메뉴 건너뛰기




Volumn 88, Issue 8, 2014, Pages 4403-4413

Mechanism of action and capsid-stabilizing properties of VHHs with an in vitro antipolioviral activity

Author keywords

[No Author keywords available]

Indexed keywords

ARILDONE; NANOBODY; PIRODAVIR; PVSP19B ANTIBODY; PVSP29F ANTIBODY; PVSP6A ANTIBODY; PVSS21E ANTIBODY; PVSS8A ANTIBODY; UNCLASSIFIED DRUG;

EID: 84896920110     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03402-13     Document Type: Article
Times cited : (24)

References (49)
  • 1
    • 77952320069 scopus 로고    scopus 로고
    • The global introduction of inactivated polio vaccine can circumvent the oral polio vaccine paradox
    • Heinsbroek E, Ruitenberg EJ. 2010. The global introduction of inactivated polio vaccine can circumvent the oral polio vaccine paradox. Vaccine 28:3778-3783. http://dx.doi.org/10.1016/j.vaccine.2010.02.095.
    • (2010) Vaccine , vol.28 , pp. 3778-3783
    • Heinsbroek, E.1    Ruitenberg, E.J.2
  • 2
    • 84896923357 scopus 로고    scopus 로고
    • Committee on Development of a Polio Antiviral and its Potential Role in Global Poliomyelitis Eradication-National Research Council. The National Academies Press, Washington, DC.
    • Committee on Development of a Polio Antiviral and its Potential Role in Global Poliomyelitis Eradication-National Research Council. 2006. Exploring the role of antiviral drugs in the eradication of polio: workshop report. The National Academies Press, Washington, DC. http://www.nap.edu/openbook.php?record_id=11599.
    • (2006) Exploring the role of antiviral drugs in the eradication of polio: workshop report
  • 3
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • Arbabi Ghahroudi M, Desmyter A, Wyns L, Hamers R, Muyldermans S. 1997. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett. 414:521-526. http://dx.doi.org/10.1016/S0014-5793(97)01062-4.
    • (1997) FEBS Lett. , vol.414 , pp. 521-526
    • Arbabi Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 6
  • 7
    • 0018696940 scopus 로고
    • Topographical studies on poliovirus capsid proteins by chemical modification and cross-linking with bifunctional reagents
    • Wetz K, Habermehl KO. 1979. Topographical studies on poliovirus capsid proteins by chemical modification and cross-linking with bifunctional reagents. J. Gen. Virol. 44:525-534. http://dx.doi.org/10.1099/0022-1317-44-2-525.
    • (1979) J. Gen. Virol. , vol.44 , pp. 525-534
    • Wetz, K.1    Habermehl, K.O.2
  • 8
    • 0023198719 scopus 로고
    • Myristylation of picornavirus capsid protein VP4 and its structural significance
    • Chow M, Newman JF, Filman D, Hogle JM, Rowlands DJ, Brown F. 1987. Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature 327:482-486. http://dx.doi.org/10.1038/327482a0.
    • (1987) Nature , vol.327 , pp. 482-486
    • Chow, M.1    Newman, J.F.2    Filman, D.3    Hogle, J.M.4    Rowlands, D.J.5    Brown, F.6
  • 9
    • 0025273268 scopus 로고
    • Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding
    • Fricks CE, Hogle JM. 1990. Cell-induced conformational change in poliovirus: externalization of the amino terminus of VP1 is responsible for liposome binding. J. Virol. 64:1934-1945.
    • (1990) J. Virol. , vol.64 , pp. 1934-1945
    • Fricks, C.E.1    Hogle, J.M.2
  • 10
    • 0022409872 scopus 로고
    • Three-dimensional structure of poliovirus at 2.9 A resolution
    • Hogle JM, Chow M, Filman DJ. 1985. Three-dimensional structure of poliovirus at 2.9 A resolution. Science 229:1358-1365. http://dx.doi.org/10.1126/science.2994218.
    • (1985) Science , vol.229 , pp. 1358-1365
    • Hogle, J.M.1    Chow, M.2    Filman, D.J.3
  • 11
    • 0345734205 scopus 로고    scopus 로고
    • Cholesterol removal by methyl-betacyclodextrin inhibits poliovirus entry
    • Danthi P, Chow M. 2004. Cholesterol removal by methyl-betacyclodextrin inhibits poliovirus entry. J. Virol. 78:33-41. http://dx.doi.org/10.1128/JVI.78.1.33-41.2004.
    • (2004) J. Virol. , vol.78 , pp. 33-41
    • Danthi, P.1    Chow, M.2
  • 12
    • 33645997366 scopus 로고    scopus 로고
    • Characterization of early steps in the poliovirus infection process: receptor-decorated liposomes induce conversion of the virus to membrane-anchored entryintermediate particles
    • Tuthill TJ, Bubeck D, Rowlands DJ, Hogle JM. 2006. Characterization of early steps in the poliovirus infection process: receptor-decorated liposomes induce conversion of the virus to membrane-anchored entryintermediate particles. J. Virol. 80:172-180. http://dx.doi.org/10.1128/JVI.80.1.172-180.2006.
    • (2006) J. Virol. , vol.80 , pp. 172-180
    • Tuthill, T.J.1    Bubeck, D.2    Rowlands, D.J.3    Hogle, J.M.4
  • 13
    • 77950852687 scopus 로고    scopus 로고
    • Catching a virus in the act of RNA release: a novel poliovirus uncoating intermediate characterized by cryo-electron microscopy
    • Levy HC, Bostina M, Filman DJ, Hogle JM. 2010. Catching a virus in the act of RNA release: a novel poliovirus uncoating intermediate characterized by cryo-electron microscopy. J. Virol. 84:4426-4441. http://dx.doi.org/10.1128/JVI.02393-09.
    • (2010) J. Virol. , vol.84 , pp. 4426-4441
    • Levy, H.C.1    Bostina, M.2    Filman, D.J.3    Hogle, J.M.4
  • 14
    • 84875520601 scopus 로고    scopus 로고
    • RNA transfer from poliovirus 135S particles across membranes is mediated by long umbilical connectors
    • Strauss M, Levy HC, Bostina M, Filman DJ, Hogle JM. 2013. RNA transfer from poliovirus 135S particles across membranes is mediated by long umbilical connectors. J. Virol. 87:3903-3914. http://dx.doi.org/10.1128/JVI.03209-12.
    • (2013) J. Virol. , vol.87 , pp. 3903-3914
    • Strauss, M.1    Levy, H.C.2    Bostina, M.3    Filman, D.J.4    Hogle, J.M.5
  • 15
    • 34249030028 scopus 로고    scopus 로고
    • Neutralization of animal virus infectivity by antibody
    • Reading SA, Dimmock NJ. 2007. Neutralization of animal virus infectivity by antibody. Arch. Virol. 152:1047-1059. http://dx.doi.org/10.1007/s00705-006-0923-8.
    • (2007) Arch. Virol. , vol.152 , pp. 1047-1059
    • Reading, S.A.1    Dimmock, N.J.2
  • 16
    • 0022341105 scopus 로고
    • Hit-and-run neutralization of poliovirus
    • Brioen P, Rombaut B, Boeye A. 1985. Hit-and-run neutralization of poliovirus. J. Gen. Virol. 66(Part 11):2495-2499. http://dx.doi.org/10.1099/0022-1317-66-11-2495.
    • (1985) J. Gen. Virol. , vol.66 , Issue.PART 11 , pp. 2495-2499
    • Brioen, P.1    Rombaut, B.2    Boeye, A.3
  • 17
    • 0027221067 scopus 로고
    • Monoclonal antibodies that disrupt poliovirus only at fever temperatures
    • Delaet I, Boeye A. 1993. Monoclonal antibodies that disrupt poliovirus only at fever temperatures. J. Virol. 67:5299-5302.
    • (1993) J. Virol. , vol.67 , pp. 5299-5302
    • Delaet, I.1    Boeye, A.2
  • 18
    • 0026645482 scopus 로고
    • Antigenic N to H conversion of poliovirus by a monoclonal antibody at low ionic strength
    • Delaet I, Vrijsen R, Boeye A. 1992. Antigenic N to H conversion of poliovirus by a monoclonal antibody at low ionic strength. Virology 188: 93-101. http://dx.doi.org/10.1016/0042-6822(92)90738-B.
    • (1992) Virology , vol.188 , pp. 93-101
    • Delaet, I.1    Vrijsen, R.2    Boeye, A.3
  • 19
    • 0028344850 scopus 로고
    • Capsid destabilization is required for antibodymediated disruption of poliovirus
    • Delaet I, Boeye A. 1994. Capsid destabilization is required for antibodymediated disruption of poliovirus. J. Gen. Virol. 75(Part 3):581-587. http://dx.doi.org/10.1099/0022-1317-75-3-581.
    • (1994) J. Gen. Virol. , vol.75 , Issue.PART 3 , pp. 581-587
    • Delaet, I.1    Boeye, A.2
  • 20
    • 79954580247 scopus 로고    scopus 로고
    • A simple quantitative affinity capturing assay of poliovirus antigens and subviral particles by single-domain antibodies using magnetic beads
    • Thys B, Saerens D, Schotte L, De BG, Muyldermans S, Hassanzadeh-Ghassabeh G, Rombaut B. 2011. A simple quantitative affinity capturing assay of poliovirus antigens and subviral particles by single-domain antibodies using magnetic beads. J. Virol. Methods 173:300-305. http://dx.doi.org/10.1016/j.jviromet.2011.02.023.
    • (2011) J. Virol. Methods , vol.173 , pp. 300-305
    • Thys, B.1    Saerens, D.2    Schotte, L.3    De, B.G.4    Muyldermans, S.5    Hassanzadeh-Ghassabeh, G.6    Rombaut, B.7
  • 21
    • 2542501627 scopus 로고    scopus 로고
    • Mechanism of action at the molecular level of the antiviral drug 3(2H)-isoflavene against type 2 poliovirus
    • Salvati AL, De DA, Tait S, Canitano A, Lahm A, Fiore L. 2004. Mechanism of action at the molecular level of the antiviral drug 3(2H)-isoflavene against type 2 poliovirus. Antimicrob. Agents Chemother. 48: 2233-2243. http://dx.doi.org/10.1128/AAC.48.6.2233-2243.2004.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 2233-2243
    • Salvati, A.L.1    De, D.A.2    Tait, S.3    Canitano, A.4    Lahm, A.5    Fiore, L.6
  • 22
    • 0026502172 scopus 로고
    • In vitro activity of pirodavir (R 77975), a substituted phenoxy-pyridazinamine with broad-spectrum antipicornaviral activity
    • Andries K, Dewindt B, Snoeks J, Willebrords R, van Eemeren K, Stokbroekx R, Janssen PA. 1992. In vitro activity of pirodavir (R 77975), a substituted phenoxy-pyridazinamine with broad-spectrum antipicornaviral activity. Antimicrob. Agents Chemother. 36:100-107. http://dx.doi.org/10.1128/AAC.36.1.100.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 100-107
    • Andries, K.1    Dewindt, B.2    Snoeks, J.3    Willebrords, R.4    van Eemeren, K.5    Stokbroekx, R.6    Janssen, P.A.7
  • 23
    • 83955164248 scopus 로고    scopus 로고
    • Combating enterovirus replication: state-of-the-art on antiviral research
    • Thibaut HJ, De Palma AM, Neyts J. 2012. Combating enterovirus replication: state-of-the-art on antiviral research. Biochem. Pharmacol. 83: 185-192. http://dx.doi.org/10.1016/j.bcp.2011.08.016.
    • (2012) Biochem. Pharmacol. , vol.83 , pp. 185-192
    • Thibaut, H.J.1    De Palma, A.M.2    Neyts, J.3
  • 24
    • 0024382865 scopus 로고
    • Eclipse products of poliovirus after cold-synchronized infection of HeLa cells
    • Everaert L, Vrijsen R, Boeye A. 1989. Eclipse products of poliovirus after cold-synchronized infection of HeLa cells. Virology 171:76-82. http://dx.doi.org/10.1016/0042-6822(89)90512-6.
    • (1989) Virology , vol.171 , pp. 76-82
    • Everaert, L.1    Vrijsen, R.2    Boeye, A.3
  • 25
    • 78650255354 scopus 로고    scopus 로고
    • Antipoliovirus activity and mechanism of action of 3-methylthio-5-phenyl-4-isothiazolecarbonitrile
    • Garozzo A, Stivala A, Tempera G, Castro A. 2010. Antipoliovirus activity and mechanism of action of 3-methylthio-5-phenyl-4-isothiazolecarbonitrile. Antiviral Res. 88:325-328. http://dx.doi.org/10.1016/j.antiviral.2010.10.003.
    • (2010) Antiviral Res. , vol.88 , pp. 325-328
    • Garozzo, A.1    Stivala, A.2    Tempera, G.3    Castro, A.4
  • 27
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, GrigorieffN. 2003. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142:334-347. http://dx.doi.org/10.1016/S1047-8477(03)00069-8.
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 29
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: high-resolution refinement of single particle structures
    • GrigorieffN. 2007. FREALIGN: high-resolution refinement of single particle structures. J. Struct. Biol. 157:117-125. http://dx.doi.org/10.1016/j.jsb.2006.05.004.
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 30
    • 77958193837 scopus 로고    scopus 로고
    • GPU-enabled FREALIGN: accelerating single particle 3D reconstruction and refinement in Fourier space on graphics processors
    • Li X, GrigorieffN, Cheng Y. 2010. GPU-enabled FREALIGN: accelerating single particle 3D reconstruction and refinement in Fourier space on graphics processors. J. Struct. Biol. 172:407-412. http://dx.doi.org/10.1016/j.jsb.2010.06.010.
    • (2010) J. Struct. Biol. , vol.172 , pp. 407-412
    • Li, X.1    Grigorieff, N.2    Cheng, Y.3
  • 31
    • 51549084591 scopus 로고    scopus 로고
    • Sharpening high resolution information in single particle electron cryomicroscopy
    • Fernandez JJ, Luque D, Caston JR, Carrascosa JL. 2008. Sharpening high resolution information in single particle electron cryomicroscopy. J. Struct. Biol. 164:170-175. http://dx.doi.org/10.1016/j.jsb.2008.05.010.
    • (2008) J. Struct. Biol. , vol.164 , pp. 170-175
    • Fernandez, J.J.1    Luque, D.2    Caston, J.R.3    Carrascosa, J.L.4
  • 36
    • 84892469578 scopus 로고    scopus 로고
    • Cryo-electron microscopy reconstruction shows poliovirus 135s particles poised for membrane interaction and RNA release
    • Butan C, Filman DJ, Hogle JM. 2014. Cryo-electron microscopy reconstruction shows poliovirus 135s particles poised for membrane interaction and RNA release. J. Virol. 88:1758-1770. http://dx.doi.org/10.1128/JVI.01949-13.
    • (2014) J. Virol. , vol.88 , pp. 1758-1770
    • Butan, C.1    Filman, D.J.2    Hogle, J.M.3
  • 37
    • 0034725699 scopus 로고    scopus 로고
    • Two distinct binding affinities of poliovirus for its cellular receptor
    • McDermott BM, Jr, Rux AH, Eisenberg RJ, Cohen GH, Racaniello VR. 2000. Two distinct binding affinities of poliovirus for its cellular receptor. J. Biol. Chem. 275:23089-23096. http://dx.doi.org/10.1074/jbc. M002146200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23089-23096
    • McDermott Jr., B.M.1    Rux, A.H.2    Eisenberg, R.J.3    Cohen, G.H.4    Racaniello, V.R.5
  • 38
    • 0034070027 scopus 로고    scopus 로고
    • An antiviral compound that blocks structural transitions of poliovirus prevents receptor binding at low temperatures
    • Dove AW, Racaniello VR. 2000. An antiviral compound that blocks structural transitions of poliovirus prevents receptor binding at low temperatures. J. Virol. 74:3929-3931. http://dx.doi.org/10.1128/JVI.74.8.3929-3931.2000.
    • (2000) J. Virol. , vol.74 , pp. 3929-3931
    • Dove, A.W.1    Racaniello, V.R.2
  • 39
    • 22144468063 scopus 로고    scopus 로고
    • Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex
    • Bubeck D, Filman DJ, Hogle JM. 2005. Cryo-electron microscopy reconstruction of a poliovirus-receptor-membrane complex. Nat. Struct. Mol. Biol. 12:615-618. http://dx.doi.org/10.1038/nsmb955.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 615-618
    • Bubeck, D.1    Filman, D.J.2    Hogle, J.M.3
  • 40
    • 35148838173 scopus 로고    scopus 로고
    • Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus-receptor-membrane complex at 30 A resolution
    • Bostina M, Bubeck D, Schwartz C, Nicastro D, Filman DJ, Hogle JM. 2007. Single particle cryoelectron tomography characterization of the structure and structural variability of poliovirus-receptor-membrane complex at 30 A resolution. J. Struct. Biol. 160:200-210. http://dx.doi.org/10.1016/j.jsb.2007.08.009.
    • (2007) J. Struct. Biol. , vol.160 , pp. 200-210
    • Bostina, M.1    Bubeck, D.2    Schwartz, C.3    Nicastro, D.4    Filman, D.J.5    Hogle, J.M.6
  • 42
    • 0024402908 scopus 로고
    • Lack of quantitative correlation between inhibition of replication of rhinoviruses by an antiviral drug and their stabilization
    • Andries K, Dewindt B, Snoeks J, Willebrords R. 1989. Lack of quantitative correlation between inhibition of replication of rhinoviruses by an antiviral drug and their stabilization. Arch. Virol. 106:51-61. http://dx.doi.org/10.1007/BF01311037.
    • (1989) Arch. Virol. , vol.106 , pp. 51-61
    • Andries, K.1    Dewindt, B.2    Snoeks, J.3    Willebrords, R.4
  • 46
    • 84857488318 scopus 로고    scopus 로고
    • Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid
    • Garriga D, Pickl-Herk A, Luque D, Wruss J, Caston JR, Blaas D, Verdaguer N. 2012. Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid. PLoS Pathog. 8:e1002473. http://dx.doi.org/10.1371/journal.ppat.1002473.
    • (2012) PLoS Pathog. , vol.8
    • Garriga, D.1    Pickl-Herk, A.2    Luque, D.3    Wruss, J.4    Caston, J.R.5    Blaas, D.6    Verdaguer, N.7
  • 47
    • 0020564666 scopus 로고
    • Neutralization of poliovirus by antibody-mediated polymerization
    • Brioen P, Dekegel D, Boeye A. 1983. Neutralization of poliovirus by antibody-mediated polymerization. Virology 127:463-468. http://dx.doi.org/10.1016/0042-6822(83)90159-9.
    • (1983) Virology , vol.127 , pp. 463-468
    • Brioen, P.1    Dekegel, D.2    Boeye, A.3
  • 48
    • 0020619874 scopus 로고
    • Neutralization of poliovirus by a monoclonal antibody: kinetics and stoichiometry
    • Icenogle J, Shiwen H, Duke G, Gilbert S, Rueckert R, Anderegg J. 1983. Neutralization of poliovirus by a monoclonal antibody: kinetics and stoichiometry. Virology 127:412-425. http://dx.doi.org/10.1016/0042-6822(83)90154-X.
    • (1983) Virology , vol.127 , pp. 412-425
    • Icenogle, J.1    Shiwen, H.2    Duke, G.3    Gilbert, S.4    Rueckert, R.5    Anderegg, J.6
  • 49
    • 0028341259 scopus 로고
    • Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature
    • Li Q, Yafal AG, Lee YM, Hogle J, Chow M. 1994. Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature. J. Virol. 68:3965-3970.
    • (1994) J. Virol. , vol.68 , pp. 3965-3970
    • Li, Q.1    Yafal, A.G.2    Lee, Y.M.3    Hogle, J.4    Chow, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.