메뉴 건너뛰기




Volumn 18, Issue 6, 2008, Pages 658-668

The effect of bovine whey proteins on the ability of poliovirus and Coxsackie virus to infect Vero cell cultures

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; ESTERIFICATION; RNA; VIRUSES;

EID: 43049178399     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2007.11.023     Document Type: Article
Times cited : (18)

References (46)
  • 1
    • 0002625153 scopus 로고    scopus 로고
    • Lactoferrin three-dimensional structure: A framework for interpreting function
    • Shimazaki K., Tsuda H., Tomita M., Kuwata T., and Perraudin J.P. (Eds), Excerpta Medica, Elsevier, Amsterdam, The Netherlands
    • Baker E.N. Lactoferrin three-dimensional structure: A framework for interpreting function. In: Shimazaki K., Tsuda H., Tomita M., Kuwata T., and Perraudin J.P. (Eds). Lactoferrin: Structure, function and applications (2000), Excerpta Medica, Elsevier, Amsterdam, The Netherlands 3-15
    • (2000) Lactoferrin: Structure, function and applications , pp. 3-15
    • Baker, E.N.1
  • 3
    • 43049178771 scopus 로고    scopus 로고
    • Beljaars, L., van der Strate, B. W. A., Floris, R., Smit, C., Wiegmans, F. C., Molema, G., et al. (2001). Antiviral activity and mechanism of charged modified proteins on cytomegalovirus replication in vitro. In: Anti-cytomegalovirus applications of the intrinsically active drug carrier lactoferrin (pp. 69-90) 〈www.dissertations.ub.rug.nl/FILES/faculties/science/2001/〉, Dissertations of the University of Groningen [Chapter 4].
    • Beljaars, L., van der Strate, B. W. A., Floris, R., Smit, C., Wiegmans, F. C., Molema, G., et al. (2001). Antiviral activity and mechanism of charged modified proteins on cytomegalovirus replication in vitro. In: Anti-cytomegalovirus applications of the intrinsically active drug carrier lactoferrin (pp. 69-90) 〈www.dissertations.ub.rug.nl/FILES/faculties/science/2001/〉, Dissertations of the University of Groningen [Chapter 4].
  • 5
    • 0001704077 scopus 로고
    • Esterification of food proteins: Characterization of the derivatives by a colorimetric method and by electrophoresis
    • Bertrand-Harb C., Chobert J.-M., Dufour E., and Haertlé T. Esterification of food proteins: Characterization of the derivatives by a colorimetric method and by electrophoresis. Sciences des Aliments 11 (1991) 641-652
    • (1991) Sciences des Aliments , vol.11 , pp. 641-652
    • Bertrand-Harb, C.1    Chobert, J.-M.2    Dufour, E.3    Haertlé, T.4
  • 6
    • 0029107952 scopus 로고
    • Modification of membrane permeability by animal viruses
    • Carrasco L. Modification of membrane permeability by animal viruses. Advances in Virus Research 45 (1995) 61-112
    • (1995) Advances in Virus Research , vol.45 , pp. 61-112
    • Carrasco, L.1
  • 7
    • 43049161507 scopus 로고    scopus 로고
    • Chobert, J.-M., & Haertlé, T. (2003). Composition pour l'inactivation de particules virales et applications d'une telle composition. French patent # FR-03/06786.
    • Chobert, J.-M., & Haertlé, T. (2003). Composition pour l'inactivation de particules virales et applications d'une telle composition. French patent # FR-03/06786.
  • 9
    • 0021256785 scopus 로고
    • Inhibition of herpes simplex virus-induced cytopathic effect by modified hen egg-white lysozymes
    • Cisani G., Varaldo P.E., Ingianni A., Pompei R., and Satta G. Inhibition of herpes simplex virus-induced cytopathic effect by modified hen egg-white lysozymes. Current Microbiology 10 (1984) 35-40
    • (1984) Current Microbiology , vol.10 , pp. 35-40
    • Cisani, G.1    Varaldo, P.E.2    Ingianni, A.3    Pompei, R.4    Satta, G.5
  • 10
    • 0024330848 scopus 로고
    • Cell fusion induced by herpes simplex is inhibited by hen egg-white lysozyme
    • Cisani G., Varaldo P.E., Pompei R., Valisena S., and Satta G. Cell fusion induced by herpes simplex is inhibited by hen egg-white lysozyme. Microbios 59 (1989) 73-83
    • (1989) Microbios , vol.59 , pp. 73-83
    • Cisani, G.1    Varaldo, P.E.2    Pompei, R.3    Valisena, S.4    Satta, G.5
  • 12
    • 0022292466 scopus 로고
    • Elected functionality changes of β-lactoglobulin upon esterification of side chain carboxyl groups
    • Halpin M.I., and Richardson T. Elected functionality changes of β-lactoglobulin upon esterification of side chain carboxyl groups. Journal of Dairy Science 68 (1985) 3189-3198
    • (1985) Journal of Dairy Science , vol.68 , pp. 3189-3198
    • Halpin, M.I.1    Richardson, T.2
  • 13
    • 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 Béthune M.P., Pauwels R., de Clercq E., The T.H., et al. Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro. Journal of Infectious Disease 172 (1995) 380-388
    • (1995) Journal of Infectious Disease , vol.172 , pp. 380-388
    • Harmsen, M.C.1    Swart, P.J.2    de Béthune, M.P.3    Pauwels, R.4    de Clercq, E.5    The, T.H.6
  • 15
    • 0030448689 scopus 로고    scopus 로고
    • Chemically modified bovine β-lactoglobulin blocks uptake of HIV-1 by colon- and cervix-derived epithelial cell lines
    • Jiang S., Lin K., Strick N., Li Y.-Y., and Neurath A.R. Chemically modified bovine β-lactoglobulin blocks uptake of HIV-1 by colon- and cervix-derived epithelial cell lines. Journal of Acquired Immune Deficiency Syndromes 13 (1996) 461-462
    • (1996) Journal of Acquired Immune Deficiency Syndromes , vol.13 , pp. 461-462
    • Jiang, S.1    Lin, K.2    Strick, N.3    Li, Y.-Y.4    Neurath, A.R.5
  • 16
    • 0023247109 scopus 로고
    • Protective influence of lactoferrin on mice infected with the polythemia-inducing strain of Friend virus complex
    • Lu L., Hangoc G., Oliff A., Chen L., Shen R.N., and Broxmeyer H.E. Protective influence of lactoferrin on mice infected with the polythemia-inducing strain of Friend virus complex. Cancer Research 47 (1987) 4184-4188
    • (1987) Cancer Research , vol.47 , pp. 4184-4188
    • Lu, L.1    Hangoc, G.2    Oliff, A.3    Chen, L.4    Shen, R.N.5    Broxmeyer, H.E.6
  • 17
    • 84987300635 scopus 로고
    • Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting out at low pH
    • Mailliart P., and Ribadeau Dumas B. Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting out at low pH. Journal of Food Science 53 (1988) 743-752
    • (1988) Journal of Food Science , vol.53 , pp. 743-752
    • Mailliart, P.1    Ribadeau Dumas, B.2
  • 18
    • 0031910817 scopus 로고    scopus 로고
    • Metal complexes of bovine lactoferrin inhibit in vitro replication of Herpes simplex virus type 1 and 2
    • Marchetti M., Pisani S., Antonini G., Valenti P., Seganti L., and Orsi N. Metal complexes of bovine lactoferrin inhibit in vitro replication of Herpes simplex virus type 1 and 2. BioMetals 11 (1998) 89-94
    • (1998) BioMetals , vol.11 , pp. 89-94
    • Marchetti, M.1    Pisani, S.2    Antonini, G.3    Valenti, P.4    Seganti, L.5    Orsi, N.6
  • 20
    • 0017040330 scopus 로고
    • Antiviral activity in milk and possible clinical importance
    • Matthews T.H.J., Nair C.D.G., Lawrence M.K., and Tyrrel D.A.J. Antiviral activity in milk and possible clinical importance. Lancet 308 (1976) 1387-1389
    • (1976) Lancet , vol.308 , pp. 1387-1389
    • Matthews, T.H.J.1    Nair, C.D.G.2    Lawrence, M.K.3    Tyrrel, D.A.J.4
  • 21
    • 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. Journal of Applied Microbiology 95 (2003) 1026-1033
    • (2003) Journal of Applied Microbiology , vol.95 , pp. 1026-1033
    • McCann, K.B.1    Lee, A.2    Wan, J.3    Roginski, H.4    Coventry, M.J.5
  • 24
    • 0002880420 scopus 로고
    • Epidemiology (of human enterovirus infections)
    • Rotbart H.A. (Ed), American Society for Microbiology, Washington, DC, USA
    • Morens D.M., and Pallansch M.A. Epidemiology (of human enterovirus infections). In: Rotbart H.A. (Ed). Human enterovirus infections (1995), American Society for Microbiology, Washington, DC, USA 3-23
    • (1995) Human enterovirus infections , pp. 3-23
    • Morens, D.M.1    Pallansch, M.A.2
  • 25
    • 0031052759 scopus 로고    scopus 로고
    • 3-Hydroxyphthaloyl-β-lactoglobulin. 1. Optimization of production and comparison with other compounds considered for chemoprophylaxis of mucosally transmitted human immunodeficiency virus type 1
    • Neurath A.R., Debnath A.K., Strick N., Li Y.-Y., and Lin K. 3-Hydroxyphthaloyl-β-lactoglobulin. 1. Optimization of production and comparison with other compounds considered for chemoprophylaxis of mucosally transmitted human immunodeficiency virus type 1. Antiviral Chemistry & Chemotherapy 8 (1997) 131-139
    • (1997) Antiviral Chemistry & Chemotherapy , vol.8 , pp. 131-139
    • Neurath, A.R.1    Debnath, A.K.2    Strick, N.3    Li, Y.-Y.4    Lin, K.5
  • 26
    • 19144370943 scopus 로고    scopus 로고
    • Bovine β-lactoglobulin modified by 3-hydroxyphthalic anhydride blocks the CD4 receptor for HIV
    • Neurath A.R., Jiang S., Strick N., Lin K., Li Y.-Y., and Debnath A.K. Bovine β-lactoglobulin modified by 3-hydroxyphthalic anhydride blocks the CD4 receptor for HIV. Nature Medicine 2 (1996) 230-234
    • (1996) Nature Medicine , vol.2 , pp. 230-234
    • Neurath, A.R.1    Jiang, S.2    Strick, N.3    Lin, K.4    Li, Y.-Y.5    Debnath, A.K.6
  • 27
    • 0031948483 scopus 로고    scopus 로고
    • 3-Hydroxyphthaloyl-β-lactoglobulin. III. Antiviral activity against herpes viruses
    • Neurath A.R., Strick N., and Li Y.-Y. 3-Hydroxyphthaloyl-β-lactoglobulin. III. Antiviral activity against herpes viruses. Antiviral Chemistry & Chemotherapy 9 (1998) 177-184
    • (1998) Antiviral Chemistry & Chemotherapy , vol.9 , pp. 177-184
    • Neurath, A.R.1    Strick, N.2    Li, Y.-Y.3
  • 28
    • 0002219457 scopus 로고
    • Development of antiviral agents for picornavirus infections
    • Rotbart H.A. (Ed), ASM Press, Washington, DC, USA
    • O'Connell J.F., Albin R., Blum D., Grint P., and Schwartz J. Development of antiviral agents for picornavirus infections. In: Rotbart H.A. (Ed). Human enterovirus infections (1995), ASM Press, Washington, DC, USA 419-434
    • (1995) Human enterovirus infections , pp. 419-434
    • O'Connell, J.F.1    Albin, R.2    Blum, D.3    Grint, P.4    Schwartz, J.5
  • 29
  • 31
    • 33847071664 scopus 로고    scopus 로고
    • Comparison of the effects of acylation and amidation on the antimicrobial and antiviral properties of lactoferrin
    • Pan Y., Wan J., Roginski H., Lee A., Shiell B., Michalski W.P., et al. Comparison of the effects of acylation and amidation on the antimicrobial and antiviral properties of lactoferrin. Letters in Applied Microbiology 44 (2007) 229-234
    • (2007) Letters in Applied Microbiology , vol.44 , pp. 229-234
    • Pan, Y.1    Wan, J.2    Roginski, H.3    Lee, A.4    Shiell, B.5    Michalski, W.P.6
  • 32
    • 0030925288 scopus 로고    scopus 로고
    • Poliovirus infection and expression of the poliovirus protein 2B provoke the disassembly of the Golgi complex, the organelle target for the anti poliovirus drug Ro-090179
    • Sandoval I.V., and Carrasco L. Poliovirus infection and expression of the poliovirus protein 2B provoke the disassembly of the Golgi complex, the organelle target for the anti poliovirus drug Ro-090179. Journal of Virology 71 (1997) 4679-4693
    • (1997) Journal of Virology , vol.71 , pp. 4679-4693
    • Sandoval, I.V.1    Carrasco, L.2
  • 35
    • 0035586024 scopus 로고    scopus 로고
    • Simplified short-time method for the esterification of milk proteins
    • Sitohy M., Chobert J.-M., and Haertlé T. Simplified short-time method for the esterification of milk proteins. Milchwissenschaft 56 (2001) 127-131
    • (2001) Milchwissenschaft , vol.56 , pp. 127-131
    • Sitohy, M.1    Chobert, J.-M.2    Haertlé, T.3
  • 36
    • 19944363530 scopus 로고    scopus 로고
    • Esterified whey proteins can protect Lactococcus lactis against bacteriophage infection. Comparison with the effect of native basic proteins and L-polylysines
    • Sitohy M., Chobert J.-M., and Haertlé T. Esterified whey proteins can protect Lactococcus lactis against bacteriophage infection. Comparison with the effect of native basic proteins and L-polylysines. Journal of Agricultural and Food Chemistry 53 (2005) 3727-3734
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 3727-3734
    • Sitohy, M.1    Chobert, J.-M.2    Haertlé, T.3
  • 38
    • 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. Medical Microbiology and Immunology 186 (1997) 83-91
    • (1997) Medical Microbiology and Immunology , vol.186 , pp. 83-91
    • Superti, F.1    Ammendolia, M.G.2    Valenti, P.3    Seganti, L.4
  • 40
    • 0031610282 scopus 로고    scopus 로고
    • Lactoferrin: Antiviral activity of lactoferrin
    • Spik G., Legrand D., Mazurier J., Pierce A., and Perraudin J.P. (Eds), Plenum Press, New York, USA
    • Swart P.J., Kuipers M.E., Smit C., Van der Strate B.W.A., Harmsen M.C., and Meijer D.K.F. Lactoferrin: Antiviral activity of lactoferrin. In: Spik G., Legrand D., Mazurier J., Pierce A., and Perraudin J.P. (Eds). Advances in lactoferrin research (1998), Plenum Press, New York, USA 205-213
    • (1998) Advances in lactoferrin research , pp. 205-213
    • Swart, P.J.1    Kuipers, M.E.2    Smit, C.3    Van der Strate, B.W.A.4    Harmsen, M.C.5    Meijer, D.K.F.6
  • 41
    • 0028236956 scopus 로고
    • Negatively charged albumins: A novel class of polyanionic proteins with a potent anti-HIV activity
    • Swart P.J., and Meijer D.K.F. Negatively charged albumins: A novel class of polyanionic proteins with a potent anti-HIV activity. Antiviral News 2 (1994) 69-71
    • (1994) Antiviral News , vol.2 , pp. 69-71
    • Swart, P.J.1    Meijer, D.K.F.2
  • 43
  • 44
    • 0032737846 scopus 로고    scopus 로고
    • Lactoferrin: A multifunctional glycoprotein
    • Vorland L.H. Lactoferrin: A multifunctional glycoprotein. Apmis 107 (1999) 971-981
    • (1999) Apmis , vol.107 , pp. 971-981
    • Vorland, L.H.1
  • 45
    • 13844250553 scopus 로고    scopus 로고
    • Antiviral activity of human lactoferrin: Inhibition of alphavirus interaction with heparin sulfate
    • Waarts B., Aneke O.J.C., Smit J.M., Kimata K., Bittman R., Meijer D.K.F., et al. Antiviral activity of human lactoferrin: Inhibition of alphavirus interaction with heparin sulfate. Virology 333 (2005) 284-292
    • (2005) Virology , vol.333 , pp. 284-292
    • Waarts, B.1    Aneke, O.J.C.2    Smit, J.M.3    Kimata, K.4    Bittman, R.5    Meijer, D.K.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.