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Volumn 288, Issue 12, 2013, Pages 8085-8091

Mutations in the putative dimer-dimer interfaces of the measles virus hemagglutinin head domain affect membrane fusion triggering

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE EXPRESSION; CELLULAR RECEPTORS; CONFORMATIONAL SHIFTS; DIMER-DIMER INTERACTION; MEMBRANE FUSION; RECEPTOR BINDING; TRANSMEMBRANE REGIONS; VIRAL ENVELOPE PROTEINS;

EID: 84875435272     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.427609     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 34547601896 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • (Knipe, D. M., Howley, P. M., Griffin, D. E., Lamb, R. A., Martin, M. A., Roizman, B., and Straus, S. E., eds) 5th Ed., Lippincott Williams & Wilkins, Philadelphia
    • Lamb, R. A., and Parks, G. D. (2007) Paramyxoviridae: The viruses and their replication, in Fields Virology (Knipe, D. M., Howley, P. M., Griffin, D. E., Lamb, R. A., Martin, M. A., Roizman, B., and Straus, S. E., eds) 5th Ed., pp. 1449-1496, Lippincott Williams & Wilkins, Philadelphia
    • (2007) Fields Virology , pp. 1449-1496
    • Lamb, R.A.1    Parks, G.D.2
  • 2
    • 41549166734 scopus 로고    scopus 로고
    • Paramyxoviruses. Different receptorsdifferent mechanisms of fusion
    • Iorio, R. M., and Mahon, P. J. (2008) Paramyxoviruses. Different receptorsdifferent mechanisms of fusion. Trends. Microbiol. 16, 135-137
    • (2008) Trends. Microbiol. , vol.16 , pp. 135-137
    • Iorio, R.M.1    Mahon, P.J.2
  • 3
    • 71949123985 scopus 로고    scopus 로고
    • Viral entry mechanisms. The increasing diversity of paramyxovirus entry
    • Smith, E. C., Popa, A., Chang, A., Masante, C., and Dutch, R. E. (2009) Viral entry mechanisms. The increasing diversity of paramyxovirus entry. FEBS J. 276, 7217-7227
    • (2009) FEBS J. , vol.276 , pp. 7217-7227
    • Smith, E.C.1    Popa, A.2    Chang, A.3    Masante, C.4    Dutch, R.E.5
  • 4
    • 79959835596 scopus 로고    scopus 로고
    • Structural and mechanistic studies of measles virus illuminate paramyxovirus entry
    • Plemper, R. K., Brindley, M. A., and Iorio, R. M. (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
  • 5
    • 79960918320 scopus 로고    scopus 로고
    • Modes of paramyxovirus fusion. A Henipavirus perspective
    • Lee, B., and Ataman, Z. A. (2011) Modes of paramyxovirus fusion. A Henipavirus perspective. Trends. Microbiol. 19, 389-399
    • (2011) Trends. Microbiol. , vol.19 , pp. 389-399
    • Lee, B.1    Ataman, Z.A.2
  • 6
    • 70350277403 scopus 로고    scopus 로고
    • Bimolecular complementation of paramyxovirus fusion and hemagglutinin- neuraminidase proteins enhances fusion. Implications for the mechanism of fusion triggering
    • Connolly, S. A., Leser, G. P., Jardetzky, T. S., and Lamb, R. A. (2009) Bimolecular complementation of paramyxovirus fusion and hemagglutinin- neuraminidase proteins enhances fusion. Implications for the mechanism of fusion triggering. J. Virol. 83, 10857-10868
    • (2009) J. Virol. , vol.83 , pp. 10857-10868
    • Connolly, S.A.1    Leser, G.P.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 7
    • 84869027005 scopus 로고    scopus 로고
    • Membrane fusion triggering. Three modules with different structure and function in the upper half of the measles virus attachment protein stalk
    • Navaratnarajah, C. K., Negi, S., Braun, W., and Cattaneo, R. (2012) Membrane fusion triggering. Three modules with different structure and function in the upper half of the measles virus attachment protein stalk. J. Biol. Chem. 287, 38543-38551
    • (2012) J. Biol. Chem. , vol.287 , pp. 38543-38551
    • Navaratnarajah, C.K.1    Negi, S.2    Braun, W.3    Cattaneo, R.4
  • 8
    • 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., Welch, B. D., Kors, C. A., Yuan, P., Jardetzky, T. S., and Lamb, R. A. (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    Welch, B.D.2    Kors, C.A.3    Yuan, P.4    Jardetzky, T.S.5    Lamb, R.A.6
  • 9
    • 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
    • DOI 10.1128/JVI.80.2.623-633.2006
    • Melanson, V. R., and Iorio, R. M. (2006) Addition of N-glycans in the stalk of the Newcastle disease virusHNprotein blocks its interaction with the F protein and prevents fusion. J. Virol. 80, 623-633 (Pubitemid 43062875)
    • (2006) Journal of Virology , vol.80 , Issue.2 , pp. 623-633
    • Melanson, V.R.1    Iorio, R.M.2
  • 10
    • 0029836433 scopus 로고    scopus 로고
    • Functional interaction of paramyxovirus glycoproteins: Identification of a domain in Sendai virus HN which promotes cell fusion
    • Tanabayashi, K., and Compans, R. W. (1996) Functional interaction of paramyxovirus glycoproteins. Identification of a domain in Sendai virus HN which promotes cell fusion. J. Virol. 70, 6112-6118 (Pubitemid 26266827)
    • (1996) Journal of Virology , vol.70 , Issue.9 , pp. 6112-6118
    • Tanabayashi, K.1    Compans, R.W.2
  • 11
    • 1642430785 scopus 로고    scopus 로고
    • An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion
    • DOI 10.1016/j.virusres.2003.11.010
    • Wang, Z., Mirza, A. M., Li, J., Mahon, P. J., and Iorio, R. M. (2004) An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion. Virus. Res. 99, 177-185 (Pubitemid 38121666)
    • (2004) Virus Research , vol.99 , Issue.2 , pp. 177-185
    • Wang, Z.1    Mirza, A.M.2    Li, J.3    Mahon, P.J.4    Iorio, R.M.5
  • 12
    • 35448970026 scopus 로고    scopus 로고
    • Measles virus
    • (Knipe, D. M., Howley, P. M., Griffin, D. E., Lamb, R. A., Martin, M. A., Roizman, B., and Straus, S. E., eds), 5th Ed., Lippincott Williams & Wilkins, Philadelphia
    • Griffin, D. E. (2007) Measles virus, in Fields Virology (Knipe, D. M., Howley, P. M., Griffin, D. E., Lamb, R. A., Martin, M. A., Roizman, B., and Straus, S. E., eds), 5th Ed., pp. 1551-1585, Lippincott Williams & Wilkins, Philadelphia
    • (2007) Fields Virology , pp. 1551-1585
    • Griffin, D.E.1
  • 14
    • 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, M. A., and Plemper, R. K. (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
  • 15
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemagglutinin- neuraminidase tetramer in complex with its receptor, sialyllactose
    • DOI 10.1016/j.str.2005.02.019, PII S0969212605001310
    • Yuan, P., Thompson, T. B., Wurzburg, B. A., Paterson, R. G., Lamb, R. A., and Jardetzky, T. S. (2005) Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13, 803-815 (Pubitemid 40704668)
    • (2005) Structure , vol.13 , Issue.5 , pp. 803-815
    • Yuan, P.1    Thompson, T.B.2    Wurzburg, B.A.3    Paterson, R.G.4    Lamb, R.A.5    Jardetzky, T.S.6
  • 16
    • 1842614339 scopus 로고    scopus 로고
    • Second sialic acid binding site in newcastle disease virus hemagglutinin-neuraminidase: Implications for fusion
    • DOI 10.1128/JVI.78.7.3733-3741.2004
    • Zaitsev, V., von Itzstein, M., Groves, D., Kiefel, M., Takimoto, T., Portner, A., and Taylor, G. (2004) Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase. Implications for fusion. J. Virol. 78, 3733-3741 (Pubitemid 38568312)
    • (2004) Journal of Virology , vol.78 , Issue.7 , pp. 3733-3741
    • Zaitsev, V.1    Von Itzstein, M.2    Groves, D.3    Kiefel, M.4    Takimoto, T.5    Portner, A.6    Taylor, G.7
  • 17
    • 80052564183 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus hemagglutinin- neuraminidase (HN) ectodomain reveals a four-helix bundle stalk
    • Yuan, P., Swanson, K. A., Leser, G. P., Paterson, R. G., Lamb, R. A., and Jardetzky, T. S. (2011) Structure of the Newcastle disease virus hemagglutinin- neuraminidase (HN) ectodomain reveals a four-helix bundle stalk. Proc. Natl. Acad. Sci. U.S.A. 108, 14920-14925
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14920-14925
    • Yuan, P.1    Swanson, K.A.2    Leser, G.P.3    Paterson, R.G.4    Lamb, R.A.5    Jardetzky, T.S.6
  • 19
    • 0026582218 scopus 로고
    • Measles virus inhibits mitogen-induced T cell proliferation but does not directly perturb the T cell activation process inside the cell
    • Yanagi, Y., Cubitt, B. A., and Oldstone, M. B. (1992) Measles virus inhibits mitogen-induced T cell proliferation but does not directly perturb the T cell activation process inside the cell. Virology 187, 280-289
    • (1992) Virology , vol.187 , pp. 280-289
    • Yanagi, Y.1    Cubitt, B.A.2    Oldstone, M.B.3
  • 20
    • 0029994029 scopus 로고    scopus 로고
    • Isolation and characterization of a Chinese hamster ovary mutant cell line with altered sensitivity to vaccinia virus killing
    • Bair, C. H., Chung, C. S., Vasilevskaya, I. A., and Chang, W. (1996) Isolation and characterization of a Chinese hamster ovary mutant cell line with altered sensitivity to vaccinia virus killing. J. Virol. 70, 4655-4666 (Pubitemid 26187460)
    • (1996) Journal of Virology , vol.70 , Issue.7 , pp. 4655-4666
    • Bair, C.-H.1    Chung, C.-S.2    Vasilevskaya, I.A.3    Chang, W.4
  • 22
    • 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
    • DOI 10.1128/JVI.75.9.4399-4401.2001
    • Ono, N., Tatsuo, H., Hidaka, Y., Aoki, T., Minagawa, H., and Yanagi, Y. (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 (Pubitemid 32410152)
    • (2001) Journal of Virology , vol.75 , Issue.9 , pp. 4399-4401
    • Ono, N.1    Tatsuo, H.2    Hidaka, Y.3    Aoki, T.4    Minagawa, H.5    Yanagi, Y.6
  • 23
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • DOI 10.1073/pnas.212519299
    • Reeves, P. J., Callewaert, N., Contreras, R., and Khorana, H. G. (2002) Structure and function in rhodopsin. High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acad. Sci. U.S.A. 99, 13419-13424 (Pubitemid 35215396)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.21 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 24
    • 0019313084 scopus 로고
    • Monospecific antibody to the haemagglutinin of measles virus
    • McFarlin, D. E., Bellini, W. J., Mingioli, E. S., Behar, T. N., and Trudgett, A. (1980) Monospecific antibody to the haemagglutinin of measles virus. J. Gen. Virol. 48, 425-429 (Pubitemid 10014071)
    • (1980) Journal of General Virology , vol.48 , Issue.2 , pp. 425-429
    • McFarlin, D.E.1    Bellini, W.J.2    Mingioli, E.S.3
  • 25
    • 47749143663 scopus 로고    scopus 로고
    • Functional interaction between paramyxovirus fusion and attachment proteins
    • Lee, J. K., Prussia, A., Paal, T., White, L. K., Snyder, J. P., and Plemper, R. K. (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    Prussia, A.2    Paal, T.3    White, L.K.4    Snyder, J.P.5    Plemper, R.K.6
  • 27
    • 77957199952 scopus 로고    scopus 로고
    • Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry
    • Ennis, M. K., Hu, C., Naik, S. K., Hallak, L. K., Peng, K. W., Russell, S. J., and Dingli, D. (2010) Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry. J. Virol. 84, 10913-10917
    • (2010) J. Virol. , vol.84 , pp. 10913-10917
    • Ennis, M.K.1    Hu, C.2    Naik, S.K.3    Hallak, L.K.4    Peng, K.W.5    Russell, S.J.6    Dingli, D.7
  • 28
    • 0027302020 scopus 로고
    • Mutations in the transmembrane domain of theHNprotein of Newcastle disease virus affect the structure and activity of the protein
    • McGinnes, L., Sergel, T., and Morrison, T. (1993) Mutations in the transmembrane domain of theHNprotein of Newcastle disease virus affect the structure and activity of the protein. Virology 196, 101-110
    • (1993) Virology , vol.196 , pp. 101-110
    • McGinnes, L.1    Sergel, T.2    Morrison, T.3
  • 29
    • 49049109230 scopus 로고    scopus 로고
    • Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein
    • Yuan, P., Leser, G. P., Demeler, B., Lamb, R. A., and Jardetzky, T. S. (2008) Domain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein. Virology 378, 282-291
    • (2008) Virology , vol.378 , pp. 282-291
    • Yuan, P.1    Leser, G.P.2    Demeler, B.3    Lamb, R.A.4    Jardetzky, T.S.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., Brindley, M. A., Avila, M., Origgi, F. C., Langedijk, J. P., Örvell, C., Vandevelde, M., Zurbriggen, A., Plemper, R. K., and Plattet, P. (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    Brindley, M.A.2    Avila, M.3    Origgi, F.C.4    Langedijk, J.P.5    Örvell, C.6    Vandevelde, M.7    Zurbriggen, A.8    Plemper, R.K.9    Plattet, P.10
  • 32
    • 77449145697 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin bound to the CD46 receptor
    • Santiago, C., Celma, M. L., Stehle, T., and Casasnovas, J. M. (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
  • 33
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell, S., Takimoto, T., Portner A, Taylor G. (2000) Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat. Struct. Biol. 7, 1068-1074
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 34
    • 84866859065 scopus 로고    scopus 로고
    • Fusion activation by a headless parainfluenza virus 5 hemagglutinin- neuraminidase stalk suggests a modular mechanism for triggering
    • Bose, S., Zokarkar, A., Welch, B. D., Leser, G. P., Jardetzky, T. S., and Lamb, R. A. (2012) Fusion activation by a headless parainfluenza virus 5 hemagglutinin- neuraminidase stalk suggests a modular mechanism for triggering. Proc. Natl. Acad. Sci. U.S.A. 109, E2625-2634
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Bose, S.1    Zokarkar, A.2    Welch, B.D.3    Leser, G.P.4    Jardetzky, T.S.5    Lamb, R.A.6
  • 35
    • 0036380741 scopus 로고    scopus 로고
    • Neutralizing B cell response in measles
    • Bouche, F. B., Ertl, O. T., and Muller, C. P. (2002) Neutralizing B cell response in measles. Viral. Immunol. 15, 451-471
    • (2002) Viral. Immunol. , vol.15 , pp. 451-471
    • Bouche, F.B.1    Ertl, O.T.2    Muller, C.P.3
  • 36
    • 0027258145 scopus 로고
    • Molecular characterization of epitopes on the measles virus hemagglutinin protein
    • Hu, A., Sheshberadaran, H., Norrby, E., and Kövamees, J. (1993) Molecular characterization of epitopes on the measles virus hemagglutinin protein. Virology 192, 351-354
    • (1993) Virology , vol.192 , pp. 351-354
    • Hu, A.1    Sheshberadaran, H.2    Norrby, E.3    Kövamees, J.4


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