메뉴 건너뛰기




Volumn 14, Issue 4, 2011, Pages 476-482

Transferrin receptor 1 in the zoonosis and pathogenesis of New World hemorrhagic fever arenaviruses

Author keywords

[No Author keywords available]

Indexed keywords

CD71 ANTIGEN; GLYCOPROTEIN; IRON;

EID: 80051800509     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2011.07.014     Document Type: Review
Times cited : (46)

References (47)
  • 2
    • 0036186280 scopus 로고    scopus 로고
    • Molecular phylogeny of the arenaviruses
    • Clegg J.C. Molecular phylogeny of the arenaviruses. Curr Top Microbiol Immunol 2002, 262:1-24.
    • (2002) Curr Top Microbiol Immunol , vol.262 , pp. 1-24
    • Clegg, J.C.1
  • 3
    • 0029975554 scopus 로고    scopus 로고
    • The phylogeny of New World (Tacaribe complex) arenaviruses
    • Bowen M.D., Peters C.J., Nichol S.T. The phylogeny of New World (Tacaribe complex) arenaviruses. Virology 1996, 219:285-290.
    • (1996) Virology , vol.219 , pp. 285-290
    • Bowen, M.D.1    Peters, C.J.2    Nichol, S.T.3
  • 4
    • 0014750032 scopus 로고
    • Serological relationship of the Tacaribe complex of viruses to lymphocytic choriomeningitis virus
    • Rowe W.P., Pugh W.E., Webb P.A., Peters C.J. Serological relationship of the Tacaribe complex of viruses to lymphocytic choriomeningitis virus. J Virol 1970, 5:289-292.
    • (1970) J Virol , vol.5 , pp. 289-292
    • Rowe, W.P.1    Pugh, W.E.2    Webb, P.A.3    Peters, C.J.4
  • 5
    • 1842840105 scopus 로고    scopus 로고
    • Phylogeny of the Venezuelan arenaviruses
    • Cajimat M.N., Fulhorst C.F. Phylogeny of the Venezuelan arenaviruses. Virus Res 2004, 102:199-206.
    • (2004) Virus Res , vol.102 , pp. 199-206
    • Cajimat, M.N.1    Fulhorst, C.F.2
  • 6
    • 73949117750 scopus 로고    scopus 로고
    • Zoonotic aspects of arenavirus infections
    • Charrel R.N., de Lamballerie X. Zoonotic aspects of arenavirus infections. Vet Microbiol 2010, 140:213-220.
    • (2010) Vet Microbiol , vol.140 , pp. 213-220
    • Charrel, R.N.1    de Lamballerie, X.2
  • 7
    • 50849117037 scopus 로고    scopus 로고
    • Diversity among tacaribe serocomplex viruses (family Arenaviridae) naturally associated with the white-throated woodrat (Neotoma albigula) in the southwestern United States
    • Milazzo M.L., Cajimat M.N., Haynie M.L., Abbott K.D., Bradley R.D., Fulhorst C.F. Diversity among tacaribe serocomplex viruses (family Arenaviridae) naturally associated with the white-throated woodrat (Neotoma albigula) in the southwestern United States. Vector Borne Zoonotic Dis 2008, 8:523-540.
    • (2008) Vector Borne Zoonotic Dis , vol.8 , pp. 523-540
    • Milazzo, M.L.1    Cajimat, M.N.2    Haynie, M.L.3    Abbott, K.D.4    Bradley, R.D.5    Fulhorst, C.F.6
  • 10
    • 0036389713 scopus 로고    scopus 로고
    • Phylogeny of New World arenaviruses based on the complete coding sequences of the small genomic segment identified an evolutionary lineage produced by intrasegmental recombination
    • Charrel R.N., Feldmann H., Fulhorst C.F., Khelifa R., de Chesse R., de Lamballerie X. Phylogeny of New World arenaviruses based on the complete coding sequences of the small genomic segment identified an evolutionary lineage produced by intrasegmental recombination. Biochem Biophys Res Commun 2002, 296:1118-1124.
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 1118-1124
    • Charrel, R.N.1    Feldmann, H.2    Fulhorst, C.F.3    Khelifa, R.4    de Chesse, R.5    de Lamballerie, X.6
  • 14
    • 33646192966 scopus 로고    scopus 로고
    • Animal origins of the severe acute respiratory syndrome coronavirus: insight from ACE2-S-protein interactions
    • Li W., Wong S.K., Li F., Kuhn J.H., Huang I.C., Choe H., Farzan M. Animal origins of the severe acute respiratory syndrome coronavirus: insight from ACE2-S-protein interactions. J Virol 2006, 80:4211-4219.
    • (2006) J Virol , vol.80 , pp. 4211-4219
    • Li, W.1    Wong, S.K.2    Li, F.3    Kuhn, J.H.4    Huang, I.C.5    Choe, H.6    Farzan, M.7
  • 15
    • 0942298133 scopus 로고    scopus 로고
    • A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2
    • Wong S.K., Li W., Moore M.J., Choe H., Farzan M. A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2. J Biol Chem 2004, 279:3197-3201.
    • (2004) J Biol Chem , vol.279 , pp. 3197-3201
    • Wong, S.K.1    Li, W.2    Moore, M.J.3    Choe, H.4    Farzan, M.5
  • 16
    • 77950517857 scopus 로고    scopus 로고
    • Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses
    • Abraham J., Corbett K.D., Farzan M., Choe H., Harrison S.C. Structural basis for receptor recognition by New World hemorrhagic fever arenaviruses. Nat Struct Mol Biol 2010, 17:438-444.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 438-444
    • Abraham, J.1    Corbett, K.D.2    Farzan, M.3    Choe, H.4    Harrison, S.C.5
  • 19
    • 0032775091 scopus 로고    scopus 로고
    • Molecular insights into mechanisms of iron transport
    • Andrews N.C., Fleming M.D., Levy J.E. Molecular insights into mechanisms of iron transport. Curr Opin Hematol 1999, 6:61-64.
    • (1999) Curr Opin Hematol , vol.6 , pp. 61-64
    • Andrews, N.C.1    Fleming, M.D.2    Levy, J.E.3
  • 20
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: molecular control of mammalian iron metabolism
    • Hentze M.W., Muckenthaler M.U., Andrews N.C. Balancing acts: molecular control of mammalian iron metabolism. Cell 2004, 117:285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 21
    • 1342264310 scopus 로고    scopus 로고
    • Structure of the human transferrin receptor-transferrin complex
    • Cheng Y., Zak O., Aisen P., Harrison S.C., Walz T. Structure of the human transferrin receptor-transferrin complex. Cell 2004, 116:565-576.
    • (2004) Cell , vol.116 , pp. 565-576
    • Cheng, Y.1    Zak, O.2    Aisen, P.3    Harrison, S.C.4    Walz, T.5
  • 23
    • 33750019824 scopus 로고    scopus 로고
    • The transferrin receptor part I: biology and targeting with cytotoxic antibodies for the treatment of cancer
    • Daniels T.R., Delgado T., Rodriguez J.A., Helguera G., Penichet M.L. The transferrin receptor part I: biology and targeting with cytotoxic antibodies for the treatment of cancer. Clin Immunol 2006, 121:159-176.
    • (2006) Clin Immunol , vol.121 , pp. 159-176
    • Daniels, T.R.1    Delgado, T.2    Rodriguez, J.A.3    Helguera, G.4    Penichet, M.L.5
  • 24
    • 37849036757 scopus 로고    scopus 로고
    • New world clade B arenaviruses can use transferrin receptor 1 (TfR1)-dependent and -independent entry pathways, and glycoproteins from human pathogenic strains are associated with the use of TfR1
    • Flanagan M.L., Oldenburg J., Reignier T., Holt N., Hamilton G.A., Martin V.K., Cannon P.M. New world clade B arenaviruses can use transferrin receptor 1 (TfR1)-dependent and -independent entry pathways, and glycoproteins from human pathogenic strains are associated with the use of TfR1. J Virol 2008, 82:938-948.
    • (2008) J Virol , vol.82 , pp. 938-948
    • Flanagan, M.L.1    Oldenburg, J.2    Reignier, T.3    Holt, N.4    Hamilton, G.A.5    Martin, V.K.6    Cannon, P.M.7
  • 25
    • 64049100955 scopus 로고    scopus 로고
    • Iron in innate immunity: starve the invaders
    • Ganz T. Iron in innate immunity: starve the invaders. Curr Opin Immunol 2009, 21:63-67.
    • (2009) Curr Opin Immunol , vol.21 , pp. 63-67
    • Ganz, T.1
  • 26
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • Nemeth E., Rivera S., Gabayan V., Keller C., Taudorf S., Pedersen B.K., Ganz T. IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. J Clin Invest 2004, 113:1271-1276.
    • (2004) J Clin Invest , vol.113 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7
  • 28
    • 72949102435 scopus 로고    scopus 로고
    • The role of the vascular endothelium in arenavirus haemorrhagic fevers
    • Kunz S. The role of the vascular endothelium in arenavirus haemorrhagic fevers. Thromb Haemost 2009, 102:1024-1029.
    • (2009) Thromb Haemost , vol.102 , pp. 1024-1029
    • Kunz, S.1
  • 29
    • 33748102856 scopus 로고    scopus 로고
    • Hepcidin-a peptide hormone at the interface of innate immunity and iron metabolism
    • Ganz T. Hepcidin-a peptide hormone at the interface of innate immunity and iron metabolism. Curr Top Microbiol Immunol 2006, 306:183-198.
    • (2006) Curr Top Microbiol Immunol , vol.306 , pp. 183-198
    • Ganz, T.1
  • 30
    • 0038662619 scopus 로고    scopus 로고
    • Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
    • Nemeth E., Valore E.V., Territo M., Schiller G., Lichtenstein A., Ganz T. Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. Blood 2003, 101:2461-2463.
    • (2003) Blood , vol.101 , pp. 2461-2463
    • Nemeth, E.1    Valore, E.V.2    Territo, M.3    Schiller, G.4    Lichtenstein, A.5    Ganz, T.6
  • 32
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: an update
    • Pantopoulos K. Iron metabolism and the IRE/IRP regulatory system: an update. Ann N Y Acad Sci 2004, 1012:1-13.
    • (2004) Ann N Y Acad Sci , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 33
    • 34547636893 scopus 로고    scopus 로고
    • Capturing the onset of the common cold and its effects on iron absorption
    • Hoppe M., Hulthen L. Capturing the onset of the common cold and its effects on iron absorption. Eur J Clin Nutr 2007, 61:1032-1034.
    • (2007) Eur J Clin Nutr , vol.61 , pp. 1032-1034
    • Hoppe, M.1    Hulthen, L.2
  • 34
    • 34250363169 scopus 로고    scopus 로고
    • Changes of gene expression of iron regulatory proteins during turpentine oil-induced acute-phase response in the rat
    • Sheikh N., Dudas J., Ramadori G. Changes of gene expression of iron regulatory proteins during turpentine oil-induced acute-phase response in the rat. Lab Invest 2007, 87:713-725.
    • (2007) Lab Invest , vol.87 , pp. 713-725
    • Sheikh, N.1    Dudas, J.2    Ramadori, G.3
  • 37
    • 77449086323 scopus 로고    scopus 로고
    • Plasma prohepcidin as a negative acute phase reactant after large cardiac surgery with a deep hypothermic circulatory arrest
    • Maruna P., Lindner J., Kunstyr J., Plocova K., Hubacek J. Plasma prohepcidin as a negative acute phase reactant after large cardiac surgery with a deep hypothermic circulatory arrest. Physiol Res 2009, 58:827-833.
    • (2009) Physiol Res , vol.58 , pp. 827-833
    • Maruna, P.1    Lindner, J.2    Kunstyr, J.3    Plocova, K.4    Hubacek, J.5
  • 38
    • 23944502314 scopus 로고    scopus 로고
    • Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS
    • Kemna E., Pickkers P., Nemeth E., van der Hoeven H., Swinkels D. Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS. Blood 2005, 106:1864-1866.
    • (2005) Blood , vol.106 , pp. 1864-1866
    • Kemna, E.1    Pickkers, P.2    Nemeth, E.3    van der Hoeven, H.4    Swinkels, D.5
  • 40
    • 70349582011 scopus 로고    scopus 로고
    • The expression of TfR1 mRNA and IRP1 mRNA in the placenta from different maternal iron status
    • Liu C.Y., Liu Y.F., Zeng L., Zhang S.G., Xu H. The expression of TfR1 mRNA and IRP1 mRNA in the placenta from different maternal iron status. Zhonghua Xue Ye Xue Za Zhi 2007, 28:255-258.
    • (2007) Zhonghua Xue Ye Xue Za Zhi , vol.28 , pp. 255-258
    • Liu, C.Y.1    Liu, Y.F.2    Zeng, L.3    Zhang, S.G.4    Xu, H.5
  • 41
    • 0029286136 scopus 로고
    • Transferrin receptor and iron deposition pattern in the hepatic lobules of the iron-deficient and iron-overloaded rats
    • Lu J., Hayashi K., Hu X. Transferrin receptor and iron deposition pattern in the hepatic lobules of the iron-deficient and iron-overloaded rats. Zhonghua Bing Li Xue Za Zhi 1995, 24:75-77.
    • (1995) Zhonghua Bing Li Xue Za Zhi , vol.24 , pp. 75-77
    • Lu, J.1    Hayashi, K.2    Hu, X.3
  • 43
    • 0037405911 scopus 로고    scopus 로고
    • Iron deficiency alters iron regulatory protein and iron transport protein expression in the perinatal rat brain
    • Siddappa A.J., Rao R.B., Wobken J.D., Casperson K., Leibold E.A., Connor J.R., Georgieff M.K. Iron deficiency alters iron regulatory protein and iron transport protein expression in the perinatal rat brain. Pediatr Res 2003, 53:800-807.
    • (2003) Pediatr Res , vol.53 , pp. 800-807
    • Siddappa, A.J.1    Rao, R.B.2    Wobken, J.D.3    Casperson, K.4    Leibold, E.A.5    Connor, J.R.6    Georgieff, M.K.7
  • 47
    • 0036232837 scopus 로고    scopus 로고
    • New World arenavirus clade C, but not clade A and B viruses, utilizes alpha-dystroglycan as its major receptor
    • Spiropoulou C.F., Kunz S., Rollin P.E., Campbell K.P., Oldstone M.B. New World arenavirus clade C, but not clade A and B viruses, utilizes alpha-dystroglycan as its major receptor. J Virol 2002, 76:5140-5146.
    • (2002) J Virol , vol.76 , pp. 5140-5146
    • Spiropoulou, C.F.1    Kunz, S.2    Rollin, P.E.3    Campbell, K.P.4    Oldstone, M.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.