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Volumn 86, Issue 24, 2012, Pages 13467-13474

Inhibition of marburg virus budding by nonneutralizing antibodiesto the envelope glycoprotein

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G1 ANTIBODY; IMMUNOGLOBULIN M ANTIBODY; MATRIX PROTEIN; NEUTRALIZING ANTIBODY; NONSTRUCTURAL PROTEIN 4; PROTEIN VP40; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; VIRUS NUCLEOPROTEIN;

EID: 84870660384     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01896-12     Document Type: Article
Times cited : (53)

References (53)
  • 1
    • 0034059510 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibody to the E1 glycoprotein epitope of rubella virus mediates virus arrest in VERO cells
    • Corboba P, Grutadauria S, Cuffini C, Zapata M. 2000. Neutralizing monoclonal antibody to the E1 glycoprotein epitope of rubella virus mediates virus arrest in VERO cells. Viral Immunol. 13:83-92.
    • (2000) Viral Immunol. , vol.13 , pp. 83-92
    • Corboba, P.1    Grutadauria, S.2    Cuffini, C.3    Zapata, M.4
  • 2
    • 0017706369 scopus 로고
    • Inhibition of bovine leukemia virus release by antiviral antibodies
    • Driscoll DM, Onuma M, Olson C. 1977. Inhibition of bovine leukemia virus release by antiviral antibodies. Arch. Virol. 55:139 -144.
    • (1977) Arch. Virol. , vol.55
    • Driscoll, D.M.1    Onuma, M.2    Olson, C.3
  • 3
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • DuBridge RB, et al. 1987. Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Mol. Cell. Biol. 7:379 -387.
    • (1987) Mol. Cell. Biol. , vol.7
    • Dubridge, R.B.1
  • 4
    • 84859462127 scopus 로고    scopus 로고
    • Postexposure antibody prophylaxis protects nonhuman primates from filovirus disease
    • Dye JM, et al. 2012. Postexposure antibody prophylaxis protects nonhuman primates from filovirus disease. Proc. Natl. Acad. Sci. U. S. A. 109: 5034-5039.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 5034-5039
    • Dye, J.M.1
  • 5
    • 0028246971 scopus 로고
    • Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein
    • Feldmann H, Nichol ST, Klenk HD, Peters CJ, Sanchez A. 1994. Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein. Virology 199:469-473.
    • (1994) Virology , vol.199 , pp. 469-473
    • Feldmann, H.1    Nichol, S.T.2    Klenk, H.D.3    Peters, C.J.4    Sanchez, A.5
  • 6
    • 0025760333 scopus 로고
    • Glycosylation and oligomerization of the spike protein of Marburg virus
    • Feldmann H, Will C, Schikore M, Slenczka W, Klenk HD. 1991. Glycosylation and oligomerization of the spike protein of Marburg virus. Virology 182:353-356.
    • (1991) Virology , vol.182 , pp. 353-356
    • Feldmann, H.1    Will, C.2    Schikore, M.3    Slenczka, W.4    Klenk, H.D.5
  • 7
    • 0021248989 scopus 로고
    • Antigenic modulation induced by monoclonal antibodies: antibodies to measles virus hemagglutinin alters expression of other viral polypeptides in infected cells
    • Fujinami RS, Norrby E, Oldstone MB. 1984. Antigenic modulation induced by monoclonal antibodies: antibodies to measles virus hemagglutinin alters expression of other viral polypeptides in infected cells. J. Immunol. 132:2618 -2621.
    • (1984) J. Immunol. , vol.132
    • Fujinami, R.S.1    Norrby, E.2    Oldstone, M.B.3
  • 8
    • 0018943514 scopus 로고
    • Alterations in expression of measles virus polypeptides by antibody: molecular events in antibody-induced antigenic modulation
    • Fujinami RS, Oldstone MB. 1980. Alterations in expression of measles virus polypeptides by antibody: molecular events in antibody-induced antigenic modulation. J. Immunol. 125:78-85.
    • (1980) J. Immunol. , vol.125 , pp. 78-85
    • Fujinami, R.S.1    Oldstone, M.B.2
  • 9
    • 60249086364 scopus 로고    scopus 로고
    • No exit: targeting the budding process to inhibit filovirus replication
    • Harty RN. 2009. No exit: targeting the budding process to inhibit filovirus replication. Antiviral Res. 81:189 -197.
    • (2009) Antiviral Res. , vol.81
    • Harty, R.N.1
  • 10
    • 0034610295 scopus 로고    scopus 로고
    • A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding
    • Harty RN, Brown ME, Wang G, Huibregtse J, Hayes FP. 2000. A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding. Proc. Natl. Acad. Sci. U. S. A. 97:13871-13876.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13871-13876
    • Harty, R.N.1    Brown, M.E.2    Wang, G.3    Huibregtse, J.4    Hayes, F.P.5
  • 11
    • 0035031534 scopus 로고    scopus 로고
    • Ebola virus VP40-induced particle formation and association with the lipid bilayer
    • Jasenosky LD, Neumann G, Lukashevich I, Kawaoka Y. 2001. Ebola virus VP40-induced particle formation and association with the lipid bilayer. J. Virol. 75:5205-5214.
    • (2001) J. Virol. , vol.75 , pp. 5205-5214
    • Jasenosky, L.D.1    Neumann, G.2    Lukashevich, I.3    Kawaoka, Y.4
  • 12
    • 0027483843 scopus 로고
    • Infection-permissive immunization with influenza virus neuraminidase prevents weight loss in infected mice
    • Johansson BE, Grajower B, Kilbourne ED. 1993. Infection-permissive immunization with influenza virus neuraminidase prevents weight loss in infected mice. Vaccine 11:1037-1039.
    • (1993) Vaccine , vol.11 , pp. 1037-1039
    • Johansson, B.E.1    Grajower, B.2    Kilbourne, E.D.3
  • 13
    • 1242342119 scopus 로고    scopus 로고
    • The matrix protein of Marburg virus is transported to the plasma membrane along cellular membranes: exploiting the retrograde late endosomal pathway
    • Kolesnikova L, Bamberg S, Berghöfer B, Becker S. 2004. The matrix protein of Marburg virus is transported to the plasma membrane along cellular membranes: exploiting the retrograde late endosomal pathway. J. Virol. 78:2382-2393.
    • (2004) J. Virol. , vol.78 , pp. 2382-2393
    • Kolesnikova, L.1    Bamberg, S.2    Berghöfer, B.3    Becker, S.4
  • 14
    • 7644231754 scopus 로고    scopus 로고
    • Multivesicular bodies as a platform for formation of the Marburg virus envelope
    • Kolesnikova L, Berghöfer B, Bamberg S, Becker S. 2004. Multivesicular bodies as a platform for formation of the Marburg virus envelope. J. Virol. 78:12277-12287.
    • (2004) J. Virol. , vol.78 , pp. 12277-12287
    • Kolesnikova, L.1    Berghöfer, B.2    Bamberg, S.3    Becker, S.4
  • 16
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to a human survivor antibody
    • Lee JE, et al. 2008. Structure of the Ebola virus glycoprotein bound to a human survivor antibody. Nature 454:177-182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1
  • 17
    • 69249132055 scopus 로고    scopus 로고
    • Neutralizing ebolavirus: structural insights into the envelope glycoprotein and antibodies targeted against it
    • Lee JE, Saphire EO. 2009. Neutralizing ebolavirus: structural insights into the envelope glycoprotein and antibodies targeted against it. Curr. Opin. Struct. Biol. 19:408-417.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 408-417
    • Lee, J.E.1    Saphire, E.O.2
  • 18
    • 3142710288 scopus 로고    scopus 로고
    • Contribution of Ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 viruslike particles
    • Licata JM, Johnson RF, Han Z, Harty RN. 2004. Contribution of Ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 viruslike particles. J. Virol. 78:7344 -7351.
    • (2004) J. Virol. , vol.78
    • Licata, J.M.1    Johnson, R.F.2    Han, Z.3    Harty, R.N.4
  • 19
    • 77954936778 scopus 로고    scopus 로고
    • Viral and host proteins that modulate filovirus budding
    • Liu Y, Harty RN. 2010. Viral and host proteins that modulate filovirus budding. Future Virol. 5:481-491.
    • (2010) Future Virol. , vol.5 , pp. 481-491
    • Liu, Y.1    Harty, R.N.2
  • 20
    • 80053019483 scopus 로고    scopus 로고
    • Human cytomegalovirus escapes a naturally occurring neutralizing antibody by incorporating it into assembling virions
    • Manley K, et al. 2011. Human cytomegalovirus escapes a naturally occurring neutralizing antibody by incorporating it into assembling virions. Cell Host Microbe 10:197-209.
    • (2011) Cell Host Microbe , vol.10 , pp. 197-209
    • Manley, K.1
  • 21
    • 84860456246 scopus 로고    scopus 로고
    • Protective efficacy of neutralizing monoclonal antibodies in a nonhuman primate model of Ebola hemorrhagic fever
    • doi:10.1371/journal.pone.0036192
    • Marzi A, et al. 2012. Protective efficacy of neutralizing monoclonal antibodies in a nonhuman primate model of Ebola hemorrhagic fever. PLoS One 7:e36192. doi:10.1371/journal.pone.0036192.
    • (2012) PLoS One , vol.7
    • Marzi, A.1
  • 22
    • 77951439172 scopus 로고    scopus 로고
    • Different potential of C-type lectin-mediated entry between Marburg virus strains
    • Matsuno K, et al. 2010. Different potential of C-type lectin-mediated entry between Marburg virus strains. J. Virol. 84:5140 -5147.
    • (2010) J. Virol. , vol.84
    • Matsuno, K.1
  • 24
    • 80054722475 scopus 로고    scopus 로고
    • Antibody-dependent enhancement of Marburg virus infection
    • doi:10.1093/infdis/jir334
    • Nakayama E, et al. 2011. Antibody-dependent enhancement of Marburg virus infection. J. Infect. Dis. 204:S978 -S985. doi:10.1093/infdis/jir334.
    • (2011) J. Infect. Dis. , vol.204
    • Nakayama, E.1
  • 25
    • 78449264916 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assay for detection of filovirus species-specific antibodies
    • Nakayama E, et al. 2010. Enzyme-linked immunosorbent assay for detection of filovirus species-specific antibodies. Clin. Vaccine Immunol. 17:1723-1728.
    • (2010) Clin. Vaccine Immunol. , vol.17 , pp. 1723-1728
    • Nakayama, E.1
  • 26
    • 77649205430 scopus 로고    scopus 로고
    • Contributions of the avian influenza virus HA, NA, and M2 surface proteins to the induction of neutralizing antibodies and protective immunity
    • Nayak B, et al. 2010. Contributions of the avian influenza virus HA, NA, and M2 surface proteins to the induction of neutralizing antibodies and protective immunity. J. Virol. 84:2408 -2420.
    • (2010) J. Virol. , vol.84
    • Nayak, B.1
  • 27
    • 0036235725 scopus 로고    scopus 로고
    • Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP
    • Noda T, et al. 2002. Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP. J. Virol. 76:4855-4865.
    • (2002) J. Virol. , vol.76 , pp. 4855-4865
    • Noda, T.1
  • 28
    • 0022248918 scopus 로고
    • The effects of monoclonal antibodies against the hemagglutinin-neuraminidase and fusion protein on the release of Sendai virus from infected cells
    • Orvell C, Kristensson K. 1985. The effects of monoclonal antibodies against the hemagglutinin-neuraminidase and fusion protein on the release of Sendai virus from infected cells. Arch. Virol. 86:1-15.
    • (1985) Arch. Virol. , vol.86 , pp. 1-15
    • Orvell, C.1    Kristensson, K.2
  • 29
    • 84862525229 scopus 로고    scopus 로고
    • Successful treatment of Ebola virus-infected cynomolgus macaques with monoclonal antibodies
    • doi:10.1126/scitranslmed.3003876
    • Qiu X, et al. 2012. Successful treatment of Ebola virus-infected cynomolgus macaques with monoclonal antibodies. Sci. Transl. Med. 4:138ra81. doi:10.1126/scitranslmed.3003876.
    • (2012) Sci. Transl. Med. , vol.4
    • Qiu, X.1
  • 30
    • 34548512432 scopus 로고    scopus 로고
    • Filoviridae: Marburg and Ebola viruses, p 1409-1448
    • In Knipe DM, et al (ed), 5th ed, vol 1. Lippincott Williams & Wilkins, Philadelphia, PA
    • Sanchez A, Geisbert TW, Feldmann H. 2007. Filoviridae: Marburg and Ebola viruses, p 1409-1448. In Knipe DM, et al (ed), Fields virology, 5th ed, vol 1. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology
    • Sanchez, A.1    Geisbert, T.W.2    Feldmann, H.3
  • 31
    • 0026805982 scopus 로고
    • Antibody-dependent transcriptional regulation of measles virus in persistently infected neural cells
    • Schneider-Schaulies S, et al. 1992. Antibody-dependent transcriptional regulation of measles virus in persistently infected neural cells. J. Virol. 66:5534 -5541.
    • (1992) J. Virol. , vol.66
    • Schneider-schaulies, S.1
  • 33
    • 34249107414 scopus 로고    scopus 로고
    • Production and characterization of monoclonal antibodies against different epitopes of Ebola virus antigens
    • Shahhosseini S, et al. 2007. Production and characterization of monoclonal antibodies against different epitopes of Ebola virus antigens. J. Virol. Methods 143:29 -37.
    • (2007) J. Virol. Methods , vol.143
    • Shahhosseini, S.1
  • 34
    • 77952309575 scopus 로고    scopus 로고
    • Antibody-mediated neutralization of Ebola virus can occur by two distinct mechanisms
    • Shedlock DJ, et al. 2010. Antibody-mediated neutralization of Ebola virus can occur by two distinct mechanisms. Virology 401:228 -235.
    • (2010) Virology , vol.401
    • Shedlock, D.J.1
  • 35
    • 79961199513 scopus 로고    scopus 로고
    • Neutralizing anti-gH antibody of varicella-zoster virus modulates distribution of gH and induces gene regulation, mimicking latency
    • Shiraki K, et al. 2011. Neutralizing anti-gH antibody of varicella-zoster virus modulates distribution of gH and induces gene regulation, mimicking latency. J. Virol. 85:8172-8180.
    • (2011) J. Virol. , vol.85 , pp. 8172-8180
    • Shiraki, K.1
  • 36
    • 0036171135 scopus 로고    scopus 로고
    • Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence
    • Simmons G, Wool-Lewis RJ, Baribaud F, Netter RC, Bates P. 2002. Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence. J. Virol. 76:2518 -2528.
    • (2002) J. Virol. , vol.76
    • Simmons, G.1    Wool-lewis, R.J.2    Baribaud, F.3    Netter, R.C.4    Bates, P.5
  • 37
    • 84860424652 scopus 로고    scopus 로고
    • Filovirus tropism: cellular molecules for viral entry
    • doi:10.3389/fmicb.2012.00034.
    • Takada A. 2012. Filovirus tropism: cellular molecules for viral entry. Front. Microbiol. 3:34. doi:10.3389/fmicb.2012.00034.
    • (2012) Front. Microbiol. , vol.3 , pp. 34
    • Takada, A.1
  • 38
    • 33845584363 scopus 로고    scopus 로고
    • Protective efficacy of neutralizing antibodies against Ebola virus infection
    • Takada A, Ebihara H, Jones S, Feldmann H, Kawaoka Y. 2007. Protective efficacy of neutralizing antibodies against Ebola virus infection. Vaccine 25:993-999.
    • (2007) Vaccine , vol.25 , pp. 993-999
    • Takada, A.1    Ebihara, H.2    Jones, S.3    Feldmann, H.4    Kawaoka, Y.5
  • 39
    • 0037229321 scopus 로고    scopus 로고
    • Identification of protective epitopes on Ebola virus glycoprotein at the single amino acid level by using recombinant vesicular stomatitis viruses
    • Takada A, et al. 2003. Identification of protective epitopes on Ebola virus glycoprotein at the single amino acid level by using recombinant vesicular stomatitis viruses. J. Virol. 77:1069 -1074.
    • (2003) J. Virol. , vol.77
    • Takada, A.1
  • 40
    • 12144290776 scopus 로고    scopus 로고
    • Human macrophage C-type lectin specific for galactose and N-acetylgalactosamine promotes filovirus entry
    • Takada A, et al. 2004. Human macrophage C-type lectin specific for galactose and N-acetylgalactosamine promotes filovirus entry. J. Virol. 78:2943-2947.
    • (2004) J. Virol. , vol.78 , pp. 2943-2947
    • Takada, A.1
  • 41
    • 0031449064 scopus 로고    scopus 로고
    • A system for functional analysis of Ebola virus glycoprotein
    • Takada A, et al. 1997. A system for functional analysis of Ebola virus glycoprotein. Proc. Natl. Acad. Sci. U. S. A. 94:14764 -14769.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94
    • Takada, A.1
  • 43
    • 70049115327 scopus 로고    scopus 로고
    • Isolation of genetically diverse Marburg viruses from Egyptian fruit bats
    • doi:10.1371/ journal.ppat.1000536
    • Towner JS, et al. 2009. Isolation of genetically diverse Marburg viruses from Egyptian fruit bats. PLoS Pathog. 5:e1000536. doi:10.1371/ journal.ppat.1000536.
    • (2009) PLoS Pathog. , vol.5
    • Towner, J.S.1
  • 44
    • 34247633960 scopus 로고    scopus 로고
    • Interaction of Tsg101 with Marburg virus VP40 depends on the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and Tsg101 plays a critical role in the budding of Marburg virus-like particles induced by VP40, NP, and GP
    • Urata S, et al. 2007. Interaction of Tsg101 with Marburg virus VP40 depends on the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and Tsg101 plays a critical role in the budding of Marburg virus-like particles induced by VP40, NP, and GP. J. Virol. 81:4895-4899.
    • (2007) J. Virol. , vol.81 , pp. 4895-4899
    • Urata, S.1
  • 45
    • 73149117324 scopus 로고    scopus 로고
    • Regulation of Marburg virus (MARV) budding by Nedd4.1: a different WW domain of Nedd4.1 is critical for binding to MARV and Ebola virus VP40
    • Urata S, Yasuda J. 2010. Regulation of Marburg virus (MARV) budding by Nedd4.1: a different WW domain of Nedd4.1 is critical for binding to MARV and Ebola virus VP40. J. Gen. Virol. 91:228 -234.
    • (2010) J. Gen. Virol. , vol.91
    • Urata, S.1    Yasuda, J.2
  • 46
    • 0030849402 scopus 로고    scopus 로고
    • Antibodies against vaccinia virus do not neutralize extracellular enveloped virus but prevent virus release from infected cells and comet formation
    • Vanderplasschen A, Hollinshead M, Smith GL. 1997. Antibodies against vaccinia virus do not neutralize extracellular enveloped virus but prevent virus release from infected cells and comet formation. J. Gen. Virol. 78: 2041-2048.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2041-2048
    • Vanderplasschen, A.1    Hollinshead, M.2    Smith, G.L.3
  • 47
    • 0034101994 scopus 로고    scopus 로고
    • Proteolytic processing of Marburg virus glycoprotein
    • Volchkov VE, et al. 2000. Proteolytic processing of Marburg virus glycoprotein. Virology 268:1-6.
    • (2000) Virology , vol.268 , pp. 1-6
    • Volchkov, V.E.1
  • 48
    • 0346057848 scopus 로고    scopus 로고
    • Production of novel Ebola virus-like particles from cDNAs: an alternative to Ebola virus generation by reverse genetics
    • Watanabe S, et al. 2004. Production of novel Ebola virus-like particles from cDNAs: an alternative to Ebola virus generation by reverse genetics. J. Virol. 78:999 -1005.
    • (2004) J. Virol. , vol.78
    • Watanabe, S.1
  • 49
    • 0023899347 scopus 로고
    • Protection against lethal influenza with neuraminidase
    • Webster RG, Reay PA, Laver WG. 1988. Protection against lethal influenza with neuraminidase. Virology 164:230 -237.
    • (1988) Virology , vol.164
    • Webster, R.G.1    Reay, P.A.2    Laver, W.G.3
  • 50
    • 0034051595 scopus 로고    scopus 로고
    • Epitopes involved in antibody-mediated protection from Ebola virus
    • Wilson JA, et al. 2000. Epitopes involved in antibody-mediated protection from Ebola virus. Science 287:1664 -1666.
    • (2000) Science , vol.287
    • Wilson, J.A.1
  • 51
    • 0031954296 scopus 로고    scopus 로고
    • Characterization of Ebola virus entry by using pseudotyped viruses: identification of receptor-deficient cell lines
    • Wool-Lewis RJ, Bates P. 1998. Characterization of Ebola virus entry by using pseudotyped viruses: identification of receptor-deficient cell lines. J. Virol. 72:3155-3160.
    • (1998) J. Virol. , vol.72 , pp. 3155-3160
    • Wool-Lewis, R.J.1    Bates, P.2
  • 52
    • 19044383768 scopus 로고    scopus 로고
    • Marburg haemorrhagic fever, Angola
    • World Health Organization
    • World Health Organization. 2005. Marburg haemorrhagic fever, Angola. Wkly. Epidemiol. Rec. 80:158-159.
    • (2005) Wkly. Epidemiol. Rec. , vol.80
  • 53
    • 0025353274 scopus 로고
    • Antigenic modulation of measles subacute sclerosing panencephalitis virus in a persistently infected rat glioma cell line by monoclonal anti-haemagglutinin antibodies
    • Zinnheimer-Dreikorn J, Koschel KP. 1990. Antigenic modulation of measles subacute sclerosing panencephalitis virus in a persistently infected rat glioma cell line by monoclonal anti-haemagglutinin antibodies. J. Gen. Virol. 71:1391-1394.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1391-1394
    • Zinnheimer-dreikorn, J.1    Koschel, K.P.2


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