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Volumn 75, Issue 3, 2007, Pages 258-265

The anti-papillomavirus activity of human and bovine lactoferricin

Author keywords

Antiviral activity; Human papillomavirus; Lactoferricin; Lactoferrin

Indexed keywords

LACTOFERRICIN; LACTOFERRIN;

EID: 34250211795     PISSN: 01663542     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.antiviral.2007.03.012     Document Type: Article
Times cited : (71)

References (78)
  • 1
    • 33847043131 scopus 로고    scopus 로고
    • Bovine lactoferrin inhibits echovirus endocytic pathway by interacting with viral structural polypeptides
    • Ammendolia M.G., Pietrantoni A., Tinari A., Valenti P., and Superti F. Bovine lactoferrin inhibits echovirus endocytic pathway by interacting with viral structural polypeptides. Antiviral Res. 73 3 (2007) 151-160
    • (2007) Antiviral Res. , vol.73 , Issue.3 , pp. 151-160
    • Ammendolia, M.G.1    Pietrantoni, A.2    Tinari, A.3    Valenti, P.4    Superti, F.5
  • 2
    • 0034960102 scopus 로고    scopus 로고
    • Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts
    • Andersen J.H., Osbakk S.A., Vorland L.H., Traavik T., and Gutteberg T.J. Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts. Antiviral Res. 51 2 (2001) 141-149
    • (2001) Antiviral Res. , vol.51 , Issue.2 , pp. 141-149
    • Andersen, J.H.1    Osbakk, S.A.2    Vorland, L.H.3    Traavik, T.4    Gutteberg, T.J.5
  • 3
    • 0037721339 scopus 로고    scopus 로고
    • Lactoferrin and lactoferricin inhibit Herpes simplex 1 and 2 infection and exhibit synergy when combined with acyclovir
    • Andersen J.H., Jenssen H., and Gutteberg T.J. Lactoferrin and lactoferricin inhibit Herpes simplex 1 and 2 infection and exhibit synergy when combined with acyclovir. Antiviral Res. 58 3 (2003) 209-215
    • (2003) Antiviral Res. , vol.58 , Issue.3 , pp. 209-215
    • Andersen, J.H.1    Jenssen, H.2    Gutteberg, T.J.3
  • 4
    • 4344615913 scopus 로고    scopus 로고
    • Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface
    • Andersen J.H., Jenssen H., Sandvik K., and Gutteberg T.J. Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface. J. Med. Virol. 74 2 (2004) 262-271
    • (2004) J. Med. Virol. , vol.74 , Issue.2 , pp. 262-271
    • Andersen, J.H.1    Jenssen, H.2    Sandvik, K.3    Gutteberg, T.J.4
  • 6
    • 4544260057 scopus 로고    scopus 로고
    • High-risk papillomavirus infection is associated with altered antibody responses in genital tract: non-specific responses in HPV infection
    • Bard E., Riethmuller D., Meillet D., Pretet J.L., Schaal J.P., Mougin C., and Seilles E. High-risk papillomavirus infection is associated with altered antibody responses in genital tract: non-specific responses in HPV infection. Viral Immunol. 17 3 (2004) 381-389
    • (2004) Viral Immunol. , vol.17 , Issue.3 , pp. 381-389
    • Bard, E.1    Riethmuller, D.2    Meillet, D.3    Pretet, J.L.4    Schaal, J.P.5    Mougin, C.6    Seilles, E.7
  • 7
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W., Takase M., Wakabayashi H., Kawase K., and Tomita M. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol. 73 6 (1992) 472-479
    • (1992) J. Appl. Bacteriol. , vol.73 , Issue.6 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5
  • 10
    • 0028795617 scopus 로고
    • Nested PCR approach for detection and typing of epidermodysplasia verruciformis-associated human papillomavirus types in cutaneous cancers from renal transplant recipients
    • Berkhout R.J., Tieben L.M., Smits H.L., Bavinck J.N., Vermeer B.J., and ter Schegget J. Nested PCR approach for detection and typing of epidermodysplasia verruciformis-associated human papillomavirus types in cutaneous cancers from renal transplant recipients. J. Clin. Microbiol. 33 3 (1995) 690-695
    • (1995) J. Clin. Microbiol. , vol.33 , Issue.3 , pp. 690-695
    • Berkhout, R.J.1    Tieben, L.M.2    Smits, H.L.3    Bavinck, J.N.4    Vermeer, B.J.5    ter Schegget, J.6
  • 11
    • 0036289423 scopus 로고    scopus 로고
    • Characterization of the anti-HIV effects of native lactoferrin and other milk proteins and protein-derived peptides
    • Berkhout B., van Wamel J.L., Beljaars L., Meijer D.K., Visser S., and Floris R. Characterization of the anti-HIV effects of native lactoferrin and other milk proteins and protein-derived peptides. Antiviral Res. 55 2 (2002) 341-355
    • (2002) Antiviral Res. , vol.55 , Issue.2 , pp. 341-355
    • Berkhout, B.1    van Wamel, J.L.2    Beljaars, L.3    Meijer, D.K.4    Visser, S.5    Floris, R.6
  • 12
  • 13
    • 2542430315 scopus 로고    scopus 로고
    • Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity
    • Bousarghin L., Touze A., Yvonnet B., and Coursaget P. Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity. J. Med. Virol. 73 3 (2004) 474-480
    • (2004) J. Med. Virol. , vol.73 , Issue.3 , pp. 474-480
    • Bousarghin, L.1    Touze, A.2    Yvonnet, B.3    Coursaget, P.4
  • 14
    • 0027428420 scopus 로고
    • Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis
    • Britigan B.E., Hayek M.B., Doebbeling B.N., and Fick Jr. R.B. Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis. Infect. Immun. 61 12 (1993) 5049-5055
    • (1993) Infect. Immun. , vol.61 , Issue.12 , pp. 5049-5055
    • Britigan, B.E.1    Hayek, M.B.2    Doebbeling, B.N.3    Fick Jr., R.B.4
  • 15
    • 0346688642 scopus 로고    scopus 로고
    • Efficient intracellular assembly of papillomaviral vectors
    • Buck C.B., Pastrana D.V., Lowy D.R., and Schiller J.T. Efficient intracellular assembly of papillomaviral vectors. J. Virol. 78 2 (2004) 751-757
    • (2004) J. Virol. , vol.78 , Issue.2 , pp. 751-757
    • Buck, C.B.1    Pastrana, D.V.2    Lowy, D.R.3    Schiller, J.T.4
  • 16
    • 33644843775 scopus 로고    scopus 로고
    • Generation of HPV pseudovirions using transfection and their use in neutralization assays
    • Buck C.B., Pastrana D.V., Lowy D.R., and Schiller J.T. Generation of HPV pseudovirions using transfection and their use in neutralization assays. Methods Mol. Med. 119 (2005) 445-462
    • (2005) Methods Mol. Med. , vol.119 , pp. 445-462
    • Buck, C.B.1    Pastrana, D.V.2    Lowy, D.R.3    Schiller, J.T.4
  • 20
    • 0023639356 scopus 로고
    • Preliminary observations on lactoferrin secretion in human vaginal mucus: variation during the menstrual cycle, evidence of hormonal regulation, and implications for infection with Neisseria gonorrhoeae
    • Cohen M.S., Britigan B.E., French M., and Bean K. Preliminary observations on lactoferrin secretion in human vaginal mucus: variation during the menstrual cycle, evidence of hormonal regulation, and implications for infection with Neisseria gonorrhoeae. Am. J. Obstet. Gynecol. 157 5 (1987) 1122-1125
    • (1987) Am. J. Obstet. Gynecol. , vol.157 , Issue.5 , pp. 1122-1125
    • Cohen, M.S.1    Britigan, B.E.2    French, M.3    Bean, K.4
  • 21
    • 0035899891 scopus 로고    scopus 로고
    • Gene transfer using human papillomavirus pseudovirions varies according to virus genotype and requires cell surface heparan sulfate
    • Combita A.L., Touze A., Bousarghin L., Sizaret P.Y., Munoz N., and Coursaget P. Gene transfer using human papillomavirus pseudovirions varies according to virus genotype and requires cell surface heparan sulfate. FEMS Microbiol. Lett. 204 1 (2001) 183-188
    • (2001) FEMS Microbiol. Lett. , vol.204 , Issue.1 , pp. 183-188
    • Combita, A.L.1    Touze, A.2    Bousarghin, L.3    Sizaret, P.Y.4    Munoz, N.5    Coursaget, P.6
  • 22
    • 0025778068 scopus 로고
    • p53 point mutation in HPV negative human cervical carcinoma cell lines
    • Crook T., Wrede D., and Vousden K.H. p53 point mutation in HPV negative human cervical carcinoma cell lines. Oncogene 6 5 (1991) 873-875
    • (1991) Oncogene , vol.6 , Issue.5 , pp. 873-875
    • Crook, T.1    Wrede, D.2    Vousden, K.H.3
  • 23
    • 4644352291 scopus 로고    scopus 로고
    • Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression
    • Day P.M., Baker C.C., Lowy D.R., and Schiller J.T. Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression. Proc. Natl. Acad. Sci. U.S.A. 101 39 (2004) 14252-14257
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.39 , pp. 14252-14257
    • Day, P.M.1    Baker, C.C.2    Lowy, D.R.3    Schiller, J.T.4
  • 26
    • 0031115106 scopus 로고    scopus 로고
    • Antibacterial peptides of bovine lactoferrin: purification and characterization
    • Dionysius D.A., and Milne J.M. Antibacterial peptides of bovine lactoferrin: purification and characterization. J. Dairy Sci. 80 4 (1997) 667-674
    • (1997) J. Dairy Sci. , vol.80 , Issue.4 , pp. 667-674
    • Dionysius, D.A.1    Milne, J.M.2
  • 27
    • 0037530219 scopus 로고    scopus 로고
    • Carboxy-fluorescein diacetate, succinimidyl ester labeled papillomavirus virus-like particles fluoresce after internalization and interact with heparan sulfate for binding and entry
    • Drobni P., Mistry N., McMillan N., and Evander M. Carboxy-fluorescein diacetate, succinimidyl ester labeled papillomavirus virus-like particles fluoresce after internalization and interact with heparan sulfate for binding and entry. Virology 310 1 (2003) 163-172
    • (2003) Virology , vol.310 , Issue.1 , pp. 163-172
    • Drobni, P.1    Mistry, N.2    McMillan, N.3    Evander, M.4
  • 28
    • 4644281454 scopus 로고    scopus 로고
    • Lactoferrin inhibits human papillomavirus binding and uptake in vitro
    • Drobni P., Naslund J., and Evander M. Lactoferrin inhibits human papillomavirus binding and uptake in vitro. Antiviral Res. 64 1 (2004) 63-68
    • (2004) Antiviral Res. , vol.64 , Issue.1 , pp. 63-68
    • Drobni, P.1    Naslund, J.2    Evander, M.3
  • 30
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., and Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462 1-2 (1999) 11-28
    • (1999) Biochim. Biophys. Acta , vol.1462 , Issue.1-2 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 31
    • 0030614485 scopus 로고    scopus 로고
    • Identification of the alpha 6 integrin as a candidate receptor for papillomaviruses
    • Evander M., Frazer I.H., Payne E., Qi Y.M., Hengst K., and McMillan N.A. Identification of the alpha 6 integrin as a candidate receptor for papillomaviruses. J. Virol. 71 3 (1997) 2449-2456
    • (1997) J. Virol. , vol.71 , Issue.3 , pp. 2449-2456
    • Evander, M.1    Frazer, I.H.2    Payne, E.3    Qi, Y.M.4    Hengst, K.5    McMillan, N.A.6
  • 32
    • 0030690035 scopus 로고    scopus 로고
    • Neoplastic transformation of the endocervix associated with downregulation of lactoferrin expression
    • Farley J., Loup D., Nelson M., Mitchell A., Esplund G., Macri C., Harrison C., and Gray K. Neoplastic transformation of the endocervix associated with downregulation of lactoferrin expression. Mol. Carcinog. 20 2 (1997) 240-250
    • (1997) Mol. Carcinog. , vol.20 , Issue.2 , pp. 240-250
    • Farley, J.1    Loup, D.2    Nelson, M.3    Mitchell, A.4    Esplund, G.5    Macri, C.6    Harrison, C.7    Gray, K.8
  • 33
    • 28344438950 scopus 로고    scopus 로고
    • Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties
    • Gifford J.L., Hunter H.N., and Vogel H.J. Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell. Mol. Life Sci. 62 22 (2005) 2588-2598
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.22 , pp. 2588-2598
    • Gifford, J.L.1    Hunter, H.N.2    Vogel, H.J.3
  • 34
    • 0035156505 scopus 로고    scopus 로고
    • Human papillomavirus infection requires cell surface heparan sulfate
    • Giroglou T., Florin L., Schafer F., Streeck R.E., and Sapp M. Human papillomavirus infection requires cell surface heparan sulfate. J. Virol. 75 3 (2001) 1565-1570
    • (2001) J. Virol. , vol.75 , Issue.3 , pp. 1565-1570
    • Giroglou, T.1    Florin, L.2    Schafer, F.3    Streeck, R.E.4    Sapp, M.5
  • 36
    • 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
    • Harmsen M.C., Swart P.J., de Bethune M.P., Pauwels R., De Clercq E., The T.H., and Meijer D.K. 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 2 (1995) 380-388
    • (1995) J. Infect. Dis. , vol.172 , Issue.2 , pp. 380-388
    • Harmsen, M.C.1    Swart, P.J.2    de Bethune, M.P.3    Pauwels, R.4    De Clercq, E.5    The, T.H.6    Meijer, D.K.7
  • 37
    • 0028114753 scopus 로고
    • Inhibition with lactoferrin of in vitro infection with human herpes virus
    • Hasegawa K., Motsuchi W., Tanaka S., and Dosako S. Inhibition with lactoferrin of in vitro infection with human herpes virus. Jpn. J. Med. Sci. Biol. 47 2 (1994) 73-85
    • (1994) Jpn. J. Med. Sci. Biol. , vol.47 , Issue.2 , pp. 73-85
    • Hasegawa, K.1    Motsuchi, W.2    Tanaka, S.3    Dosako, S.4
  • 38
    • 0033801238 scopus 로고    scopus 로고
    • Human lactoferrin and peptides derived from a surface-exposed helical region reduce experimental Escherichia coli urinary tract infection in mice
    • Haversen L.A., Engberg I., Baltzer L., Dolphin G., Hanson L.A., and Mattsby-Baltzer I. Human lactoferrin and peptides derived from a surface-exposed helical region reduce experimental Escherichia coli urinary tract infection in mice. Infect. Immun. 68 10 (2000) 5816-5823
    • (2000) Infect. Immun. , vol.68 , Issue.10 , pp. 5816-5823
    • Haversen, L.A.1    Engberg, I.2    Baltzer, L.3    Dolphin, G.4    Hanson, L.A.5    Mattsby-Baltzer, I.6
  • 39
    • 0028910517 scopus 로고
    • Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA
    • He J., and Furmanski P. Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature 373 6516 (1995) 721-724
    • (1995) Nature , vol.373 , Issue.6516 , pp. 721-724
    • He, J.1    Furmanski, P.2
  • 41
    • 23044463641 scopus 로고    scopus 로고
    • Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent
    • Hunter H.N., Demcoe A.R., Jenssen H., Gutteberg T.J., and Vogel H.J. Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent. Antimicrob. Agents Chemother. 49 8 (2005) 3387-3395
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.8 , pp. 3387-3395
    • Hunter, H.N.1    Demcoe, A.R.2    Jenssen, H.3    Gutteberg, T.J.4    Vogel, H.J.5
  • 42
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., and Vogel H.J. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 37 12 (1998) 4288-4298
    • (1998) Biochemistry , vol.37 , Issue.12 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 45
    • 0031991248 scopus 로고    scopus 로고
    • Protective effect of lactoferricin against Toxoplasma gondii infection in mice
    • Isamida T., Tanaka T., Omata Y., Yamauchi K., Shimazaki K., and Saito A. Protective effect of lactoferricin against Toxoplasma gondii infection in mice. J. Vet. Med. Sci. 60 2 (1998) 241-244
    • (1998) J. Vet. Med. Sci. , vol.60 , Issue.2 , pp. 241-244
    • Isamida, T.1    Tanaka, T.2    Omata, Y.3    Yamauchi, K.4    Shimazaki, K.5    Saito, A.6
  • 46
    • 29344463703 scopus 로고    scopus 로고
    • Anti herpes simplex virus activity of lactoferrin/lactoferricin-an example of antiviral activity of antimicrobial protein/peptide
    • Jenssen H. Anti herpes simplex virus activity of lactoferrin/lactoferricin-an example of antiviral activity of antimicrobial protein/peptide. Cell. Mol. Life Sci. 62 24 (2005) 3002-3013
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.24 , pp. 3002-3013
    • Jenssen, H.1
  • 47
    • 7444233604 scopus 로고    scopus 로고
    • A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus
    • Jenssen H., Andersen J.H., Mantzilas D., and Gutteberg T.J. A wide range of medium-sized, highly cationic, alpha-helical peptides show antiviral activity against herpes simplex virus. Antiviral Res. 64 2 (2004) 119-126
    • (2004) Antiviral Res. , vol.64 , Issue.2 , pp. 119-126
    • Jenssen, H.1    Andersen, J.H.2    Mantzilas, D.3    Gutteberg, T.J.4
  • 48
    • 0344304749 scopus 로고    scopus 로고
    • Anti-HSV activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate
    • Jenssen H., Andersen J.H., Uhlin-Hansen L., Gutteberg T.J., and Rekdal O. Anti-HSV activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate. Antiviral Res. 61 2 (2004) 101-109
    • (2004) Antiviral Res. , vol.61 , Issue.2 , pp. 101-109
    • Jenssen, H.1    Andersen, J.H.2    Uhlin-Hansen, L.3    Gutteberg, T.J.4    Rekdal, O.5
  • 49
    • 33748437826 scopus 로고    scopus 로고
    • Comparison of NMR structures and model-membrane interactions of 15-residue antimicrobial peptides derived from bovine lactoferricin
    • Jing W., Svendsen J.S., and Vogel H.J. Comparison of NMR structures and model-membrane interactions of 15-residue antimicrobial peptides derived from bovine lactoferricin. Biochem. Cell Biol. 84 3 (2006) 312-326
    • (2006) Biochem. Cell Biol. , vol.84 , Issue.3 , pp. 312-326
    • Jing, W.1    Svendsen, J.S.2    Vogel, H.J.3
  • 50
    • 0033605153 scopus 로고    scopus 로고
    • The L1 major capsid protein of human papillomavirus type 11 recombinant virus-like particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes
    • Joyce J.G., Tung J.S., Przysiecki C.T., Cook J.C., Lehman E.D., Sands J.A., Jansen K.U., and Keller P.M. The L1 major capsid protein of human papillomavirus type 11 recombinant virus-like particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes. J. Biol. Chem. 274 9 (1999) 5810-5822
    • (1999) J. Biol. Chem. , vol.274 , Issue.9 , pp. 5810-5822
    • Joyce, J.G.1    Tung, J.S.2    Przysiecki, C.T.3    Cook, J.C.4    Lehman, E.D.5    Sands, J.A.6    Jansen, K.U.7    Keller, P.M.8
  • 52
    • 0037108680 scopus 로고    scopus 로고
    • Lactoferrin inhibits enterovirus 71 infection of human embryonal rhabdomyosarcoma cells in vitro
    • Lin T.Y., Chu C., and Chiu C.H. Lactoferrin inhibits enterovirus 71 infection of human embryonal rhabdomyosarcoma cells in vitro. J. Infect. Dis. 186 8 (2002) 1161-1164
    • (2002) J. Infect. Dis. , vol.186 , Issue.8 , pp. 1161-1164
    • Lin, T.Y.1    Chu, C.2    Chiu, C.H.3
  • 54
  • 56
    • 1242300081 scopus 로고    scopus 로고
    • Inhibition of herpes simplex virus infection by lactoferrin is dependent on interference with the virus binding to glycosaminoglycans
    • Marchetti M., Trybala E., Superti F., Johansson M., and Bergstrom T. Inhibition of herpes simplex virus infection by lactoferrin is dependent on interference with the virus binding to glycosaminoglycans. Virology 318 1 (2004) 405-413
    • (2004) Virology , vol.318 , Issue.1 , pp. 405-413
    • Marchetti, M.1    Trybala, E.2    Superti, F.3    Johansson, M.4    Bergstrom, T.5
  • 57
    • 0018145209 scopus 로고
    • Distribution of transferrin, ferritin, and lactoferrin in human tissues
    • Mason D.Y., and Taylor C.R. Distribution of transferrin, ferritin, and lactoferrin in human tissues. J. Clin. Pathol. 31 4 (1978) 316-327
    • (1978) J. Clin. Pathol. , vol.31 , Issue.4 , pp. 316-327
    • Mason, D.Y.1    Taylor, C.R.2
  • 58
    • 0242383511 scopus 로고    scopus 로고
    • The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures
    • McCann K.B., Lee A., Wan J., Roginski H., and Coventry M.J. The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures. J. Appl. Microbiol. 95 5 (2003) 1026-1033
    • (2003) J. Appl. Microbiol. , vol.95 , Issue.5 , pp. 1026-1033
    • McCann, K.B.1    Lee, A.2    Wan, J.3    Roginski, H.4    Coventry, M.J.5
  • 59
    • 31444434715 scopus 로고    scopus 로고
    • Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection
    • Pietrantoni A., Ammendolia M.G., Tinari A., Siciliano R., Valenti P., and Superti F. Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection. Antiviral Res. 69 2 (2006) 98-106
    • (2006) Antiviral Res. , vol.69 , Issue.2 , pp. 98-106
    • Pietrantoni, A.1    Ammendolia, M.G.2    Tinari, A.3    Siciliano, R.4    Valenti, P.5    Superti, F.6
  • 60
    • 0029841214 scopus 로고    scopus 로고
    • In vitro generation and type-specific neutralization of a human papillomavirus type 16 virion pseudotype
    • Roden R.B., Greenstone H.L., Kirnbauer R., Booy F.P., Jessie J., Lowy D.R., and Schiller J.T. In vitro generation and type-specific neutralization of a human papillomavirus type 16 virion pseudotype. J. Virol. 70 9 (1996) 5875-5883
    • (1996) J. Virol. , vol.70 , Issue.9 , pp. 5875-5883
    • Roden, R.B.1    Greenstone, H.L.2    Kirnbauer, R.3    Booy, F.P.4    Jessie, J.5    Lowy, D.R.6    Schiller, J.T.7
  • 61
    • 33646465686 scopus 로고    scopus 로고
    • An evidence-based review of medical and surgical treatments of genital warts
    • Scheinfeld N., and Lehman D.S. An evidence-based review of medical and surgical treatments of genital warts. Dermatol. Online J. 12 3 (2006) 5
    • (2006) Dermatol. Online J. , vol.12 , Issue.3 , pp. 5
    • Scheinfeld, N.1    Lehman, D.S.2
  • 63
    • 0345599103 scopus 로고    scopus 로고
    • Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses
    • Shafti-Keramat S., Handisurya A., Kriehuber E., Meneguzzi G., Slupetzky K., and Kirnbauer R. Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses. J. Virol. 77 24 (2003) 13125-13135
    • (2003) J. Virol. , vol.77 , Issue.24 , pp. 13125-13135
    • Shafti-Keramat, S.1    Handisurya, A.2    Kriehuber, E.3    Meneguzzi, G.4    Slupetzky, K.5    Kirnbauer, R.6
  • 64
    • 33747115336 scopus 로고    scopus 로고
    • Papillomavirus and treatment
    • Snoeck R. Papillomavirus and treatment. Antiviral Res. 71 2-3 (2006) 181-191
    • (2006) Antiviral Res. , vol.71 , Issue.2-3 , pp. 181-191
    • Snoeck, R.1
  • 65
    • 0034852346 scopus 로고    scopus 로고
    • Heparan sulfate: anchor for viral intruders?
    • Spillmann D. Heparan sulfate: anchor for viral intruders?. Biochimie 83 8 (2001) 811-817
    • (2001) Biochimie , vol.83 , Issue.8 , pp. 811-817
    • Spillmann, D.1
  • 66
    • 0033787915 scopus 로고    scopus 로고
    • Antibacterial activity of 15-residue lactoferricin derivatives
    • Strom M.B., Rekdal O., and Svendsen J.S. Antibacterial activity of 15-residue lactoferricin derivatives. J. Pept. Res. 56 5 (2000) 265-274
    • (2000) J. Pept. Res. , vol.56 , Issue.5 , pp. 265-274
    • Strom, M.B.1    Rekdal, O.2    Svendsen, J.S.3
  • 67
    • 0033511021 scopus 로고    scopus 로고
    • Human papillomavirus life cycle: active and latent phases
    • Stubenrauch F., and Laimins L.A. Human papillomavirus life cycle: active and latent phases. Semin. Cancer Biol. 9 6 (1999) 379-386
    • (1999) Semin. Cancer Biol. , vol.9 , Issue.6 , pp. 379-386
    • Stubenrauch, F.1    Laimins, L.A.2
  • 68
    • 0030661831 scopus 로고    scopus 로고
    • Antirotaviral activity of milk proteins: lactoferrin prevents rotavirus infection in the enterocyte-like cell line HT-29
    • Superti F., Ammendolia M.G., Valenti P., and Seganti L. Antirotaviral activity of milk proteins: lactoferrin prevents rotavirus infection in the enterocyte-like cell line HT-29. Med. Microbiol. Immunol. (Berl) 186 2-3 (1997) 83-91
    • (1997) Med. Microbiol. Immunol. (Berl) , vol.186 , Issue.2-3 , pp. 83-91
    • Superti, F.1    Ammendolia, M.G.2    Valenti, P.3    Seganti, L.4
  • 69
    • 0029892820 scopus 로고    scopus 로고
    • Antiviral effects of milk proteins: acylation results in polyanionic compounds with potent activity against human immunodeficiency virus types 1 and 2 in vitro
    • Swart P.J., Kuipers M.E., Smit C., Pauwels R., deBethune M.P., de Clercq E., Meijer D.K., and Huisman J.G. Antiviral effects of milk proteins: acylation results in polyanionic compounds with potent activity against human immunodeficiency virus types 1 and 2 in vitro. AIDS Res. Hum. Retroviruses 12 9 (1996) 769-775
    • (1996) AIDS Res. Hum. Retroviruses , vol.12 , Issue.9 , pp. 769-775
    • Swart, P.J.1    Kuipers, M.E.2    Smit, C.3    Pauwels, R.4    deBethune, M.P.5    de Clercq, E.6    Meijer, D.K.7    Huisman, J.G.8
  • 70
    • 20344370969 scopus 로고    scopus 로고
    • Immunolocalization of lactoferrin in surgically resected pigmented skin lesions
    • Tuccari G., Giuffre G., Scarf R., Simone A., Todaro P., and Barresi G. Immunolocalization of lactoferrin in surgically resected pigmented skin lesions. Eur. J. Histochem. 49 1 (2005) 33-38
    • (2005) Eur. J. Histochem. , vol.49 , Issue.1 , pp. 33-38
    • Tuccari, G.1    Giuffre, G.2    Scarf, R.3    Simone, A.4    Todaro, P.5    Barresi, G.6
  • 71
    • 0030947009 scopus 로고    scopus 로고
    • Generation and neutralization of pseudovirions of human papillomavirus type 33
    • Unckell F., Streeck R.E., and Sapp M. Generation and neutralization of pseudovirions of human papillomavirus type 33. J. Virol. 71 4 (1997) 2934-2939
    • (1997) J. Virol. , vol.71 , Issue.4 , pp. 2934-2939
    • Unckell, F.1    Streeck, R.E.2    Sapp, M.3
  • 72
    • 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
    • van Berkel P.H., Geerts M.E., van Veen H.A., Mericskay M., de Boer H.A., and Nuijens J.H. 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 Pt 1 (1997) 145-151
    • (1997) Biochem. J. , vol.328 , Issue.PART 1 , 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
  • 75
    • 0030740063 scopus 로고    scopus 로고
    • Hepatitis C virus envelope proteins bind lactoferrin
    • Yi M., Kaneko S., Yu D.Y., and Murakami S. Hepatitis C virus envelope proteins bind lactoferrin. J. Virol. 71 8 (1997) 5997-6002
    • (1997) J. Virol. , vol.71 , Issue.8 , pp. 5997-6002
    • Yi, M.1    Kaneko, S.2    Yu, D.Y.3    Murakami, S.4
  • 76
    • 0030940982 scopus 로고    scopus 로고
    • Bovine lactoferrin and lactoferricin, a peptide derived from bovine lactoferrin, inhibit tumor metastasis in mice
    • Yoo Y.C., Watanabe S., Watanabe R., Hata K., Shimazaki K., and Azuma I. Bovine lactoferrin and lactoferricin, a peptide derived from bovine lactoferrin, inhibit tumor metastasis in mice. Jpn. J. Cancer Res. 88 2 (1997) 184-190
    • (1997) Jpn. J. Cancer Res. , vol.88 , Issue.2 , pp. 184-190
    • Yoo, Y.C.1    Watanabe, S.2    Watanabe, R.3    Hata, K.4    Shimazaki, K.5    Azuma, I.6
  • 77
    • 0032502751 scopus 로고    scopus 로고
    • DNA packaging by L1 and L2 capsid proteins of bovine papillomavirus type 1
    • Zhao K.N., Sun X.Y., Frazer I.H., and Zhou J. DNA packaging by L1 and L2 capsid proteins of bovine papillomavirus type 1. Virology 243 2 (1998) 482-491
    • (1998) Virology , vol.243 , Issue.2 , pp. 482-491
    • Zhao, K.N.1    Sun, X.Y.2    Frazer, I.H.3    Zhou, J.4
  • 78
    • 0026648295 scopus 로고
    • Definition of linear antigenic regions of the HPV16 L1 capsid protein using synthetic virion-like particles
    • Zhou J., Sun X.Y., Davies H., Crawford L., Park D., and Frazer I.H. Definition of linear antigenic regions of the HPV16 L1 capsid protein using synthetic virion-like particles. Virology 189 2 (1992) 592-599
    • (1992) Virology , vol.189 , Issue.2 , pp. 592-599
    • Zhou, J.1    Sun, X.Y.2    Davies, H.3    Crawford, L.4    Park, D.5    Frazer, I.H.6


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