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Volumn 60, Issue 3, 1997, Pages 267-271

Anti-invasive activity of bovine lactoferrin against Listeria monocytogenes

Author keywords

cell invasion; Lactoferrin; Listeria monocytogenes

Indexed keywords

BACTERIA (MICROORGANISMS); BOVINAE; EUKARYOTA; LISTERIA MONOCYTOGENES;

EID: 0030991699     PISSN: 0362028X     EISSN: None     Source Type: Journal    
DOI: 10.4315/0362-028X-60.3.267     Document Type: Article
Times cited : (14)

References (30)
  • 1
    • 0018868141 scopus 로고
    • Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms
    • Arnold, R. R., M. Brewer, and J. J. Gauthier. 1980. Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms. Infect. Immun. 28:893-898.
    • (1980) Infect. Immun. , vol.28 , pp. 893-898
    • Arnold, R.R.1    Brewer, M.2    Gauthier, J.J.3
  • 2
    • 0025329666 scopus 로고
    • Bacillus subtilis expressing a haemolysin gene from Listeria monocytogenes can grow in mammalian cells
    • Bielecki, J., P. Youngman, P. Connelly, and D. A. Portnoy. 1990. Bacillus subtilis expressing a haemolysin gene from Listeria monocytogenes can grow in mammalian cells. Nature 345:175-176.
    • (1990) Nature , vol.345 , pp. 175-176
    • Bielecki, J.1    Youngman, P.2    Connelly, P.3    Portnoy, D.A.4
  • 4
    • 0018899060 scopus 로고
    • Lactoferrin in human milk: Its role in iron absorption and protection against enteric infection in the newborn infant
    • Brock, J. H. 1980. Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Arch. Dis. Child. 55:417-421.
    • (1980) Arch. Dis. Child. , vol.55 , pp. 417-421
    • Brock, J.H.1
  • 5
    • 0001993592 scopus 로고
    • Transferrin and lactoferrin
    • Prem Ponka, H. M. Shulman, and R. C. Woodworth (ed.), CRC Press, Boston
    • Chasteen, N. D., and R. C. Woodworth. 1990. Transferrin and lactoferrin, p. 67-69. In Prem Ponka, H. M. Shulman, and R. C. Woodworth (ed.), Iron transport and storage. CRC Press, Boston.
    • (1990) Iron Transport and Storage , pp. 67-69
    • Chasteen, N.D.1    Woodworth, R.C.2
  • 6
    • 0028353585 scopus 로고
    • The effect of iron on the invasiveness of Escherichia coli carrying the inv gene of Yersinia pseudotuberculosis
    • Conte, M. P., C. Longhi, V. Buonfiglio, M. Polidoro, L. Seganti, and P. Valenti. 1994. The effect of iron on the invasiveness of Escherichia coli carrying the inv gene of Yersinia pseudotuberculosis. J. Med. Microbiol. 40:236-240.
    • (1994) J. Med. Microbiol. , vol.40 , pp. 236-240
    • Conte, M.P.1    Longhi, C.2    Buonfiglio, V.3    Polidoro, M.4    Seganti, L.5    Valenti, P.6
  • 7
    • 0024893361 scopus 로고
    • Listeria monocytogenes. A model system for the molecular study of intracellular parasitism
    • Cossart, P., and J. Mengaud. 1989. Listeria monocytogenes. A model system for the molecular study of intracellular parasitism. Mol. Biol. Med. 6:463-474.
    • (1989) Mol. Biol. Med. , vol.6 , pp. 463-474
    • Cossart, P.1    Mengaud, J.2
  • 9
    • 0025081821 scopus 로고
    • Listeria monocytogenes moves rapidly through the host cytoplasm by inducing directional actin assembly
    • Dabiri, G. A., J. M. Sanger, D. A. Portnoy, and F. S. Southwick. 1990. Listeria monocytogenes moves rapidly through the host cytoplasm by inducing directional actin assembly. Proc. Natl. Acad. Sci. USA 87:6068-6072.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6068-6072
    • Dabiri, G.A.1    Sanger, J.M.2    Portnoy, D.A.3    Southwick, F.S.4
  • 10
    • 0023905150 scopus 로고
    • Specific binding of lactoferrin to brush-border membrane: Ontogeny and effect of glycan chain
    • Davidson, L. A., and B. Lonnerdal. 1988. Specific binding of lactoferrin to brush-border membrane: ontogeny and effect of glycan chain. Am. J. Physiol. 254:580-585.
    • (1988) Am. J. Physiol. , vol.254 , pp. 580-585
    • Davidson, L.A.1    Lonnerdal, B.2
  • 11
    • 0023815539 scopus 로고
    • Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin
    • Ellison, R. T., T. J. Giehl, and F. M. La Force. 1988. Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect. Immun. 56:2774-2781.
    • (1988) Infect. Immun. , vol.56 , pp. 2774-2781
    • Ellison, R.T.1    Giehl, T.J.2    La Force, F.M.3
  • 12
    • 0025951915 scopus 로고
    • Listeria monocytogenes, a food-borne pathogen
    • Farber, J. M., and P. I. Peterkin. 1991 Listeria monocytogenes, a food-borne pathogen. Microbiol. Rev. 55:476-511.
    • (1991) Microbiol. Rev. , vol.55 , pp. 476-511
    • Farber, J.M.1    Peterkin, P.I.2
  • 13
    • 0023617861 scopus 로고
    • In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte like cell line Caco-2
    • Gaillard, J. I., P. Berche, J. Mounier, S. Richard, and P. Sansonetti. 1987. In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte like cell line Caco-2. Infect. Immun. 55:2822-2829.
    • (1987) Infect. Immun. , vol.55 , pp. 2822-2829
    • Gaillard, J.I.1    Berche, P.2    Mounier, J.3    Richard, S.4    Sansonetti, P.5
  • 14
    • 0024539434 scopus 로고
    • Listeriosis
    • Gellin, B. G., and C. V. Broome. 1989. Listeriosis. JAMA 261:1313-1320.
    • (1989) JAMA , vol.261 , pp. 1313-1320
    • Gellin, B.G.1    Broome, A.C.V.2
  • 15
    • 0001395327 scopus 로고
    • The isolation of a red protein from milk
    • Groves, M. L. 1960. The isolation of a red protein from milk. J. Am. Chem. Soc. 82:3345-3350.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 3345-3350
    • Groves, M.L.1
  • 16
    • 0024234719 scopus 로고
    • Minimum growth temperature of Listeria monocytogenes and non-haemolytic Listeria
    • Junttila, J. R., S. I. Niemala, and J. Hirn. 1988. Minimum growth temperature of Listeria monocytogenes and non-haemolytic Listeria. J. Appl. Bacteriol. 65:321-327.
    • (1988) J. Appl. Bacteriol. , vol.65 , pp. 321-327
    • Junttila, J.R.1    Niemala, S.I.2    Hirn, J.3
  • 17
    • 0025267011 scopus 로고
    • Properties of the iron binding site of the N-terminal lobe of human and bovine lactoferrins
    • Legrand, D., J. Mazurier, D. Colavizza, J. Montreuil, and G. Spik. 1990. Properties of the iron binding site of the N-terminal lobe of human and bovine lactoferrins. Biochem. J. 266:575-581.
    • (1990) Biochem. J. , vol.266 , pp. 575-581
    • Legrand, D.1    Mazurier, J.2    Colavizza, D.3    Montreuil, J.4    Spik, G.5
  • 18
    • 0029126185 scopus 로고
    • Lactoferrin: A general review
    • Levay, P. F., and M. Viljoen. 1995. Lactoferrin: a general review. Haematologica 80:252-267.
    • (1995) Haematologica , vol.80 , pp. 252-267
    • Levay, P.F.1    Viljoen, M.2
  • 19
    • 0028247383 scopus 로고
    • Effect of lactoferricin B, a pepsin-generated peptide of bovine lactoferrin on Escherichia coli HB101 (pRI203) entry into HeLa cells
    • Longhi, C., M. P. Conte, W. Bellamy, L. Seganti, and P. Valenti. 1994. Effect of lactoferricin B, a pepsin-generated peptide of bovine lactoferrin on Escherichia coli HB101 (pRI203) entry into HeLa cells. Med. Microbiol. Immunol. 182:77-85.
    • (1994) Med. Microbiol. Immunol. , vol.182 , pp. 77-85
    • Longhi, C.1    Conte, M.P.2    Bellamy, W.3    Seganti, L.4    Valenti, P.5
  • 21
    • 0015225776 scopus 로고
    • Lactoferrin in milk from different species
    • Masson, T. L., 61nd J. F. Heremans. 1971. Lactoferrin in milk from different species. Comp. Biochem. Physiol. 39B:119-129.
    • (1971) Comp. Biochem. Physiol. , vol.39 B , pp. 119-129
    • Masson, T.L.1    Heremans, N.J.F.2
  • 22
    • 0025239739 scopus 로고
    • Intracellular and cell-to-cell spread of Listeria monocytogenes involves interactions with F-actin in the enterocyte like cell line Caco-2
    • Mounier, J., A. Ryter, M. Coquis-Rondon, and P. J. Sansonetti. 1990. Intracellular and cell-to-cell spread of Listeria monocytogenes involves interactions with F-actin in the enterocyte like cell line Caco-2. Infect. Immun. 58:1048-1058.
    • (1990) Infect. Immun. , vol.58 , pp. 1048-1058
    • Mounier, J.1    Ryter, A.2    Coquis-Rondon, M.3    Sansonetti, P.J.4
  • 23
    • 0023793037 scopus 로고
    • Particle agglutination assays for rapid detection of fibronectin, fibrinogen and collagen receptors on Staphylococcus aureus
    • Naidu, A. S., M. Paulsson, and T. Wadstrom. 1988. Particle agglutination assays for rapid detection of fibronectin, fibrinogen and collagen receptors on Staphylococcus aureus. J. Clin. Microbiol. 26:1549-1554.
    • (1988) J. Clin. Microbiol. , vol.26 , pp. 1549-1554
    • Naidu, A.S.1    Paulsson, M.2    Wadstrom, T.3
  • 25
    • 0023898917 scopus 로고
    • Role of hemolysin for the intracellular growth of Listeria monocytogenes
    • Portnoy, D. A., P. S. Jacks, and D. J. Hinrichs. 1988. Role of hemolysin for the intracellular growth of Listeria monocytogenes. J. Exp. Med. 167:1459-1471.
    • (1988) J. Exp. Med. , vol.167 , pp. 1459-1471
    • Portnoy, D.A.1    Jacks, P.S.2    Hinrichs, D.J.3
  • 26
    • 0022509516 scopus 로고
    • The human colon carcinoma cell lines HT-29 and Caco-2, two in vitro models for the study of intestinal differentiation
    • Rousset, M. 1986. The human colon carcinoma cell lines HT-29 and Caco-2, two in vitro models for the study of intestinal differentiation. Biochimie 68:1035-1040.
    • (1986) Biochimie , vol.68 , pp. 1035-1040
    • Rousset, M.1
  • 29
    • 0000912441 scopus 로고
    • Growth of Listeria monocytogenes and Aeromonas hydrophila at chill temperatures
    • Walker, S. J., and M. F. Stringer. 1987. Growth of Listeria monocytogenes and Aeromonas hydrophila at chill temperatures. J. Appl. Bacteriol. 63:R20.
    • (1987) J. Appl. Bacteriol. , vol.63
    • Walker, S.J.1    Stringer, M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.