메뉴 건너뛰기




Volumn 86, Issue 9, 2005, Pages 2535-2542

Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization

Author keywords

[No Author keywords available]

Indexed keywords

DENDRITIC CELL SPECIFIC INTERCELLULAR ADHESION MOLECULE 3 GRABBING NON INTEGRIN; MANNOSE BINDING LECTIN; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN;

EID: 23844550737     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/vir.0.81199-0     Document Type: Article
Times cited : (105)

References (66)
  • 1
    • 0036278649 scopus 로고    scopus 로고
    • C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans
    • Alvarez, C. P., Lasala, F., Carrillo, J., Muniz, O., Corbi, A. L. & Delgado, R. (2002). C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans. J Virol 76, 6841-6844.
    • (2002) J. Virol. , vol.76 , pp. 6841-6844
    • Alvarez, C.P.1    Lasala, F.2    Carrillo, J.3    Muniz, O.4    Corbi, A.L.5    Delgado, R.6
  • 2
    • 0028344851 scopus 로고
    • Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin
    • Anders, E. M., Hartley, C. A., Reading, P. C. & Ezekowitz, R. A. (1994). Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin. J Gen Virol 75, 615-622.
    • (1994) J. Gen. Virol. , vol.75 , pp. 615-622
    • Anders, E.M.1    Hartley, C.A.2    Reading, P.C.3    Ezekowitz, R.A.4
  • 3
    • 0036721331 scopus 로고    scopus 로고
    • Quantitative expression and virus transmission analysis of DC-SIGN on monocyte-derived dendritic cells
    • Baribaud, F., Pohlmann, S., Leslie, G., Mortari, F. & Doms, R. W. (2002). Quantitative expression and virus transmission analysis of DC-SIGN on monocyte-derived dendritic cells. J Virol 76, 9135-9142.
    • (2002) J. Virol. , vol.76 , pp. 9135-9142
    • Baribaud, F.1    Pohlmann, S.2    Leslie, G.3    Mortari, F.4    Doms, R.W.5
  • 6
    • 4644253146 scopus 로고    scopus 로고
    • Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity
    • Barrientos, L. G., Lasala, F., Delgado, R., Sanchez, A. & Gronenborn, A. M. (2004a). Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity. Structure 12, 1799-1807.
    • (2004) Structure , vol.12 , pp. 1799-1807
    • Barrientos, L.G.1    Lasala, F.2    Delgado, R.3    Sanchez, A.4    Gronenborn, A.M.5
  • 7
    • 2142653012 scopus 로고    scopus 로고
    • In vitro evaluation of cyanovirin-N antiviral activity, by use of lentiviral vectors pseudotyped with filovirus envelope glycoproteins
    • Barrientos, L. G., Lasala, F., Otero, J. R., Sanchez, A. & Delgado, R. (2004b). In vitro evaluation of cyanovirin-N antiviral activity, by use of lentiviral vectors pseudotyped with filovirus envelope glycoproteins. J Infect Dis 189, 1440-1443.
    • (2004) J. Infect. Dis. , vol.189 , pp. 1440-1443
    • Barrientos, L.G.1    Lasala, F.2    Otero, J.R.3    Sanchez, A.4    Delgado, R.5
  • 8
    • 0035911220 scopus 로고    scopus 로고
    • A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection
    • 10 other authors
    • Bashirova, A. A., Geijtenbeek T. B., van Duijnhoven, G. C. & 10 other authors (2001). A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection. J Exp Med 193, 671-678.
    • (2001) J. Exp. Med. , vol.193 , pp. 671-678
    • Bashirova, A.A.1    Geijtenbeek, T.B.2    van Duijnhoven, G.C.3
  • 11
    • 0019414964 scopus 로고
    • Neutralization of vesicular stomatitis virus (VSV) by human complement requires a natural IgM antibody present in human serum
    • Beebe, D. P. & Cooper, N. R. (1981). Neutralization of vesicular stomatitis virus (VSV) by human complement requires a natural IgM antibody present in human serum. J Immunol 126, 1562-1568.
    • (1981) J. Immunol. , vol.126 , pp. 1562-1568
    • Beebe, D.P.1    Cooper, N.R.2
  • 12
    • 0032191176 scopus 로고    scopus 로고
    • Role of early cytokines, including alpha and beta interferons (IFN-α/β), in innate and adaptive immune responses to viral infections
    • Biron, C. A. (1998). Role of early cytokines, including alpha and beta interferons (IFN-α/β), in innate and adaptive immune responses to viral infections. Semin Immunol 10, 383-390.
    • (1998) Semin. Immunol. , vol.10 , pp. 383-390
    • Biron, C.A.1
  • 13
  • 14
    • 0035028207 scopus 로고    scopus 로고
    • Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner
    • Bolmstedt, A. J., O'Keefe, B. R., Shenoy, S. R., McMahon, J. B. & Boyd, M. R. (2001). Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner. Mol Pharmacol 59, 949-954.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 949-954
    • Bolmstedt, A.J.1    O'Keefe, B.R.2    Shenoy, S.R.3    McMahon, J.B.4    Boyd, M.R.5
  • 15
    • 0037300816 scopus 로고    scopus 로고
    • Cyanovirin-N: A sugar-binding antiviral protein with a new twist
    • Botos, I. & Wlodawer, A. (2003). Cyanovirin-N: a sugar-binding antiviral protein with a new twist. Cell Mol Life Sci 60, 277-287.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 277-287
    • Botos, I.1    Wlodawer, A.2
  • 16
    • 0034993883 scopus 로고    scopus 로고
    • The role of the Type I interferon response in the resistance of mice to filovirus infection
    • Bray, M. (2001). The role of the Type I interferon response in the resistance of mice to filovirus infection. J Gen Virol 82, 1365-1373.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1365-1373
    • Bray, M.1
  • 17
    • 0034001723 scopus 로고    scopus 로고
    • Distinct mechanisms of entry by envelope glycoproteins of Marburg and Ebola (Zaire) viruses
    • Chan, S. Y., Speck R. F., Ma, M. C. & Goldsmith, M. A. (2000). Distinct mechanisms of entry by envelope glycoproteins of Marburg and Ebola (Zaire) viruses. J Virol 74, 4933-4937.
    • (2000) J. Virol. , vol.74 , pp. 4933-4937
    • Chan, S.Y.1    Speck, R.F.2    Ma, M.C.3    Goldsmith, M.A.4
  • 18
    • 0029170457 scopus 로고
    • The glycoprotein G of rhabdoviruses
    • Coll, J. M. (1995). The glycoprotein G of rhabdoviruses. Arch Virol 140, 827-851.
    • (1995) Arch. Virol. , vol.140 , pp. 827-851
    • Coll, J.M.1
  • 20
    • 0032921247 scopus 로고    scopus 로고
    • Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120
    • Esser, M. T., Mori, T., Mondor, I., Sattentau, Q. J., Dey, B., Berger, E. A., Boyd, M. R. & Lifson, J. D. (1999). Cyanovirin-N binds to gp120 to interfere with CD4-dependent human immunodeficiency virus type 1 virion binding, fusion, and infectivity but does not affect the CD4 binding site on gp120 or soluble CD4-induced conformational changes in gp120. J Virol 73, 4360-4371.
    • (1999) J. Virol. , vol.73 , pp. 4360-4371
    • Esser, M.T.1    Mori, T.2    Mondor, I.3    Sattentau, Q.J.4    Dey, B.5    Berger, E.A.6    Boyd, M.R.7    Lifson, J.D.8
  • 21
    • 0038348638 scopus 로고    scopus 로고
    • Role of the mannose-binding lectin in innate immunity
    • Ezekowitz, R. A. (2003). Role of the mannose-binding lectin in innate immunity. J Infect Dis 187, S335-S339.
    • (2003) J. Infect. Dis. , vol.187
    • Ezekowitz, R.A.1
  • 22
    • 0024584844 scopus 로고
    • A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
    • Ezekowitz, R. A., Kuhlman, M., Groopman, J. E. & Byrn, R. A. (1989). A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus. J Exp Med 169, 185-196.
    • (1989) J. Exp. Med. , vol.169 , pp. 185-196
    • Ezekowitz, R.A.1    Kuhlman, M.2    Groopman, J.E.3    Byrn, R.A.4
  • 23
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg, H., Mitchell, D. A., Drickamer, K. & Weis, W. I. (2001). Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 294, 2163-2166.
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 24
    • 0028246971 scopus 로고
    • Characterization of filoviruses based on differences in structure and antigenicity of the virion glycoprotein
    • Feldmann, H., Nichol, S. T., Klenk H. D., Peters, C. J. & 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
  • 25
    • 8144230009 scopus 로고    scopus 로고
    • Mannan-binding lectin modulates the response to HSV-2 infection
    • 8 other authors
    • Gadjeva, M., Paludan, S. R., Thiel, S. & 8 other authors (2004). Mannan-binding lectin modulates the response to HSV-2 infection. Clin Exp Immunol 138, 304-311.
    • (2004) Clin. Exp. Immunol. , vol.138 , pp. 304-311
    • Gadjeva, M.1    Paludan, S.R.2    Thiel, S.3
  • 26
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • 9 other authors [see comments]
    • Geijtenbeek, T. B., Kwon, D. S., Torensma, R. & 9 other authors (2000). DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells [see comments]. Cell 100, 587-597.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3
  • 27
    • 10744224131 scopus 로고    scopus 로고
    • Pathogenesis of Ebola hemorrhagic fever in cynomolgus macaques: Evidence that dendritic cells are early and sustained targets of infection
    • 7 other authors
    • Geisbert, T. W., Hensley, L. E., Larsen, T. & 7 other authors (2003). Pathogenesis of Ebola hemorrhagic fever in cynomolgus macaques: evidence that dendritic cells are early and sustained targets of infection. Am J Pathol 163, 2347-2370.
    • (2003) Am. J. Pathol. , vol.163 , pp. 2347-2370
    • Geisbert, T.W.1    Hensley, L.E.2    Larsen, T.3
  • 28
  • 29
    • 0141991144 scopus 로고    scopus 로고
    • Innate immune activation as a broad-spectrum biodefense strategy: Prospects and research challenges
    • Hackett, C. J. (2003). Innate immune activation as a broad-spectrum biodefense strategy: prospects and research challenges. J Allergy Clin Immunol 112, 686-694.
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 686-694
    • Hackett, C.J.1
  • 30
    • 0031686350 scopus 로고    scopus 로고
    • Structural aspects of collectins and receptors for collectins
    • Hansen, S. & Holmskov, U. (1998). Structural aspects of collectins and receptors for collectins. Immunobiology 199, 165-189.
    • (1998) Immunobiology , vol.199 , pp. 165-189
    • Hansen, S.1    Holmskov, U.2
  • 32
    • 0037311412 scopus 로고    scopus 로고
    • Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin
    • Hart, M. L., Saifuddin, M. & Spear, G. T. (2003). Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin. J Gen Virol 84, 353-360.
    • (2003) J. Gen. Virol. , vol.84 , pp. 353-360
    • Hart, M.L.1    Saifuddin, M.2    Spear, G.T.3
  • 34
    • 0031416787 scopus 로고    scopus 로고
    • Mechanisms of anti-influenza activity of surfactant proteins A and D: Comparison with serum collectins
    • Hartshorn, K. L., White, M. R., Shepherd, V., Reid, K., Jensenius, J. C. & Crouch, E. C. (1997). Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins. Am J Physiol 273, L1156-L1166.
    • (1997) Am. J. Physiol. , vol.273
    • Hartshorn, K.L.1    White, M.R.2    Shepherd, V.3    Reid, K.4    Jensenius, J.C.5    Crouch, E.C.6
  • 35
    • 0027372368 scopus 로고
    • Complement activation upon binding of mannan-binding protein to HIV envelope glycoproteins
    • Haurum, J. S., Thiel, S., Jones, I. M., Fischer, P. B., Laursen, S. B. & Jensenius, J. C. (1993). Complement activation upon binding of mannan-binding protein to HIV envelope glycoproteins. AIDS 7, 1307-1313.
    • (1993) AIDS , vol.7 , pp. 1307-1313
    • Haurum, J.S.1    Thiel, S.2    Jones, I.M.3    Fischer, P.B.4    Laursen, S.B.5    Jensenius, J.C.6
  • 36
    • 0141568802 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies to Marburg virus (strain Musoke) glycoprotein and identification of two protective epitopes
    • Hevey, M., Negley, D. & Schmaljohn, A. (2003). Characterization of monoclonal antibodies to Marburg virus (strain Musoke) glycoprotein and identification of two protective epitopes. Virology 314, 350-357.
    • (2003) Virology , vol.314 , pp. 350-357
    • Hevey, M.1    Negley, D.2    Schmaljohn, A.3
  • 37
    • 0034999785 scopus 로고    scopus 로고
    • Mannose-binding lectin: Targeting the microbial world for complement attack and opsonophagocytosis
    • Jack D. L., Klein, N. J. & Turner, M. W. (2001). Mannose-binding lectin: targeting the microbial world for complement attack and opsonophagocytosis. Immunol Rev 180, 86-99.
    • (2001) Immunol. Rev. , vol.180 , pp. 86-99
    • Jack, D.L.1    Klein, N.J.2    Turner, M.W.3
  • 38
    • 5444248711 scopus 로고    scopus 로고
    • Mannose binding lectin (MBL) and HIV
    • Ji, X., Gewurz, H. & Spear, G. T. (2005). Mannose binding lectin (MBL) and HIV. Mol Immunol 42, 145-152.
    • (2005) Mol. Immunol. , vol.42 , pp. 145-152
    • Ji, X.1    Gewurz, H.2    Spear, G.T.3
  • 39
    • 0037227929 scopus 로고    scopus 로고
    • Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR
    • 8 other authors
    • Lin, G., Simmons, G., Pohlmann, S. & 8 other authors (2003). Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR. J Virol 77, 1337-1346.
    • (2003) J. Virol. , vol.77 , pp. 1337-1346
    • Lin, G.1    Simmons, G.2    Pohlmann, S.3
  • 40
    • 4043053773 scopus 로고    scopus 로고
    • Pathogenesis of filoviral haemorrhagic fevers
    • Mahanty, S. & Bray, M. (2004). Pathogenesis of filoviral haemorrhagic fevers. Lancet Infect Dis 4, 487-498.
    • (2004) Lancet Infect. Dis. , vol.4 , pp. 487-498
    • Mahanty, S.1    Bray, M.2
  • 41
    • 0043166564 scopus 로고    scopus 로고
    • Protection from lethal infection is determined by innate immune responses in a mouse model of Ebola virus infection
    • Mahanty, S., Gupta, M., Paragas, J., Bray, M., Ahmed, R. & Rollin, P. E. (2003). Protection from lethal infection is determined by innate immune responses in a mouse model of Ebola virus infection. Virology 312, 415-424.
    • (2003) Virology , vol.312 , pp. 415-424
    • Mahanty, S.1    Gupta, M.2    Paragas, J.3    Bray, M.4    Ahmed, R.5    Rollin, P.E.6
  • 42
    • 6344261967 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus
    • 12 other authors
    • Marzi, A., Gramberg, T., Simmons, G. & 12 other authors (2004). DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of severe acute respiratory syndrome coronavirus. J Virol 78, 12090-12095.
    • (2004) J. Virol. , vol.78 , pp. 12090-12095
    • Marzi, A.1    Gramberg, T.2    Simmons, G.3
  • 43
    • 0035015319 scopus 로고    scopus 로고
    • Ficolins and the lectin complement pathway
    • Matsushita, M. & Fujita, T. (2001). Ficolins and the lectin complement pathway. Immunol Rev 180, 78-85.
    • (2001) Immunol. Rev. , vol.180 , pp. 78-85
    • Matsushita, M.1    Fujita, T.2
  • 44
    • 0032920138 scopus 로고    scopus 로고
    • High-level and effective production of human mannan-binding lectin (MBL) in Chinese hamster ovary (CHO) cells
    • 7 other authors
    • Ohtani, K., Suzuki, Y., Eda, S. & 7 other authors (1999). High-level and effective production of human mannan-binding lectin (MBL) in Chinese hamster ovary (CHO) cells. J Immunol Methods 222, 135-144.
    • (1999) J. Immunol. Methods , vol.222 , pp. 135-144
    • Ohtani, K.1    Suzuki, Y.2    Eda, S.3
  • 45
    • 0034868248 scopus 로고    scopus 로고
    • The mannan-binding lectin pathway of complement activation: Biology and disease association
    • Petersen, S. V., Thiel, S. & Jensenius, J. C. (2001). The mannan-binding lectin pathway of complement activation: biology and disease association. Mol Immunol 38, 133-149.
    • (2001) Mol. Immunol. , vol.38 , pp. 133-149
    • Petersen, S.V.1    Thiel, S.2    Jensenius, J.C.3
  • 46
    • 0029561157 scopus 로고
    • A serum mannose-binding lectin mediates complement-dependent lysis of influenza virus-infected cells
    • Reading, P. C., Hartley, C. A., Ezekowitz, R. A. & Anders, E. M. (1995). A serum mannose-binding lectin mediates complement-dependent lysis of influenza virus-infected cells. Biochem Biophys Res Commun 217, 1128-1136.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1128-1136
    • Reading, P.C.1    Hartley, C.A.2    Ezekowitz, R.A.3    Anders, E.M.4
  • 47
    • 4544293451 scopus 로고    scopus 로고
    • Depletion of peripheral blood T lymphocytes and NK cells during the course of Ebola hemorrhagic fever in cynomolgus macaques
    • Reed, D. S., Hensley, L. E., Gelsbert, J. B., Jahrling, P. B. & Geisbert, T. W. (2004). Depletion of peripheral blood T lymphocytes and NK cells during the course of Ebola hemorrhagic fever in cynomolgus macaques. Viral Immunol 17, 390-400.
    • (2004) Viral Immunol. , vol.17 , pp. 390-400
    • Reed, D.S.1    Hensley, L.E.2    Gelsbert, J.B.3    Jahrling, P.B.4    Geisbert, T.W.5
  • 48
    • 0034028110 scopus 로고    scopus 로고
    • Interaction of mannose-binding lectin with primary isolates of human immunodeficiency virus type 1
    • Saifuddin, M., Hart, M. L., Gewurz, H., Zhang, Y. & Spear, G. T. (2000). Interaction of mannose-binding lectin with primary isolates of human immunodeficiency virus type 1. J Gen Virol 81, 949-955.
    • (2000) J. Gen. Virol. , vol.81 , pp. 949-955
    • Saifuddin, M.1    Hart, M.L.2    Gewurz, H.3    Zhang, Y.4    Spear, G.T.5
  • 49
    • 0029976177 scopus 로고    scopus 로고
    • The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing
    • Sanchez, A., Trappier, S. G., Mahy, B. W., Peters, C. J. & Nichol, S. T. (1996). The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing. Proc Natl Acad Sci U S A 93, 3602-3607.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3602-3607
    • Sanchez, A.1    Trappier, S.G.2    Mahy, B.W.3    Peters, C.J.4    Nichol, S.T.5
  • 50
    • 4544228226 scopus 로고    scopus 로고
    • Analysis of human peripheral blood samples from fatal and nonfatal cases of Ebola (Sudan) hemorrhagic fever: Cellular responses, virus load, and nitric oxide levels
    • Sanchez, A., Lukwiya, M., Bausch, D., Mahanty, S., Sanchez, A. J., Wagoner, K. D. & Rollin, P. E. (2004). Analysis of human peripheral blood samples from fatal and nonfatal cases of Ebola (Sudan) hemorrhagic fever: cellular responses, virus load, and nitric oxide levels. J Virol 78, 10370-10377.
    • (2004) J. Virol. , vol.78 , pp. 10370-10377
    • Sanchez, A.1    Lukwiya, M.2    Bausch, D.3    Mahanty, S.4    Sanchez, A.J.5    Wagoner, K.D.6    Rollin, P.E.7
  • 51
    • 0036171135 scopus 로고    scopus 로고
    • Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence
    • Simmons, G., Wool-Lewis, R. J., Baribaud, F., Netter, R. C. & 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 , pp. 2518-2528
    • Simmons, G.1    Wool-Lewis, R.J.2    Baribaud, F.3    Netter, R.C.4    Bates, P.5
  • 52
    • 0037227457 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR bind Ebola glycoproteins and enhance infection of macrophages and endothelial cells
    • 10 other authors
    • Simmons, G., Reeves, J. D., Grogan, C. C. & 10 other authors (2003). DC-SIGN and DC-SIGNR bind Ebola glycoproteins and enhance infection of macrophages and endothelial cells. Virology 305, 115-123.
    • (2003) Virology , vol.305 , pp. 115-123
    • Simmons, G.1    Reeves, J.D.2    Grogan, C.C.3
  • 53
    • 0033663327 scopus 로고    scopus 로고
    • Innate defences against viraemia
    • Singh, I. P. & Baron, S. (2000). Innate defences against viraemia. Rev Med Virol 10, 395-403.
    • (2000) Rev. Med. Virol. , vol.10 , pp. 395-403
    • Singh, I.P.1    Baron, S.2
  • 55
    • 0032521296 scopus 로고    scopus 로고
    • Requirement for the alternative pathway as well as C4 and C2 in complement-dependent hemolysis via the lectin pathway
    • Suankratay, C., Zhang, X. H., Zhang, Y., Lint T. F. & Gewurz, H. (1998). Requirement for the alternative pathway as well as C4 and C2 in complement-dependent hemolysis via the lectin pathway. J Immunol 160, 3006-3013.
    • (1998) J. Immunol. , vol.160 , pp. 3006-3013
    • Suankratay, C.1    Zhang, X.H.2    Zhang, Y.3    Lint, T.F.4    Gewurz, H.5
  • 56
    • 10644277846 scopus 로고    scopus 로고
    • Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent protein-trafficking pathway
    • Sullivan, N. J., Peterson, M., Yang, Z. Y., Kong, W. P., Duckers, H., Nabel, E. & Nabel, G. J. (2005). Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent protein-trafficking pathway. J Virol 79, 547-553.
    • (2005) J. Virol. , vol.79 , pp. 547-553
    • Sullivan, N.J.1    Peterson, M.2    Yang, Z.Y.3    Kong, W.P.4    Duckers, H.5    Nabel, E.6    Nabel, G.J.7
  • 57
    • 0035476472 scopus 로고    scopus 로고
    • The pathogenesis of Ebola hemorrhagic fever
    • Takada, A. & Kawaoka, Y. (2001). The pathogenesis of Ebola hemorrhagic fever. Trends Microbiol 9, 506-511.
    • (2001) Trends Microbiol. , vol.9 , pp. 506-511
    • Takada, A.1    Kawaoka, Y.2
  • 58
    • 0242526931 scopus 로고    scopus 로고
    • Antibody-dependent enhancement of viral infection: Molecular mechanisms and in vivo implications
    • Takada, A. & Kawaoka, Y. (2003). Antibody-dependent enhancement of viral infection: molecular mechanisms and in vivo implications. Rev Med Virol 13, 387-398.
    • (2003) Rev. Med. Virol. , vol.13 , pp. 387-398
    • Takada, A.1    Kawaoka, Y.2
  • 59
    • 0038467640 scopus 로고    scopus 로고
    • Antibody-dependent enhancement of Ebola virus infection
    • Takada, A., Feldmann, H., Ksiazek, T. G. & Kawaoka, Y. (2003). Antibody-dependent enhancement of Ebola virus infection. J Virol 77, 7539-7544.
    • (2003) J. Virol. , vol.77 , pp. 7539-7544
    • Takada, A.1    Feldmann, H.2    Ksiazek, T.G.3    Kawaoka, Y.4
  • 60
    • 12144290776 scopus 로고    scopus 로고
    • Human macrophage C-type lectin specific for galactose and N-acetylgalactosamine promotes filovirus entry
    • 7 other authors
    • Takada, A., Fujioka, K., Tsuiji, M. & 7 other authors (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    Fujioka, K.2    Tsuiji, M.3
  • 64
    • 1242319488 scopus 로고    scopus 로고
    • Raji B cells, misidentified as THP-1 cells, stimulate DC-SIGN-mediated HIV transmission
    • Wu, L., Martin, T. D., Carrington, M. & Kewal Ramani, V. N. (2004). Raji B cells, misidentified as THP-1 cells, stimulate DC-SIGN-mediated HIV transmission. Virology 318, 17-23.
    • (2004) Virology , vol.318 , pp. 17-23
    • Wu, L.1    Martin, T.D.2    Carrington, M.3    Kewal Ramani, V.N.4
  • 65
    • 1842450254 scopus 로고    scopus 로고
    • Interaction of mannose-binding lectin with HIV type 1 is sufficient for virus opsonization but not neutralization
    • Ying, H., Ji, X., Hart, M. L., Gupta, K., Saifuddin, M., Zariffard, M. R. & Spear, G. T. (2004). Interaction of mannose-binding lectin with HIV type 1 is sufficient for virus opsonization but not neutralization. AIDS Res Hum Retroviruses 20, 327-335.
    • (2004) AIDS Res. Hum. Retroviruses , vol.20 , pp. 327-335
    • Ying, H.1    Ji, X.2    Hart, M.L.3    Gupta, K.4    Saifuddin, M.5    Zariffard, M.R.6    Spear, G.T.7
  • 66
    • 3042726675 scopus 로고    scopus 로고
    • Dynamics of complement hemolytic activity in experimental Ebola infection
    • (in Russian)
    • Zabavichene, N. M. & Chepurnov, A. A. (2004). Dynamics of complement hemolytic activity in experimental Ebola infection. Vopr Virusol 49, 21-25 (in Russian).
    • (2004) Vopr. Virusol. , vol.49 , pp. 21-25
    • Zabavichene, N.M.1    Chepurnov, A.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.