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Volumn 1, Issue 1, 2011, Pages 13-18

Receptors and tropisms of envelope viruses

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; VIRUS PROTEIN; VIRUS RECEPTOR; VIRUS VECTOR;

EID: 79960466427     PISSN: 18796257     EISSN: 18796265     Source Type: Journal    
DOI: 10.1016/j.coviro.2011.05.001     Document Type: Article
Times cited : (26)

References (48)
  • 2
    • 0004250845 scopus 로고    scopus 로고
    • edn 5. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins
    • Fields BN, Knipe DM, Howley PM: Fields' Virology. edn 5. Philadelphia: Wolters Kluwer Health/Lippincott Williams & Wilkins; 2007.
    • (2007) Fields' Virology
    • Fields, B.N.1    Knipe, D.M.2    Howley, P.M.3
  • 3
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • DOI 10.1080/10409230802058320, PII 794225034
    • White JM, Delos SE, Brecher M, Schornberg K: Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit Rev Biochem Mol Biol 2008, 43:189-219. (Pubitemid 351883153)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 4
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes W, Boerger AL, Narayan S, Cunningham JM, Young JA: Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 2000, 103:679-689.
    • (2000) Cell , vol.103 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.5
  • 5
    • 0037404499 scopus 로고    scopus 로고
    • Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells
    • DOI 10.1128/JVI.77.9.5324-5332.2003
    • Nicola AV, McEvoy AM, Straus SE: Roles for endocytosis and low pH in herpes simplex virus entry into HeLa and Chinese hamster ovary cells. J Virol 2003, 77:5324-5332. (Pubitemid 36460946)
    • (2003) Journal of Virology , vol.77 , Issue.9 , pp. 5324-5332
    • Nicola, A.V.1    McEvoy, A.M.2    Straus, S.E.3
  • 6
    • 79954692758 scopus 로고    scopus 로고
    • Ex vivo gene transfer and correction for cell-based therapies
    • Naldini L: Ex vivo gene transfer and correction for cell-based therapies. Nat Rev Genet 2011, 12:301-315.
    • (2011) Nat Rev Genet , vol.12 , pp. 301-315
    • Naldini, L.1
  • 7
    • 44049094771 scopus 로고    scopus 로고
    • Clinical gene therapy using recombinant adeno-associated virus vectors
    • DOI 10.1038/gt.2008.68, PII GT200868, Special Issue: AAV Vectors for Clinical GeneTherapy
    • Mueller C, Flotte TR: Clinical gene therapy using recombinant adeno-associated virus vectors. Gene Ther 2008, 15:858-863. (Pubitemid 351712619)
    • (2008) Gene Therapy , vol.15 , Issue.11 , pp. 858-863
    • Mueller, C.1    Flotte, T.R.2
  • 8
    • 44849135037 scopus 로고    scopus 로고
    • Gene therapy progress and prospects cancer: Oncolytic viruses
    • DOI 10.1038/gt.2008.72, PII GT200872
    • Liu TC, Kirn D: Gene therapy progress and prospects cancer: oncolytic viruses. Gene Ther 2008, 15:877-884. (Pubitemid 351791475)
    • (2008) Gene Therapy , vol.15 , Issue.12 , pp. 877-884
    • Liu, T.-C.1    Kirn, D.2
  • 9
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley DC, Skehel JJ: The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu Rev Biochem 1987, 56:365-394.
    • (1987) Annu Rev Biochem , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 10
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson IA, Skehel JJ, Wiley DC: Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 1981, 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 11
    • 79955373167 scopus 로고    scopus 로고
    • Structural characterization of an early fusion intermediate of influenza virus hemagglutinin
    • Xu R, Wilson IA: Structural characterization of an early fusion intermediate of influenza virus hemagglutinin. J Virol 2011, 85:5172-5182.
    • (2011) J Virol , vol.85 , pp. 5172-5182
    • Xu, R.1    Wilson, I.A.2
  • 14
    • 0030835821 scopus 로고    scopus 로고
    • Cell-specific targeting of sindbis virus vectors displaying IgG-binding domains of protein A
    • Ohno K, Sawai K, Iijima Y, Levin B, Meruelo D: Cell-specific targeting of Sindbis virus vectors displaying IgG-binding domains of protein A. Nat Biotechnol 1997, 15:763-767. (Pubitemid 27329479)
    • (1997) Nature Biotechnology , vol.15 , Issue.8 , pp. 763-767
    • Ohno, K.1    Sawai, K.2    Lijima, Y.3    Levin, B.4    Meruelo, D.5
  • 17
    • 70350340830 scopus 로고    scopus 로고
    • Dealing with low pH: Entry and exit of alphaviruses and flaviviruses
    • Sanchez-San Martin C, Liu CY, Kielian M: Dealing with low pH: entry and exit of alphaviruses and flaviviruses. Trends Microbiol 2009, 17:514-521.
    • (2009) Trends Microbiol , vol.17 , pp. 514-521
    • Sanchez-San Martin, C.1    Liu, C.Y.2    Kielian, M.3
  • 18
    • 7444242684 scopus 로고    scopus 로고
    • Preferential targeting of vesicular stomatitis virus to breast cancer cells
    • DOI 10.1016/j.virol.2004.06.048, PII S0042682204004568
    • Bergman I, Whitaker-Dowling P, Gao Y, Griffin JA: Preferential targeting of vesicular stomatitis virus to breast cancer cells. Virology 2004, 330:24-33. (Pubitemid 39446564)
    • (2004) Virology , vol.330 , Issue.1 , pp. 24-33
    • Bergman, I.1    Whitaker-Dowling, P.2    Gao, Y.3    Griffin, J.A.4
  • 19
    • 0034872863 scopus 로고    scopus 로고
    • Antibody-directed targeting of retroviral vectors via cell surface antigens
    • DOI 10.1128/JVI.75.17.8016-8020.2001
    • Morizono K, Bristol G, Xie YM, Kung SK, Chen IS: Antibodydirected targeting of retroviral vectors via cell surface antigens. J Virol 2001, 75:8016-8020. (Pubitemid 32743673)
    • (2001) Journal of Virology , vol.75 , Issue.17 , pp. 8016-8020
    • Morizono, M.1    Bristol, G.2    Xie, Y.-M.3    Kung, S.K.-P.4    Chen, I.S.Y.5
  • 20
    • 16244394824 scopus 로고    scopus 로고
    • Lentiviral vector retargeting to P-glycoprotein on metastatic melanoma through intravenous injection
    • DOI 10.1038/nm1192
    • Morizono K, Xie Y, Ringpis GE, Johnson M, Nassanian H, Lee B, Wu L, Chen IS: Lentiviral vector retargeting to P-glycoprotein on metastatic melanoma through intravenous injection. Nat Med 2005, 11:346-352. (Pubitemid 40460565)
    • (2005) Nature Medicine , vol.11 , Issue.3 , pp. 346-352
    • Morizono, K.1    Xie, Y.2    Ringpis, G.-E.3    Johnson, M.4    Nassanian, H.5    Lee, B.6    Wu, L.7    Chen, I.S.Y.8
  • 21
    • 68949220821 scopus 로고    scopus 로고
    • Redirecting lentiviral vectors by insertion of integrin-tageting peptides into envelope proteins
    • Morizono K, Pariente N, Xie Y, Chen IS: Redirecting lentiviral vectors by insertion of integrin-tageting peptides into envelope proteins. J Gene Med 2009, 11:549-558.
    • (2009) J Gene Med , vol.11 , pp. 549-558
    • Morizono, K.1    Pariente, N.2    Xie, Y.3    Chen, I.S.4
  • 22
    • 77953781716 scopus 로고    scopus 로고
    • Redirecting lentiviral vectors pseudotyped with Sindbis virus-derived envelope proteins to DC-SIGN by modification of N-linked glycans of envelope proteins
    • Morizono K, Ku A, Xie Y, Harui A, Kung SK, Roth MD, Lee B, Chen IS: Redirecting lentiviral vectors pseudotyped with Sindbis virus-derived envelope proteins to DC-SIGN by modification of N-linked glycans of envelope proteins. J Virol 2010, 84:6923-6934.
    • (2010) J Virol , vol.84 , pp. 6923-6934
    • Morizono, K.1    Ku, A.2    Xie, Y.3    Harui, A.4    Kung, S.K.5    Roth, M.D.6    Lee, B.7    Chen, I.S.8
  • 25
    • 0023878973 scopus 로고
    • The envelope glycoprotein of the human immunodeficiency virus binds to the immunoglobulin-like domain of CD4
    • Landau NR, Warton M, Littman DR: The envelope glycoprotein of the human immunodeficiency virus binds to the immunoglobulin-like domain of CD4. Nature 1988, 334:159-162.
    • (1988) Nature , vol.334 , pp. 159-162
    • Landau, N.R.1    Warton, M.2    Littman, D.R.3
  • 26
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y, Broder CC, Kennedy PE, Berger EA: HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 1996, 272:872-877. (Pubitemid 26154590)
    • (1996) Science , vol.272 , Issue.5263 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 30
    • 0028567517 scopus 로고
    • Tissue-specific targeting of retroviral vectors through ligand-receptor interactions
    • Kasahara N, Dozy AM, Kan YW: Tissue-specific targeting of retroviral vectors through ligand-receptor interactions. Science 1994, 266:1373-1376.
    • (1994) Science , vol.266 , pp. 1373-1376
    • Kasahara, N.1    Dozy, A.M.2    Kan, Y.W.3
  • 32
    • 0027426010 scopus 로고
    • The human CD46 molecule is a receptor for measles virus (Edmonston strain)
    • DOI 10.1016/0092-8674(93)80071-L
    • Dorig RE, Marcil A, Chopra A, Richardson CD: The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 1993, 75:295-305. (Pubitemid 23320293)
    • (1993) Cell , vol.75 , Issue.2 , pp. 295-305
    • Dorig, R.E.1    Marcil, A.2    Chopra, A.3    Richardson, C.D.4
  • 33
    • 0034710650 scopus 로고    scopus 로고
    • Slam (CDw150) is a cellular receptor for measles virus
    • DOI 10.1038/35022579
    • Tatsuo H, Ono N, Tanaka K, Yanagi Y: SLAM (CDw150) is a cellular receptor for measles virus. Nature 2000, 406:893-897. (Pubitemid 30664265)
    • (2000) Nature , vol.406 , Issue.6798 , pp. 893-897
    • Tatsuo, H.1    Ono, N.2    Tanaka, K.3    Yanagi, Y.4
  • 34
    • 79551638780 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM
    • This study presented the crystal structure of the measles virus H protein bound to CD150, which could represent the initial structural change of the H protein to elicit signals that trigger the conformational change of F
    • Hashiguchi T, Ose T, Kubota M, Maita N, Kamishikiryo J, •• Maenaka K, Yanagi Y: Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM. Nat Struct Mol Biol 2011, 18:135-141. This study presented the crystal structure of the measles virus H protein bound to CD150, which could represent the initial structural change of the H protein to elicit signals that trigger the conformational change of F.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 135-141
    • Hashiguchi, T.1    Ose, T.2    Kubota, M.3    Maita, N.4    Kamishikiryo, J.5    Maenaka, K.6    Yanagi, Y.7
  • 35
    • 79551621397 scopus 로고    scopus 로고
    • The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
    • This study attempted to elucidate how the measles virus H protein conformational change occurs after binding to CD150 by introducing mutations into H proteins. This study also identified the regions of the H protein that can elicit signals to trigger fusion activity of the F protein after binding to target antigens
    • Navaratnarajah CK, Oezguen N, Rupp L, Kay L, Leonard VH, •• Braun W, Cattaneo R: The heads of the measles virus attachment protein move to transmit the fusion-triggering signal. Nat Struct Mol Biol 2011, 18:128-134. This study attempted to elucidate how the measles virus H protein conformational change occurs after binding to CD150 by introducing mutations into H proteins. This study also identified the regions of the H protein that can elicit signals to trigger fusion activity of the F protein after binding to target antigens.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 128-134
    • Navaratnarajah, C.K.1    Oezguen, N.2    Rupp, L.3    Kay, L.4    Leonard, V.H.5    Braun, W.6    Cattaneo, R.7
  • 39
    • 79955051520 scopus 로고    scopus 로고
    • •• The soluble serum protein Gas6 bridges virion envelope phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate viral entry
    • This study demonstrated that pseudotyped lentiviral vectors and replication-competent vaccinia virus utilize a cellular mechanism for their entry that is typically used to remove dead cells
    • Morizono K, Xie Y, Olafsen T, Lee B, Dasgupta A, Wu AM, Chen IS: •• The soluble serum protein Gas6 bridges virion envelope phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate viral entry. Cell Host Microbe 2011, 9:286-298. This study demonstrated that pseudotyped lentiviral vectors and replication-competent vaccinia virus utilize a cellular mechanism for their entry that is typically used to remove dead cells.
    • (2011) Cell Host Microbe , vol.9 , pp. 286-298
    • Morizono, K.1    Xie, Y.2    Olafsen, T.3    Lee, B.4    Dasgupta, A.5    Wu, A.M.6    Chen, I.S.7
  • 40
    • 77649152255 scopus 로고    scopus 로고
    • Autoimmunity and the clearance of dead cells
    • Nagata S, Hanayama R, Kawane K: Autoimmunity and the clearance of dead cells. Cell 2010, 140:619-630.
    • (2010) Cell , vol.140 , pp. 619-630
    • Nagata, S.1    Hanayama, R.2    Kawane, K.3
  • 41
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • DOI 10.1126/science.1155164
    • Mercer J, Helenius A: Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 2008, 320:531-535. (Pubitemid 351590666)
    • (2008) Science , vol.320 , Issue.5875 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 43
    • 57349140230 scopus 로고    scopus 로고
    • Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases
    • Soares MM, King SW, Thorpe PE: Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases. Nat Med 2008, 14:1357-1362.
    • (2008) Nat Med , vol.14 , pp. 1357-1362
    • Soares, M.M.1    King, S.W.2    Thorpe, P.E.3
  • 44
    • 33751079330 scopus 로고    scopus 로고
    • Gas6 and protein S: Vitamin K-dependent ligands for the Axl receptor tyrosine kinase subfamily
    • DOI 10.1111/j.1742-4658.2006.05529.x
    • Hafizi S, Dahlback B: Gas6 and protein S. Vitamin K-dependent ligands for the Axl receptor tyrosine kinase subfamily. FEBS J 2006, 273:5231-5244. (Pubitemid 44772384)
    • (2006) FEBS Journal , vol.273 , Issue.23 , pp. 5231-5244
    • Hafizi, S.1    Dahlback, B.2
  • 46
    • 65549140728 scopus 로고    scopus 로고
    • HIV-1 entry inhibitors: An overview
    • Kuritzkes DR: HIV-1 entry inhibitors: an overview. Curr Opin HIV AIDS 2009, 4:82-87.
    • (2009) Curr Opin HIV AIDS , vol.4 , pp. 82-87
    • Kuritzkes, D.R.1
  • 48
    • 67049115575 scopus 로고    scopus 로고
    • The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection
    • Hauber I, Hohenberg H, Holstermann B, Hunstein W, Hauber J: The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection. Proc Natl Acad Sci USA 2009, 106:9033-9038.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9033-9038
    • Hauber, I.1    Hohenberg, H.2    Holstermann, B.3    Hunstein, W.4    Hauber, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.