 scopus 로고
    • Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike
    • Deng R, Wang Z, Mirza AM, Iorio RM (1995) Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike. Virology 209:457-469.
    • (1995) Virology , vol.209 , pp. 457-469
    • Deng, R.1    Wang, Z.2    Mirza, A.M.3    Iorio, R.M.4
  • 4
    • 30344467852 scopus 로고    scopus 로고
    • Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion
    • Melanson VR, Iorio RM (2006) Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion. J Virol 80:623-633.
    • (2006) J Virol , vol.80 , pp. 623-633
    • Melanson, V.R.1    Iorio, R.M.2
  • 5
    • 0029836433 scopus 로고    scopus 로고
    • Functional interaction of paramyxovirus glycoproteins: Identification of a domain in Sendai virus HN which promotes cell fusion
    • Tanabayashi K, Compans RW (1996) Functional interaction of paramyxovirus glycoproteins: Identification of a domain in Sendai virus HN which promotes cell fusion. J Virol 70:6112-6118.
    • (1996) J Virol , vol.70 , pp. 6112-6118
    • Tanabayashi, K.1    Compans, R.W.2
  • 6
    • 70349747076 scopus 로고    scopus 로고
    • Probing the spatial organization of measles virus fusion complexes
    • Paal T, et al. (2009) Probing the spatial organization of measles virus fusion complexes. J Virol 83:10480-10493.
    • (2009) J Virol , vol.83 , pp. 10480-10493
    • Paal, T.1
  • 7
    • 47749143663 scopus 로고    scopus 로고
    • Functional interaction between paramyxovirus fusion and attachment proteins
    • Lee JK, et al. (2008) Functional interaction between paramyxovirus fusion and attachment proteins. J Biol Chem 283:16561-16572.
    • (2008) J Biol Chem , vol.283 , pp. 16561-16572
    • Lee, J.K.1
  • 8
    • 78049490873 scopus 로고    scopus 로고
    • Blue native PAGE and biomolecular complementation reveal a tetrameric or higher-order oligomer organization of the physiological measles virus attachment protein H
    • Brindley MA, Plemper RK (2010) Blue native PAGE and biomolecular complementation reveal a tetrameric or higher-order oligomer organization of the physiological measles virus attachment protein H. J Virol 84:12174-12184.
    • (2010) J Virol , vol.84 , pp. 12174-12184
    • Brindley, M.A.1    Plemper, R.K.2
  • 9
    • 79551638780 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM
    • Hashiguchi T, et al. (2011) Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM. Nat Struct Mol Biol 18:135-141.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 135-141
    • Hashiguchi, T.1
  • 10
    • 36849029202 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin
    • Colf LA, Juo ZS, Garcia KC (2007) Structure of the measles virus hemagglutinin. Nat Struct Mol Biol 14:1227-1228.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1227-1228
    • Colf, L.A.1    Juo, Z.S.2    Garcia, K.C.3
  • 11
    • 77449145697 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin bound to the CD46 receptor
    • Santiago C, Celma ML, Stehle T, Casasnovas JM (2010) Structure of the measles virus hemagglutinin bound to the CD46 receptor. Nat Struct Mol Biol 17:124-129.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 124-129
    • Santiago, C.1    Celma, M.L.2    Stehle, T.3    Casasnovas, J.M.4
  • 12
    • 37649006255 scopus 로고    scopus 로고
    • Crystal structure of measles virus hemagglutinin provides insight into effective vaccines
    • Hashiguchi T, et al. (2007) Crystal structure of measles virus hemagglutinin provides insight into effective vaccines. Proc Natl Acad Sci USA 104:19535-19540.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19535-19540
    • Hashiguchi, T.1
  • 13
    • 80052315535 scopus 로고    scopus 로고
    • Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus
    • Noyce RS, et al. (2011) Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus. PLoS Pathog 7:e1002240.
    • (2011) PLoS Pathog , vol.7
    • Noyce, R.S.1
  • 14
    • 84868140783 scopus 로고    scopus 로고
    • Measles virus hemagglutinin: Structural insights into cell entry and measles vaccine
    • Hashiguchi T, Maenaka K, Yanagi Y (2011) Measles virus hemagglutinin: Structural insights into cell entry and measles vaccine. Front Microbiol 2:247.
    • (2011) Front Microbiol , vol.2 , pp. 247
    • Hashiguchi, T.1    Maenaka, K.2    Yanagi, Y.3
  • 15
    • 0035941299 scopus 로고    scopus 로고
    • Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum
    • Plemper RK, Hammond AL, Cattaneo R (2001) Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum. J Biol Chem 276:44239-44246.
    • (2001) J Biol Chem , vol.276 , pp. 44239-44246
    • Plemper, R.K.1    Hammond, A.L.2    Cattaneo, R.3
  • 16
    • 35348888403 scopus 로고    scopus 로고
    • Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein
    • Corey EA, Iorio RM (2007) Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein. J Virol 81:9900-9910.
    • (2007) J Virol , vol.81 , pp. 9900-9910
    • Corey, E.A.1    Iorio, R.M.2
  • 17
    • 79959835596 scopus 로고    scopus 로고
    • Structural and mechanistic studies of measles virus illuminate paramyxovirus entry
    • Plemper RK, Brindley MA, Iorio RM (2011) Structural and mechanistic studies of measles virus illuminate paramyxovirus entry. PLoS Pathog 7:e1002058.
    • (2011) PLoS Pathog , vol.7
    • Plemper, R.K.1    Brindley, M.A.2    Iorio, R.M.3
  • 18
    • 80052564183 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus hemagglutininneuraminidase (HN) ectodomain reveals a four-helix bundle stalk
    • Yuan P, et al. (2011) Structure of the Newcastle disease virus hemagglutininneuraminidase (HN) ectodomain reveals a four-helix bundle stalk. Proc Natl Acad Sci USA 108:14920-14925.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14920-14925
    • Yuan, P.1
  • 19
    • 84855845971 scopus 로고    scopus 로고
    • Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion
    • Bose S, et al. (2011) Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion. J Virol 85:12855-12866.
    • (2011) J Virol , vol.85 , pp. 12855-12866
    • Bose, S.1
  • 20
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemagglutininneuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan P, et al. (2005) Structural studies of the parainfluenza virus 5 hemagglutininneuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13: 803-815.
    • (2005) Structure , vol.13 , pp. 803-815
    • Yuan, P.1
  • 21
    • 0033934723 scopus 로고    scopus 로고
    • Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization
    • Plemper RK, Hammond AL, Cattaneo R (2000) Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization. J Virol 74:6485-6493.
    • (2000) J Virol , vol.74 , pp. 6485-6493
    • Plemper, R.K.1    Hammond, A.L.2    Cattaneo, R.3
  • 22
    • 79954417748 scopus 로고    scopus 로고
    • Disulfide bonds in ER protein folding and homeostasis
    • Feige MJ, Hendershot LM (2011) Disulfide bonds in ER protein folding and homeostasis. Curr Opin Cell Biol 23:167-175.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 167-175
    • Feige, M.J.1    Hendershot, L.M.2
  • 23
    • 0033616528 scopus 로고    scopus 로고
    • Structural and functional studies of the measles virus hemagglutinin: Identification of a novel site required for CD46 interaction
    • Patterson JB, Scheiflinger F, Manchester M, Yilma T, Oldstone MB (1999) Structural and functional studies of the measles virus hemagglutinin: Identification of a novel site required for CD46 interaction. Virology 256:142-151.
    • (1999) Virology , vol.256 , pp. 142-151
    • Patterson, J.B.1    Scheiflinger, F.2    Manchester, M.3    Yilma, T.4    Oldstone, M.B.5
  • 24
    • 57049160334 scopus 로고    scopus 로고
    • Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein
    • Corey EA, Iorio RM (2009) Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein. Virology 383:1-5.
    • (2009) Virology , vol.383 , pp. 1-5
    • Corey, E.A.1    Iorio, R.M.2
  • 25
    • 0035121424 scopus 로고    scopus 로고
    • Single-chain antibody displayed on a recombinant measles virus confers entry through the tumor-associated carcinoembryonic antigen
    • Hammond AL, et al. (2001) Single-chain antibody displayed on a recombinant measles virus confers entry through the tumor-associated carcinoembryonic antigen. J Virol 75:2087-2096.
    • (2001) J Virol , vol.75 , pp. 2087-2096
    • Hammond, A.L.1
  • 26
    • 48849107198 scopus 로고    scopus 로고
    • Solubilization of membrane protein complexes for blue native PAGE
    • Reisinger V, Eichacker LA (2008) Solubilization of membrane protein complexes for blue native PAGE. J Proteomics 71:277-283.
    • (2008) J Proteomics , vol.71 , pp. 277-283
    • Reisinger, V.1    Eichacker, L.A.2
  • 27
    • 79951857737 scopus 로고    scopus 로고
    • Metal ion stimulators of PDE5 cause similar conformational changes in the enzyme as does cGMP or sildenafil
    • Corbin JD, et al. (2011) Metal ion stimulators of PDE5 cause similar conformational changes in the enzyme as does cGMP or sildenafil. Cell Signal 23:778-784.
    • (2011) Cell Signal , vol.23 , pp. 778-784
    • Corbin, J.D.1
  • 28
    • 76349088032 scopus 로고    scopus 로고
    • Biochemical evidence for conformational changes in the cross-talk between adenylation and peptidyl-carrier protein domains of nonribosomal peptide synthetases
    • Zettler J, Mootz HD (2010) Biochemical evidence for conformational changes in the cross-talk between adenylation and peptidyl-carrier protein domains of nonribosomal peptide synthetases. FEBS J 277:1159-1171.
    • (2010) FEBS J , vol.277 , pp. 1159-1171
    • Zettler, J.1    Mootz, H.D.2
  • 29
    • 33845212315 scopus 로고    scopus 로고
    • Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy
    • Connolly SA, Leser GP, Yin HS, Jardetzky TS, Lamb RA (2006) Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy. Proc Natl Acad Sci USA 103:17903-17908.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17903-17908
    • Connolly, S.A.1    Leser, G.P.2    Yin, H.S.3    Jardetzky, T.S.4    Lamb, R.A.5
  • 30
    • 84860844283 scopus 로고    scopus 로고
    • Structural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusion
    • Ader N, et al. (2012) Structural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusion. J Biol Chem 287:16324-16334.
    • (2012) J Biol Chem , vol.287 , pp. 16324-16334
    • Ader, N.1
  • 31
    • 0025039308 scopus 로고
    • Contribution of measles virus fusion protein in protective immunity: Anti-F monoclonal antibodies neutralize virus infectivity and protect mice against challenge
    • Malvoisin E, Wild F (1990) Contribution of measles virus fusion protein in protective immunity: Anti-F monoclonal antibodies neutralize virus infectivity and protect mice against challenge. J Virol 64:5160-5162.
    • (1990) J Virol , vol.64 , pp. 5160-5162
    • Malvoisin, E.1    Wild, F.2
  • 32
    • 0020612689 scopus 로고
    • Monoclonal antibodies against five structural components of measles virus. I. Characterization of antigenic determinants on nine strains of measles virus
    • Sheshberadaran H, Chen SN, Norrby E (1983) Monoclonal antibodies against five structural components of measles virus. I. Characterization of antigenic determinants on nine strains of measles virus. Virology 128:341-353.
    • (1983) Virology , vol.128 , pp. 341-353
    • Sheshberadaran, H.1    Chen, S.N.2    Norrby, E.3
  • 33
    • 79959557008 scopus 로고    scopus 로고
    • Monitoring viral-mediated membrane fusion using fluorescent reporter methods
    • Kondo N, Miyauchi K, Matsuda Z (2011) Monitoring viral-mediated membrane fusion using fluorescent reporter methods. Curr Protoc Cell Biol, Chapter 26:26.9.1-26.9.9.
    • (2011) Curr Protoc Cell Biol, Chapter , vol.26 , pp. 2691-2699
    • Kondo, N.1    Miyauchi, K.2    Matsuda, Z.3
  • 34
    • 55549116002 scopus 로고    scopus 로고
    • Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor binding
    • Bishop KA, et al. (2008) Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor binding. J Virol 82:11398-11409.
    • (2008) J Virol , vol.82 , pp. 11398-11409
    • Bishop, K.A.1
  • 35
    • 59449099994 scopus 로고    scopus 로고
    • A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F)
    • Aguilar HC, et al. (2009) A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F). J Biol Chem 284:1628-1635.
    • (2009) J Biol Chem , vol.284 , pp. 1628-1635
    • Aguilar, H.C.1
  • 36
    • 48249113696 scopus 로고    scopus 로고
    • Host cell recognition by the henipaviruses: Crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3
    • Xu K, et al. (2008) Host cell recognition by the henipaviruses: Crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proc Natl Acad Sci USA 105:9953-9958.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9953-9958
    • Xu, K.1
  • 37
    • 84855673964 scopus 로고    scopus 로고
    • Cell entry of enveloped viruses
    • Plemper RK (2011) Cell entry of enveloped viruses. Curr Opin Virol 1:92-100.
    • (2011) Curr Opin Virol , vol.1 , pp. 92-100
    • Plemper, R.K.1
  • 38
    • 79960435702 scopus 로고    scopus 로고
    • Membrane fusion mediated by human immunodeficiency virus envelope glycoprotein
    • Melikyan GB (2011) Membrane fusion mediated by human immunodeficiency virus envelope glycoprotein. Curr Top Membr 68:81-106.
    • (2011) Curr Top Membr , vol.68 , pp. 81-106
    • Melikyan, G.B.1
  • 39
    • 84855270854 scopus 로고    scopus 로고
    • Spring-loaded model revisited: Paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein
    • Porotto M, et al. (2011) Spring-loaded model revisited: Paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein. J Virol 85:12867-12880.
    • (2011) J Virol , vol.85 , pp. 12867-12880
    • Porotto, M.1
  • 40
    • 0035046933 scopus 로고    scopus 로고
    • Measles viruses on throat swabs from measles patients use signaling lymphocytic activation molecule (CDw150) but not CD46 as a cellular receptor
    • Ono N, et al. (2001) Measles viruses on throat swabs from measles patients use signaling lymphocytic activation molecule (CDw150) but not CD46 as a cellular receptor. J Virol 75:4399-4401.
    • (2001) J Virol , vol.75 , pp. 4399-4401
    • Ono, N.1
  • 41
    • 0029084129 scopus 로고
    • Non-replicating vaccinia vector efficiently expresses bacteriophage T7 RNA polymerase
    • Sutter G, Ohlmann M, Erfle V (1995) Non-replicating vaccinia vector efficiently expresses bacteriophage T7 RNA polymerase. FEBS Lett 371:9-12.
    • (1995) FEBS Lett , vol.371 , pp. 9-12
    • Sutter, G.1    Ohlmann, M.2    Erfle, V.3
  • 42
    • 0031907095 scopus 로고    scopus 로고
    • Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence
    • Cathomen T, Naim HY, Cattaneo R (1998) Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence. J Virol 72:1224-1234.
    • (1998) J Virol , vol.72 , pp. 1224-1234
    • Cathomen, T.1    Naim, H.Y.2    Cattaneo, R.3
  • 43
    • 0035173204 scopus 로고    scopus 로고
    • Multiple tandem epitope tagging for enhanced detection of protein expressed in mammalian cells
    • Zhang L, Hernan R, Brizzard B (2001) Multiple tandem epitope tagging for enhanced detection of protein expressed in mammalian cells. Mol Biotechnol 19:313-321.
    • (2001) Mol Biotechnol , vol.19 , pp. 313-321
    • Zhang, L.1    Hernan, R.2    Brizzard, B.3


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