메뉴 건너뛰기




Volumn 333, Issue 2, 2005, Pages 284-292

Antiviral activity of human lactoferrin: Inhibition of alphavirus interaction with heparan sulfate

Author keywords

Antiviral; Heparan sulfate; Lactoferrin; Liposome; Receptor; Semliki Forest virus; Sindbis virus

Indexed keywords

LACTOFERRIN; LIPOSOME;

EID: 13844250553     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2005.01.010     Document Type: Article
Times cited : (68)

References (58)
  • 3
    • 0034633834 scopus 로고    scopus 로고
    • Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice
    • K.A. Bernard, W.B. Klimstra, and R.E. Johnston Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice Virology 276 2000 93 103
    • (2000) Virology , vol.276 , pp. 93-103
    • Bernard, K.A.1    Klimstra, W.B.2    Johnston, R.E.3
  • 5
    • 0035159830 scopus 로고    scopus 로고
    • Cell surface heparan sulfate is a receptor for human herpesvirus 8 and interacts with envelope glycoprotein K8.1
    • A. Birkmann, K. Mahr, A. Ensser, S. Yaguboglu, F. Titgemeyer, B. Fleckenstein, and F. Neipel Cell surface heparan sulfate is a receptor for human herpesvirus 8 and interacts with envelope glycoprotein K8.1 J. Virol. 75 2001 11583 11593
    • (2001) J. Virol. , vol.75 , pp. 11583-11593
    • Birkmann, A.1    Mahr, K.2    Ensser, A.3    Yaguboglu, S.4    Titgemeyer, F.5    Fleckenstein, B.6    Neipel, F.7
  • 6
    • 50549164858 scopus 로고
    • A rapid and sensitive sub-micro phosphorus determination
    • C.J.F Böttcher, C.M. van Gent, and C. Pries A rapid and sensitive sub-micro phosphorus determination Anal. Chim. Acta 24 1961 203 204
    • (1961) Anal. Chim. Acta , vol.24 , pp. 203-204
    • Böttcher, J.F.1    Van Gent, C.M.2    Pries, C.3
  • 7
    • 0027509351 scopus 로고
    • Membrane fusion of Semliki Forest virus in a model system: Correlation between fusion kinetics and structural changes in the envelope glycoprotein
    • R. Bron, J.M. Wahlberg, H. Garoff, and J. Wilschut Membrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein EMBO J. 12 1993 693 701
    • (1993) EMBO J. , vol.12 , pp. 693-701
    • Bron, R.1    Wahlberg, J.M.2    Garoff, H.3    Wilschut, J.4
  • 8
    • 0031849754 scopus 로고    scopus 로고
    • Binding of Sindbis virus to cell surface heparan sulfate
    • A.P. Byrnes, and D.E. Griffin Binding of Sindbis virus to cell surface heparan sulfate J. Virol. 72 1998 7349 7356
    • (1998) J. Virol. , vol.72 , pp. 7349-7356
    • Byrnes, A.P.1    Griffin, D.E.2
  • 10
    • 0027315907 scopus 로고
    • Initiation of human cytomegalovirus-infection requires initial interaction with cell surface heparan sulfate
    • T. Compton, D.M. Nowlin, and N.R. Cooper Initiation of human cytomegalovirus-infection requires initial interaction with cell surface heparan sulfate Virology 193 1993 834 841
    • (1993) Virology , vol.193 , pp. 834-841
    • Compton, T.1    Nowlin, D.M.2    Cooper, N.R.3
  • 11
    • 0022473613 scopus 로고
    • A single nucleotide change in the E2 glycoprotein gene of Sindbis virus affects penetration rate in cell culture and virulence in neonatal mice
    • N.L. Davis, F.J. Fuller, W.G. Dougherty, R.A. Olmsted, and R.E. Johnston A single nucleotide change in the E2 glycoprotein gene of Sindbis virus affects penetration rate in cell culture and virulence in neonatal mice Proc. Natl. Acad. Sci. U.S.A. 83 1986 6771 6775
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 6771-6775
    • Davis, N.L.1    Fuller, F.J.2    Dougherty, W.G.3    Olmsted, R.A.4    Johnston, R.E.5
  • 15
    • 0036669621 scopus 로고    scopus 로고
    • The role of breastfeeding in prevention of neonatal infection
    • L.A. Hanson, and M. Korotkova The role of breastfeeding in prevention of neonatal infection Semin. Neonatol. 7 2002 275 281
    • (2002) Semin. Neonatol. , vol.7 , pp. 275-281
    • Hanson, L.A.1    Korotkova, M.2
  • 16
    • 0029080953 scopus 로고
    • Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro
    • M.C. Harmsen, P.J. Swart, M.P. Debethune, R. Pauwels, E. Declercq, T.H. The, and D.K.F. Meijer Antiviral effects of plasma and milk proteins: lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro J. Infect. Dis. 172 1995 380 388
    • (1995) J. Infect. Dis. , vol.172 , pp. 380-388
    • Harmsen, M.C.1    Swart, P.J.2    Debethune, M.P.3    Pauwels, R.4    Declercq, E.5    The, T.H.6    Meijer, D.K.F.7
  • 17
    • 0028114753 scopus 로고
    • Inhibition with lactoferrin of in vitro infection with human herpes virus
    • K. Hasegawa, W. Motsuchi, S. Tanaka, and S. Dosako Inhibition with lactoferrin of in vitro infection with human herpes virus Jpn. J. Med. Sci. Biol. 47 1994 73 85
    • (1994) Jpn. J. Med. Sci. Biol. , vol.47 , pp. 73-85
    • Hasegawa, K.1    Motsuchi, W.2    Tanaka, S.3    Dosako, S.4
  • 18
    • 0034984146 scopus 로고    scopus 로고
    • An amino acid substitution in the coding region of the E2 glycoprotein adapts Ross River virus to utilize heparan sulfate as an attachment moiety
    • M.L. Heil, A. Albee, J.H. Strauss, and R.J. Kuhn An amino acid substitution in the coding region of the E2 glycoprotein adapts Ross River virus to utilize heparan sulfate as an attachment moiety J. Virol. 75 2001 6303 6309
    • (2001) J. Virol. , vol.75 , pp. 6303-6309
    • Heil, M.L.1    Albee, A.2    Strauss, J.H.3    Kuhn, R.J.4
  • 19
    • 0018853517 scopus 로고
    • On the entry of Semliki Forest virus into BHK-21 cells
    • A. Helenius, J. Kartenbeck, K. Simons, and E. Fries On the entry of Semliki Forest virus into BHK-21 cells J. Cell Biol. 84 1980 404 420
    • (1980) J. Cell Biol. , vol.84 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3    Fries, E.4
  • 20
    • 0033765641 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans initiate dengue virus infection of hepatocytes
    • P. Hilgard, and R. Stockert Heparan sulfate proteoglycans initiate dengue virus infection of hepatocytes Hepatology 32 2000 1069 1077
    • (2000) Hepatology , vol.32 , pp. 1069-1077
    • Hilgard, P.1    Stockert, R.2
  • 24
    • 0029108852 scopus 로고
    • Membrane fusion and the alphavirus life cycle
    • M. Kielian Membrane fusion and the alphavirus life cycle Adv. Virus Res. 45 1995 113 151
    • (1995) Adv. Virus Res. , vol.45 , pp. 113-151
    • Kielian, M.1
  • 25
    • 0031869503 scopus 로고    scopus 로고
    • Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor
    • W.B. Klimstra, K.D. Ryman, and R.E. Johnston Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor J. Virol. 72 1998 7357 7366
    • (1998) J. Virol. , vol.72 , pp. 7357-7366
    • Klimstra, W.B.1    Ryman, K.D.2    Johnston, R.E.3
  • 26
    • 0032775770 scopus 로고    scopus 로고
    • The furin protease cleavage recognition sequence of sindbis virus PE2 can mediate virion attachment to cell surface heparan sulfate
    • W.B. Klimstra, H.W. Heidner, and R.E. Johnston The furin protease cleavage recognition sequence of sindbis virus PE2 can mediate virion attachment to cell surface heparan sulfate J. Virol. 73 1999 6299 6306
    • (1999) J. Virol. , vol.73 , pp. 6299-6306
    • Klimstra, W.B.1    Heidner, H.W.2    Johnston, R.E.3
  • 27
    • 14744304517 scopus 로고
    • A new generation of animal cell expression vectors based on the Semliki Forest virus replicon
    • P. Liljeström, and H. Garoff A new generation of animal cell expression vectors based on the Semliki Forest virus replicon Biotechnology 9 1991 1356 1361
    • (1991) Biotechnology , vol.9 , pp. 1356-1361
    • Liljeström, P.1    Garoff, H.2
  • 28
    • 0025912001 scopus 로고
    • In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: The small 6,000-molecular-weight membrane protein modulates virus release
    • P. Liljeström, S. Lusa, D. Huylebroeck, and H. Garoff In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6,000-molecular-weight membrane protein modulates virus release J. Virol. 65 1991 4107 4113
    • (1991) J. Virol. , vol.65 , pp. 4107-4113
    • Liljeström, P.1    Lusa, S.2    Huylebroeck, D.3    Garoff, H.4
  • 29
    • 0037108680 scopus 로고    scopus 로고
    • Lactoferrin inhibits enterovirus 71 infection of human embryonal rhabdomyosarcoma cells in vitro
    • T.Y. Lin, C. Chu, and C.H. Chiu Lactoferrin inhibits enterovirus 71 infection of human embryonal rhabdomyosarcoma cells in vitro J. Infect. Dis. 186 2002 1161 1164
    • (2002) J. Infect. Dis. , vol.186 , pp. 1161-1164
    • Lin, T.Y.1    Chu, C.2    Chiu, C.H.3
  • 30
    • 0027978954 scopus 로고
    • Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin
    • D.M. Mann, E. Romm, and M. Migliorini Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin J. Biol. Chem. 269 1994 23661 23667
    • (1994) J. Biol. Chem. , vol.269 , pp. 23661-23667
    • Mann, D.M.1    Romm, E.2    Migliorini, M.3
  • 34
    • 0020724144 scopus 로고
    • Penetration of Semliki Forest virus from acidic prelysosomal vacuoles
    • M. Marsh, E. Bolzau, and A. Helenius Penetration of Semliki Forest virus from acidic prelysosomal vacuoles Cell 32 1983 931 940
    • (1983) Cell , vol.32 , pp. 931-940
    • Marsh, M.1    Bolzau, E.2    Helenius, A.3
  • 39
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • G.L. Peterson A simplification of the protein assay method of Lowry et al. which is more generally applicable Anal. Biochem. 83 1977 346 356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 40
    • 0031762646 scopus 로고    scopus 로고
    • Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection
    • P. Puddu, P. Borghi, S. Gessani, P. Valenti, F. Belardelli, and L. Seganti Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection Int. J. Biochem. Cell Biol. 30 1998 1055 1063
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 1055-1063
    • Puddu, P.1    Borghi, P.2    Gessani, S.3    Valenti, P.4    Belardelli, F.5    Seganti, L.6
  • 41
    • 0024565079 scopus 로고
    • Sindbis virus mutations which coordinately affect glycoprotein processing, penetration, and virulence in mice
    • D.L. Russel, J.M. Dalrymple, and R.E. Johnston Sindbis virus mutations which coordinately affect glycoprotein processing, penetration, and virulence in mice J. Virol. 63 1989 1619 1629
    • (1989) J. Virol. , vol.63 , pp. 1619-1629
    • Russel, D.L.1    Dalrymple, J.M.2    Johnston, R.E.3
  • 42
    • 0030971779 scopus 로고    scopus 로고
    • Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle
    • D. Sa-Carvalho, E. Rieder, B. Baxt, R. Rodarte, A. Tanuri, and P.W. Mason Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle J. Virol. 71 1997 5115 5123
    • (1997) J. Virol. , vol.71 , pp. 5115-5123
    • Sa-Carvalho, D.1    Rieder, E.2    Baxt, B.3    Rodarte, R.4    Tanuri, A.5    Mason, P.W.6
  • 43
    • 0034883314 scopus 로고    scopus 로고
    • Herpesviruses and heparan sulfate: An intimate relationship in aid of viral entry
    • D. Shukla, and P.G. Spear Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry J. Clin. Invest. 108 2001 503 510
    • (2001) J. Clin. Invest. , vol.108 , pp. 503-510
    • Shukla, D.1    Spear, P.G.2
  • 44
    • 0032874859 scopus 로고    scopus 로고
    • Low-pH dependent fusion of Sindbis virus with receptor free cholesterol- and sphingomyelin-containing liposomes
    • J.M. Smit, R. Bittman, and J. Wilschut Low-pH dependent fusion of Sindbis virus with receptor free cholesterol- and sphingomyelin-containing liposomes J. Virol. 73 1999 8476 8484
    • (1999) J. Virol. , vol.73 , pp. 8476-8484
    • Smit, J.M.1    Bittman, R.2    Wilschut, J.3
  • 45
    • 0034761692 scopus 로고    scopus 로고
    • PE2 cleavage mutants of Sindbis virus: Correlation between viral infectivity and pH-dependent membrane fusion activation of the spike heterodimer
    • J.M. Smit, W.B. Klimstra, K. Ryman, R. Bittman, R.E. Johnston, and J. Wilschut PE2 cleavage mutants of Sindbis virus: correlation between viral infectivity and pH-dependent membrane fusion activation of the spike heterodimer J. Virol. 75 2001 11196 11204
    • (2001) J. Virol. , vol.75 , pp. 11196-11204
    • Smit, J.M.1    Klimstra, W.B.2    Ryman, K.3    Bittman, R.4    Johnston, R.E.5    Wilschut, J.6
  • 46
    • 0036784563 scopus 로고    scopus 로고
    • Adaptation of alphaviruses to heparan sulfate: Interaction of Sindbis and Semliki Forest viruses with liposomes containing lipid-conjugated heparin
    • J.M. Smit, B.L. Waarts, K. Kimata, W.B. Klimstra, R. Bittman, and J. Wilschut Adaptation of alphaviruses to heparan sulfate: interaction of Sindbis and Semliki Forest viruses with liposomes containing lipid-conjugated heparin J. Virol. 76 2002 10128 10137
    • (2002) J. Virol. , vol.76 , pp. 10128-10137
    • Smit, J.M.1    Waarts, B.L.2    Kimata, K.3    Klimstra, W.B.4    Bittman, R.5    Wilschut, J.6
  • 47
    • 0242380863 scopus 로고    scopus 로고
    • Liposomes as target membranes in the study of virus-receptor interaction and membrane fusion
    • J.M. Smit, B.L. Waarts, R. Bittman, and J. Wilschut Liposomes as target membranes in the study of virus-receptor interaction and membrane fusion Methods Enzymol. 372 2003 374 391
    • (2003) Methods Enzymol. , vol.372 , pp. 374-391
    • Smit, J.M.1    Waarts, B.L.2    Bittman, R.3    Wilschut, J.4
  • 48
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • J.H. Strauss, and E.G. Strauss The alphaviruses: gene expression, replication, and evolution Microbiol. Rev. 58 1994 491 562
    • (1994) Microbiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 49
    • 0027264507 scopus 로고
    • Preparation of lipid-derivatized glycosaminoglycans to probe a regulatory function of the carbohydrate moieties of proteoglycans in cell-matrix interaction
    • N. Sugiura, K. Sakurai, Y. Hori, K. Karasawa, S. Suzuki, and K. Kimata Preparation of lipid-derivatized glycosaminoglycans to probe a regulatory function of the carbohydrate moieties of proteoglycans in cell-matrix interaction J. Biol. Chem. 21 1993 15779 15787
    • (1993) J. Biol. Chem. , vol.21 , pp. 15779-15787
    • Sugiura, N.1    Sakurai, K.2    Hori, Y.3    Karasawa, K.4    Suzuki, S.5    Kimata, K.6
  • 50
    • 0031906147 scopus 로고    scopus 로고
    • Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions
    • C. Summerford, and R.J. Samulski Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions J. Virol. 72 1998 1438 1445
    • (1998) J. Virol. , vol.72 , pp. 1438-1445
    • Summerford, C.1    Samulski, R.J.2
  • 52
    • 0036438885 scopus 로고    scopus 로고
    • Glycosaminoglycan-binding ability is a feature of wild-type strains of herpes simplex virus type 1
    • E. Trybala, A. Roth, M. Johansson, J.A. Liljeqvist, E. Rekabdar, O. Larm, and T. Bergstrom Glycosaminoglycan-binding ability is a feature of wild-type strains of herpes simplex virus type 1 Virology 302 2002 413 419
    • (2002) Virology , vol.302 , pp. 413-419
    • Trybala, E.1    Roth, A.2    Johansson, M.3    Liljeqvist, J.A.4    Rekabdar, E.5    Larm, O.6    Bergstrom, T.7
  • 53
    • 1842416505 scopus 로고    scopus 로고
    • Amino acid changes in the Sindbis virus E2 glycoprotein that increase neurovirulence improve entry into neuroblastoma cells
    • P.C. Tucker, S.H. Lee, N. Bui, D. Martinie, and D.E. Griffin Amino acid changes in the Sindbis virus E2 glycoprotein that increase neurovirulence improve entry into neuroblastoma cells J. Virol. 71 1997 6106 6112
    • (1997) J. Virol. , vol.71 , pp. 6106-6112
    • Tucker, P.C.1    Lee, S.H.2    Bui, N.3    Martinie, D.4    Griffin, D.E.5
  • 54
    • 0033959545 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans on the cell surface: Versatile coordinators of cellular functions
    • S. Tumova, A. Woods, and J.R. Couchman Heparan sulfate proteoglycans on the cell surface: versatile coordinators of cellular functions Int. J. Biochem. Cell Biol. 32 2000 269 288
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 269-288
    • Tumova, S.1    Woods, A.2    Couchman, J.R.3
  • 55
    • 0030664951 scopus 로고    scopus 로고
    • N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA
    • P.H. van Berkel, M.E. Geerts, H.A. van Veen, M. Mericskay, H.A. de Boer, and J.H. Nuijens N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA Biochem. J. 328 1997 145 151
    • (1997) Biochem. J. , vol.328 , pp. 145-151
    • Van Berkel, P.H.1    Geerts, M.E.2    Van Veen, H.A.3    Mericskay, M.4    De Boer, H.A.5    Nuijens, J.H.6
  • 57
    • 0028901203 scopus 로고
    • Characterization of the glycosaminoglycan-binding region of lactoferrin
    • H.F. Wu, D.M. Monroe, and F.C. Church Characterization of the glycosaminoglycan-binding region of lactoferrin Arch. Biochem. Biophys. 317 1995 85 92
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 85-92
    • Wu, H.F.1    Monroe, D.M.2    Church, F.C.3
  • 58
    • 0035915493 scopus 로고    scopus 로고
    • The binding of lactoferrin to glycosaminoglycans on enterocyte-like HT29-18-C1 cells is mediated through basic residues located in the N-terminus
    • I. Yazidi-Belkoura, D. Legrand, J. Nuijens, M.C. Slomianny, P. van Berkel, and G. Spik The binding of lactoferrin to glycosaminoglycans on enterocyte-like HT29-18-C1 cells is mediated through basic residues located in the N-terminus Biochim. Biophys. Acta 1568 2001 197 204
    • (2001) Biochim. Biophys. Acta , vol.1568 , pp. 197-204
    • Yazidi-Belkoura, I.1    Legrand, D.2    Nuijens, J.3    Slomianny, M.C.4    Van Berkel, P.5    Spik, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.