메뉴 건너뛰기




Volumn 86, Issue 9, 2012, Pages 4743-4751

Hsp70 protein positively regulates rabies virus infection

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; MESSENGER RNA; NUCLEOPROTEIN N; QUERCETIN; UNCLASSIFIED DRUG; VIRUS NUCLEOPROTEIN;

EID: 84861302576     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.06501-11     Document Type: Article
Times cited : (108)

References (42)
  • 2
    • 33846484215 scopus 로고    scopus 로고
    • Hsp70 negatively controls rotavirus protein bioavailability in caco-2 cells infected by the rotavirus RF strain
    • Broquet AH, et al. 2007. Hsp70 negatively controls rotavirus protein bioavailability in caco-2 cells infected by the rotavirus RF strain. J. Virol. 81:1297-1304.
    • (2007) J. Virol. , vol.81 , pp. 1297-1304
    • Broquet, A.H.1
  • 3
    • 20644449468 scopus 로고    scopus 로고
    • Evidence for an association between heat shock protein 70 and the respiratory syncytial virus polymerase complex within lipid-raft membranes during virus infection
    • Brown G, et al. 2005. Evidence for an association between heat shock protein 70 and the respiratory syncytial virus polymerase complex within lipid-raft membranes during virus infection. Virology 338:69-80.
    • (2005) Virology , vol.338 , pp. 69-80
    • Brown, G.1
  • 4
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • Bukau B, Deuerling E, Pfund C, Craig EA. 2000. Getting newly synthesized proteins into shape. Cell 101:119-122.
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 6
    • 0028117909 scopus 로고
    • In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): existence of two N-binding sites on P protein
    • Chenik M, Chebli K, Gaudin Y, Blondel D. 1994. In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): existence of two N-binding sites on P protein. J. Gen. Virol. 75:2889-2896.
    • (1994) J. Gen. Virol. , vol.75 , pp. 2889-2896
    • Chenik, M.1    Chebli, K.2    Gaudin, Y.3    Blondel, D.4
  • 7
    • 0032411722 scopus 로고    scopus 로고
    • Nonsegmented negative-strand RNA viruses: genetics and manipulation of viral genomes
    • Conzelmann KK. 1998. Nonsegmented negative-strand RNA viruses: genetics and manipulation of viral genomes. Annu. Rev. Genet. 32:123-162.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 123-162
    • Conzelmann, K.K.1
  • 8
    • 77950660791 scopus 로고    scopus 로고
    • High affinity binding between Hsp70 and the C-terminal domain of the measles virus nucleoprotein requires an Hsp40 co-chaperone
    • Couturier M, et al. 2010. High affinity binding between Hsp70 and the C-terminal domain of the measles virus nucleoprotein requires an Hsp40 co-chaperone. J. Mol. Recognit. 23:301-315.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 301-315
    • Couturier, M.1
  • 9
    • 0027251126 scopus 로고
    • Antiviral effect of short hyperthermic treatment at specific stages of vesicular stomatitis virus replication cycle
    • De Marco A, Santoro MG. 1993. Antiviral effect of short hyperthermic treatment at specific stages of vesicular stomatitis virus replication cycle. J. Gen. Virol. 74:1685-1690.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1685-1690
    • De Marco, A.1    Santoro, M.G.2
  • 10
    • 0030767817 scopus 로고    scopus 로고
    • Herpes simplex virus Us11 protein enhances recovery of protein synthesis and survival in heat shock treated HeLa cells
    • Diaz-Latoud C, et al. 1997. Herpes simplex virus Us11 protein enhances recovery of protein synthesis and survival in heat shock treated HeLa cells. Cell Stress Chaperones 2:119-131.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 119-131
    • Diaz-Latoud, C.1
  • 11
    • 0032731094 scopus 로고    scopus 로고
    • The V protein of simian virus 5 inhibits interferon signaling by targeting STAT1 for proteasome-mediated degradation
    • Didcock L, Young DF, Goodbourn S, Randall RE. 1999. The V protein of simian virus 5 inhibits interferon signaling by targeting STAT1 for proteasome-mediated degradation. J. Virol. 73:9928-9933.
    • (1999) J. Virol. , vol.73 , pp. 9928-9933
    • Didcock, L.1    Young, D.F.2    Goodbourn, S.3    Randall, R.E.4
  • 12
    • 0036351317 scopus 로고    scopus 로고
    • Analysis of gene function in somatic mammalian cells using small interfering RNAs
    • Elbashir SM, Harborth J, Weber K, Tuschl T. 2002. Analysis of gene function in somatic mammalian cells using small interfering RNAs. Methods 26:199-213.
    • (2002) Methods , vol.26 , pp. 199-213
    • Elbashir, S.M.1    Harborth, J.2    Weber, K.3    Tuschl, T.4
  • 13
    • 0033798704 scopus 로고    scopus 로고
    • Sendai virus C proteins must interact directly with cellular components to interfere with interferon action
    • Garcin D, Curran J, Kolakofsky D. 2000. Sendai virus C proteins must interact directly with cellular components to interfere with interferon action. J. Virol. 74:8823-8830.
    • (2000) J. Virol. , vol.74 , pp. 8823-8830
    • Garcin, D.1    Curran, J.2    Kolakofsky, D.3
  • 14
    • 0034617991 scopus 로고    scopus 로고
    • Rabies virus-induced membrane fusion pathway
    • Gaudin Y. 2000. Rabies virus-induced membrane fusion pathway. J. Cell Biol. 150:601-612.
    • (2000) J. Cell Biol. , vol.150 , pp. 601-612
    • Gaudin, Y.1
  • 15
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 16
    • 0347003598 scopus 로고    scopus 로고
    • Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex
    • Hirayama E, Atagi H, Hiraki A, Kim J. 2004. Heat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex. J. Virol. 78:1263-1270.
    • (2004) J. Virol. , vol.78 , pp. 1263-1270
    • Hirayama, E.1    Atagi, H.2    Hiraki, A.3    Kim, J.4
  • 17
    • 0032425151 scopus 로고    scopus 로고
    • Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures
    • Iseni F, Barge A, Baudin F, Blondel D, Ruigrok RW. 1998. Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures. J. Gen. Virol. 79:2909-2919.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2909-2919
    • Iseni, F.1    Barge, A.2    Baudin, F.3    Blondel, D.4    Ruigrok, R.W.5
  • 18
    • 0026803306 scopus 로고
    • Vaccinia virus infection induces a stress response that leads to association of Hsp70 with viral proteins
    • Jindal S, Young RA. 1992. Vaccinia virus infection induces a stress response that leads to association of Hsp70 with viral proteins. J. Virol. 66:5357-5362.
    • (1992) J. Virol. , vol.66 , pp. 5357-5362
    • Jindal, S.1    Young, R.A.2
  • 19
    • 79960373965 scopus 로고    scopus 로고
    • Reciprocal regulation of human immunodeficiency virus-1 gene expression and replication by heat shock proteins 40 and 70
    • Kumar M, et al. 2011. Reciprocal regulation of human immunodeficiency virus-1 gene expression and replication by heat shock proteins 40 and 70. J. Mol. Biol. 410:944-958.
    • (2011) J. Mol. Biol. , vol.410 , pp. 944-958
    • Kumar, M.1
  • 20
    • 67749104678 scopus 로고    scopus 로고
    • Functional characterization of Negri bodies (NBs) in rabies virus infected cells: evidence that NBs are sites of viral transcription and replication
    • Lahaye X, et al. 2009. Functional characterization of Negri bodies (NBs) in rabies virus infected cells: evidence that NBs are sites of viral transcription and replication. J. Virol. 83:7948-7958.
    • (2009) J. Virol. , vol.83 , pp. 7948-7958
    • Lahaye, X.1
  • 21
    • 0036146243 scopus 로고    scopus 로고
    • A novel expression cassette of lyssavirus shows that the distantly related Mokola virus can rescue a defective rabies virus genome
    • Le Mercier P, Jacob Y, Tanner K, Tordo N. 2002. A novel expression cassette of lyssavirus shows that the distantly related Mokola virus can rescue a defective rabies virus genome. J. Virol. 76:2024-2027.
    • (2002) J. Virol. , vol.76 , pp. 2024-2027
    • Le Mercier, P.1    Jacob, Y.2    Tanner, K.3    Tordo, N.4
  • 22
    • 79952076763 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits the activity of influenza a virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo
    • Li G, Zhang J, Tong X, Liu W, Ye X. 2011. Heat shock protein 70 inhibits the activity of influenza a virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo. PLoS One 6:e16546.
    • (2011) PLoS One , vol.6
    • Li, G.1    Zhang, J.2    Tong, X.3    Liu, W.4    Ye, X.5
  • 23
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • Mayer MP. 2010. Gymnastics of molecular chaperones. Mol. Cell 39:321-331.
    • (2010) Mol. Cell. , vol.39 , pp. 321-331
    • Mayer, M.P.1
  • 24
    • 16444378781 scopus 로고    scopus 로고
    • Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies
    • Mayer MP. 2005. Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies. Rev. Physiol. Biochem. Pharmacol. 153:1-46.
    • (2005) Rev. Physiol. Biochem. Pharmacol. , vol.153 , pp. 1-46
    • Mayer, M.P.1
  • 25
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer MP, Bukau B. 2005. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol. Life Sci. 62:670-684.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 26
    • 61449235415 scopus 로고    scopus 로고
    • Toll-like receptor 3 (TLR3) plays a major role in the formation of rabies virus Negri bodies
    • Menager P, et al. 2009. Toll-like receptor 3 (TLR3) plays a major role in the formation of rabies virus Negri bodies. PLoS Pathog. 5:e1000315.
    • (2009) PLoS Pathog , vol.5
    • Menager, P.1
  • 27
    • 0023260838 scopus 로고
    • Activated Ha-ras can cooperate with defective simian virus 40 in the transformation of nonestablished rat embryo fibroblasts
    • Michalovitz D, Fischer-Fantuzzi L, Vesco C, Pipas JM, Oren M. 1987. Activated Ha-ras can cooperate with defective simian virus 40 in the transformation of nonestablished rat embryo fibroblasts. J. Virol. 61:2648-2654.
    • (1987) J. Virol. , vol.61 , pp. 2648-2654
    • Michalovitz, D.1    Fischer-Fantuzzi, L.2    Vesco, C.3    Pipas, J.M.4    Oren, M.5
  • 28
    • 79952071414 scopus 로고    scopus 로고
    • Emerging picture of host chaperone and cyclophilin roles in RNA virus replication
    • Nagy PD, Wang RY, Pogany J, Hafren A, Makinen K. 2011. Emerging picture of host chaperone and cyclophilin roles in RNA virus replication. Virology 411:374-382.
    • (2011) Virology , vol.411 , pp. 374-382
    • Nagy, P.D.1    Wang, R.Y.2    Pogany, J.3    Hafren, A.4    Makinen, K.5
  • 29
    • 0025358461 scopus 로고
    • Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins
    • Oglesbee M, Ringler S, Krakowka S. 1990. Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins. J. Gen. Virol. 71:1585-1590.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1585-1590
    • Oglesbee, M.1    Ringler, S.2    Krakowka, S.3
  • 30
    • 0027180233 scopus 로고
    • Enhanced production of morbillivirus gene-specific RNAs following induction of the cellular stress response in stable persistent infection
    • Oglesbee MJ, Kenney H, Kenney T, Krakowka S. 1993. Enhanced production of morbillivirus gene-specific RNAs following induction of the cellular stress response in stable persistent infection. Virology 192: 556-567.
    • (1993) Virology , vol.192 , pp. 556-567
    • Oglesbee, M.J.1    Kenney, H.2    Kenney, T.3    Krakowka, S.4
  • 31
    • 0021219338 scopus 로고
    • Heat shock protein synthesis and cell survival in clones of normal and simian virus 40-transformed mouse embryo cells
    • Omar RA, Lanks KW. 1984. Heat shock protein synthesis and cell survival in clones of normal and simian virus 40-transformed mouse embryo cells. Cancer Res. 44:3976-3982.
    • (1984) Cancer Res , vol.44 , pp. 3976-3982
    • Omar, R.A.1    Lanks, K.W.2
  • 32
    • 0023856783 scopus 로고
    • Viral proteins required for the in vitro replication of vesicular stomatitis virus defective interfering particle genome RNA
    • Peluso RW, Moyer SA. 1988. Viral proteins required for the in vitro replication of vesicular stomatitis virus defective interfering particle genome RNA. Virology 162:369-376.
    • (1988) Virology , vol.162 , pp. 369-376
    • Peluso, R.W.1    Moyer, S.A.2
  • 33
    • 0026061319 scopus 로고
    • Analysis of the specificity and mechanism of transcriptional activation of the human hsp70 gene during infection by DNA viruses
    • Phillips B, Abravaya K, Morimoto RI. 1991. Analysis of the specificity and mechanism of transcriptional activation of the human hsp70 gene during infection by DNA viruses. J. Virol. 65:5680-5692.
    • (1991) J. Virol. , vol.65 , pp. 5680-5692
    • Phillips, B.1    Abravaya, K.2    Morimoto, R.I.3
  • 34
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO. 2003. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. 228:111-133.
    • (2003) Exp. Biol. Med. , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 35
    • 1942469432 scopus 로고    scopus 로고
    • Two RNA polymerase complexes from vesicular stomatitis virus-infected cells that carry out transcription and replication of genome RNA
    • Qanungo KR, Shaji D, Mathur M, Banerjee AK. 2004. Two RNA polymerase complexes from vesicular stomatitis virus-infected cells that carry out transcription and replication of genome RNA. Proc. Natl. Acad. Sci. U. S. A. 101:5952-5957.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 5952-5957
    • Qanungo, K.R.1    Shaji, D.2    Mathur, M.3    Banerjee, A.K.4
  • 36
    • 0031031743 scopus 로고    scopus 로고
    • Mapping of monoclonal antibody epitopes of the rabies virus P protein
    • Raux H, Iseni F, Lafay F, Blondel D. 1997. Mapping of monoclonal antibody epitopes of the rabies virus P protein. J. Gen. Virol. 78:119-124.
    • (1997) J. Gen. Virol. , vol.78 , pp. 119-124
    • Raux, H.1    Iseni, F.2    Lafay, F.3    Blondel, D.4
  • 37
    • 0026675014 scopus 로고
    • Identification of heat shock protein 70 in the rabies virion
    • Sagara J, Kawai A. 1992. Identification of heat shock protein 70 in the rabies virion. Virology 190:845-848.
    • (1992) Virology , vol.190 , pp. 845-848
    • Sagara, J.1    Kawai, A.2
  • 38
    • 0028035113 scopus 로고
    • Heat shock proteins and virus replication: hsp70s as mediators of the antiviral effects of prostaglandins
    • Santoro MG. 1994. Heat shock proteins and virus replication: hsp70s as mediators of the antiviral effects of prostaglandins. Experientia 50:1039-1047.
    • (1994) Experientia , vol.50 , pp. 1039-1047
    • Santoro, M.G.1
  • 39
    • 72849128415 scopus 로고    scopus 로고
    • A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication
    • Weeks SA, et al. 2010. A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication. J. Virol. 84:330-339.
    • (2010) J. Virol. , vol.84 , pp. 330-339
    • Weeks, S.A.1
  • 40
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: localized functions of cytosolic chaperones
    • Young JC, Barral JM, Ulrich Hartl F. 2003. More than folding: localized functions of cytosolic chaperones. Trends Biochem. Sci. 28:541-547.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Ulrich Hartl, F.3
  • 41
    • 55649120647 scopus 로고    scopus 로고
    • Protective effect of a RSV subunit vaccine candidate G1F/M2 was enhanced by a HSP70-Like protein in mice
    • Zeng R, Zhang Z, Mei X, Gong W, Wei L. 2008. Protective effect of a RSV subunit vaccine candidate G1F/M2 was enhanced by a HSP70-Like protein in mice. Biochem. Biophys. Res. Commun. 377:495-499.
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 495-499
    • Zeng, R.1    Zhang, Z.2    Mei, X.3    Gong, W.4    Wei, L.5
  • 42
    • 19444370973 scopus 로고    scopus 로고
    • Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus
    • Zhang X, et al. 2005. Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus. Virology 337:162-174.
    • (2005) Virology , vol.337 , pp. 162-174
    • Zhang, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.