메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages

Purinergic receptor functionality is necessary for infection of human hepatocytes by hepatitis delta virus and hepatitis b virus

Author keywords

[No Author keywords available]

Indexed keywords

BRILLIANT BLUE; PURINERGIC P2X7 RECEPTOR; PURINERGIC RECEPTOR; PYRIDOXAL PHOSPHATE 6 AZOPHENYL 2',4' DISULFONIC ACID; SURAMIN; COOMASSIE BRILLIANT BLUE; DRUG DERIVATIVE; FUCHSINE; PYRIDOXAL 5 PHOSPHATE; PYRIDOXAL PHOSPHATE-6-AZOPHENYL-2',4'-DISULFONIC ACID; VIRUS RNA;

EID: 78650968191     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015784     Document Type: Article
Times cited : (47)

References (49)
  • 1
    • 34547755447 scopus 로고    scopus 로고
    • Hepadnaviruses
    • In: Knipe DM, ed., Fifth ed. Philadelphia: Lippincott Williams & Wilkins
    • Seeger C, Zoulim F, Mason WS (2007) Hepadnaviruses. In: Knipe DM, ed. Fields Virology. Fifth ed. Philadelphia: Lippincott Williams & Wilkins. pp 2977-3030.
    • (2007) Fields Virology , pp. 2977-3030
    • Seeger, C.1    Zoulim, F.2    Mason, W.S.3
  • 2
    • 35448948701 scopus 로고    scopus 로고
    • Hepatitis D (delta) virus
    • In: Knipe DM, ed., Fifth ed. Philadelphia: Lippincott Williams & Wilkins
    • Taylor JM, Farci P, Purcell RH (2007) Hepatitis D (delta) virus. In: Knipe DM, ed. Fields Virology. Fifth ed. Philadelphia: Lippincott Williams & Wilkins. pp 3031-3046.
    • (2007) Fields Virology , pp. 3031-3046
    • Taylor, J.M.1    Farci, P.2    Purcell, R.H.3
  • 3
    • 0017565349 scopus 로고
    • Immunofluorescence detection of a new antigen-antibody system associated to the hepatitis B virus in the liver and in the serum of HBsAg carriers
    • Rizzetto M, Canese MG, Arico J, Crivelli O, Bonino F, et al. (1977) Immunofluorescence detection of a new antigen-antibody system associated to the hepatitis B virus in the liver and in the serum of HBsAg carriers. Gut 18: 997-1003.
    • (1977) Gut , vol.18 , pp. 997-1003
    • Rizzetto, M.1    Canese, M.G.2    Arico, J.3    Crivelli, O.4    Bonino, F.5
  • 4
    • 44149124526 scopus 로고    scopus 로고
    • New insights into hepatitis B and hepatitis delta virus entry
    • Urban S (2008) New insights into hepatitis B and hepatitis delta virus entry. Future Virol 3: 253-264.
    • (2008) Future Virol , vol.3 , pp. 253-264
    • Urban, S.1
  • 5
    • 0024206302 scopus 로고
    • Suramin inhibits in vitro infection by duck hepatitis B virus, Rous sarcoma virus, and hepatitis delta virus
    • Petcu DJ, Aldrich CE, Coates L, Taylor JM, Mason WS (1988) Suramin inhibits in vitro infection by duck hepatitis B virus, Rous sarcoma virus, and hepatitis delta virus. Virology 167: 385-392.
    • (1988) Virology , vol.167 , pp. 385-392
    • Petcu, D.J.1    Aldrich, C.E.2    Coates, L.3    Taylor, J.M.4    Mason, W.S.5
  • 6
    • 36949038870 scopus 로고    scopus 로고
    • Hepatitis B virus infection initiates with a large surface protein-dependent binding to heparan sulfate proteoglycans
    • Schulze A, Gripon P, Urban S (2007) Hepatitis B virus infection initiates with a large surface protein-dependent binding to heparan sulfate proteoglycans. Hepatology 46: 1759-1768.
    • (2007) Hepatology , vol.46 , pp. 1759-1768
    • Schulze, A.1    Gripon, P.2    Urban, S.3
  • 7
    • 0020337392 scopus 로고
    • The inhibition of yellow fever virus multiplication by suramin: A preliminary note
    • Croon JJ, Wolff HL (1982) The inhibition of yellow fever virus multiplication by suramin: a preliminary note. Acta Leiden 48: 5-8.
    • (1982) Acta Leiden , vol.48 , pp. 5-8
    • Croon, J.J.1    Wolff, H.L.2
  • 8
    • 0022612256 scopus 로고
    • Comparative inhibitory effects of suramin and other selected compounds on the infectivity and replication of human T-cell lymphotropic virus (HTLV-III)/lymphadenopathy-associated virus (LAV)
    • Balzarini J, Mitsuya H, De Clercq E, Broder S (1986) Comparative inhibitory effects of suramin and other selected compounds on the infectivity and replication of human T-cell lymphotropic virus (HTLV-III)/lymphadenopathy-associated virus (LAV). Int J Cancer 37: 451-457.
    • (1986) Int J Cancer , vol.37 , pp. 451-457
    • Balzarini, J.1    Mitsuya, H.2    de Clercq, E.3    Broder, S.4
  • 9
    • 0033602699 scopus 로고    scopus 로고
    • The polysulfonated compound suramin blocks adsorption and lateral diffusion of herpes simplex virus type-1 in vero cells
    • Aguilar JS, Rice M, Wagner EK (1999) The polysulfonated compound suramin blocks adsorption and lateral diffusion of herpes simplex virus type-1 in vero cells. Virology 258: 141-151.
    • (1999) Virology , vol.258 , pp. 141-151
    • Aguilar, J.S.1    Rice, M.2    Wagner, E.K.3
  • 11
    • 10744227483 scopus 로고    scopus 로고
    • Suramin and suramin analogues inhibit merozoite surface protein-1 secondary processing and erythrocyte invasion by the malaria parasite Plasmodium falciparum
    • Fleck SL, Birdsall B, Babon J, Dluzewski AR, Martin SR, et al. (2003) Suramin and suramin analogues inhibit merozoite surface protein-1 secondary processing and erythrocyte invasion by the malaria parasite Plasmodium falciparum. J Biol Chem 278: 47670-47677.
    • (2003) J Biol Chem , vol.278 , pp. 47670-47677
    • Fleck, S.L.1    Birdsall, B.2    Babon, J.3    Dluzewski, A.R.4    Martin, S.R.5
  • 12
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North RA (2002) Molecular physiology of P2X receptors. Physiol Rev 82: 1013-1067.
    • (2002) Physiol Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 13
    • 34248576759 scopus 로고    scopus 로고
    • Physiology and pathophysiology of purinergic neurotrans-mission
    • Burnstock G (2007) Physiology and pathophysiology of purinergic neurotrans-mission. Physiol Rev 87: 659-797.
    • (2007) Physiol Rev , vol.87 , pp. 659-797
    • Burnstock, G.1
  • 14
    • 77953106276 scopus 로고    scopus 로고
    • Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function
    • Lenertz LY, Wang Z, Guadarrama A, Hill LM, Gavala ML, et al. (2010) Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function. Biochemistry 49: 4611-4619.
    • (2010) Biochemistry , vol.49 , pp. 4611-4619
    • Lenertz, L.Y.1    Wang, Z.2    Guadarrama, A.3    Hill, L.M.4    Gavala, M.L.5
  • 15
    • 0035890154 scopus 로고    scopus 로고
    • Proteomic and functional evidence for a P2X7 receptor signalling complex
    • Kim M, Jiang LH, Wilson HL, North RA, Surprenant A (2001) Proteomic and functional evidence for a P2X7 receptor signalling complex. EMBO J 20: 6347-6358.
    • (2001) EMBO J , vol.20 , pp. 6347-6358
    • Kim, M.1    Jiang, L.H.2    Wilson, H.L.3    North, R.A.4    Surprenant, A.5
  • 16
    • 67349108796 scopus 로고    scopus 로고
    • P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways
    • Qu Y, Dubyak GR (2009) P2X7 receptors regulate multiple types of membrane trafficking responses and non-classical secretion pathways. Purinergic Signal 5: 163-173.
    • (2009) Purinergic Signal , vol.5 , pp. 163-173
    • Qu, Y.1    Dubyak, G.R.2
  • 17
    • 0033962501 scopus 로고    scopus 로고
    • Pyridoxal-phosphate-6-azophenyl-29,49-disulfonate (PPADS), a putative P2Y(1) receptor antagonist, blocks signaling at a site distal to the receptor in Madin-Darby canine kidney-D(1) cells
    • Shehnaz D, Torres B, Balboa MA, Insel PA (2000) Pyridoxal-phosphate-6-azophenyl-29,49-disulfonate (PPADS), a putative P2Y(1) receptor antagonist, blocks signaling at a site distal to the receptor in Madin-Darby canine kidney-D(1) cells. J Pharmacol Exp Ther 292: 346-350.
    • (2000) J Pharmacol Exp Ther , vol.292 , pp. 346-350
    • Shehnaz, D.1    Torres, B.2    Balboa, M.A.3    Insel, P.A.4
  • 18
  • 19
    • 77449148016 scopus 로고    scopus 로고
    • Recent patents on novel P2X(7) receptor antagonists and their potential for reducing central nervous system inflammation
    • Friedle SA, Curet MA, Watters JJ (2010) Recent patents on novel P2X(7) receptor antagonists and their potential for reducing central nervous system inflammation. Recent Pat CNS Drug Discov 5: 35-45.
    • (2010) Recent Pat CNS Drug Discov , vol.5 , pp. 35-45
    • Friedle, S.A.1    Curet, M.A.2    Watters, J.J.3
  • 20
    • 33646124242 scopus 로고    scopus 로고
    • Emerging challenges of assigning P2X7 receptor function and immunoreactivity in neurons
    • Anderson CM, Nedergaard M (2006) Emerging challenges of assigning P2X7 receptor function and immunoreactivity in neurons. Trends Neurosci 29: 257-262.
    • (2006) Trends Neurosci , vol.29 , pp. 257-262
    • Anderson, C.M.1    Nedergaard, M.2
  • 22
    • 33845189595 scopus 로고    scopus 로고
    • Characterization of a selective and potent antagonist of human P2X(7) receptors, AZ11645373
    • Stokes L, Jiang LH, Alcaraz L, Bent J, Bowers K, et al. (2006) Characterization of a selective and potent antagonist of human P2X(7) receptors, AZ11645373. Br J Pharmacol 149: 880-887.
    • (2006) Br J Pharmacol , vol.149 , pp. 880-887
    • Stokes, L.1    Jiang, L.H.2    Alcaraz, L.3    Bent, J.4    Bowers, K.5
  • 23
    • 34248345071 scopus 로고    scopus 로고
    • Immunoadhesins containing preS domains of hepatitis B virus large envelope protein are secreted and inhibit virus infection
    • Chai N, Gudima S, Chang J, Taylor J (2007) Immunoadhesins containing preS domains of hepatitis B virus large envelope protein are secreted and inhibit virus infection. J Virol 81: 4912-4918.
    • (2007) J Virol , vol.81 , pp. 4912-4918
    • Chai, N.1    Gudima, S.2    Chang, J.3    Taylor, J.4
  • 24
    • 36949024485 scopus 로고    scopus 로고
    • Role of glycosaminoglycans for binding and infection of hepatitis B virus
    • Leistner CM, Gruen-Bernhard S, Glebe D (2008) Role of glycosaminoglycans for binding and infection of hepatitis B virus. Cell Microbiol 10: 122-133.
    • (2008) Cell Microbiol , vol.10 , pp. 122-133
    • Leistner, C.M.1    Gruen-Bernhard, S.2    Glebe, D.3
  • 25
    • 58149390171 scopus 로고    scopus 로고
    • Host cell factors and functions involved in vesicular stomatitis virus entry
    • Johannsdottir HK, Mancini R, Kartenbeck J, Amato L, Helenius A (2009) Host cell factors and functions involved in vesicular stomatitis virus entry. J Virol 83: 440-453.
    • (2009) J Virol , vol.83 , pp. 440-453
    • Johannsdottir, H.K.1    Mancini, R.2    Kartenbeck, J.3    Amato, L.4    Helenius, A.5
  • 26
    • 68749092220 scopus 로고    scopus 로고
    • Mechanism of action of species-selective P2X(7) receptor antagonists
    • Michel AD, Ng SW, Roman S, Clay WC, Dean DK, et al. (2009) Mechanism of action of species-selective P2X(7) receptor antagonists. Br J Pharmacol 156: 1312-1325.
    • (2009) Br J Pharmacol , vol.156 , pp. 1312-1325
    • Michel, A.D.1    Ng, S.W.2    Roman, S.3    Clay, W.C.4    Dean, D.K.5
  • 27
    • 68149157440 scopus 로고    scopus 로고
    • Systemic administration of an antagonist of the ATP-sensitive receptor P2X7 improves recovery after spinal cord injury
    • Peng W, Cotrina ML, Han X, Yu H, Bekar L, et al. (2009) Systemic administration of an antagonist of the ATP-sensitive receptor P2X7 improves recovery after spinal cord injury. Proc Natl Acad Sci USA 106: 12489-12493.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12489-12493
    • Peng, W.1    Cotrina, M.L.2    Han, X.3    Yu, H.4    Bekar, L.5
  • 28
    • 49949084743 scopus 로고    scopus 로고
    • P2X7 receptor activation amplifies lipopolysaccharide-induced vascular hyporeactivity via interleukin-1 beta release
    • Chiao CW, Tostes RC, Webb RC (2008) P2X7 receptor activation amplifies lipopolysaccharide-induced vascular hyporeactivity via interleukin-1 beta release. J Pharmacol Exp Ther 326: 864-870.
    • (2008) J Pharmacol Exp Ther , vol.326 , pp. 864-870
    • Chiao, C.W.1    Tostes, R.C.2    Webb, R.C.3
  • 29
    • 2342650878 scopus 로고    scopus 로고
    • Analysis of host range phenotypes of primate hepadnaviruses by in vitro infections of hepatitis D virus pseudotypes
    • Barrera A, Guerra B, Lee H, Lanford RE (2004) Analysis of host range phenotypes of primate hepadnaviruses by in vitro infections of hepatitis D virus pseudotypes. J Virol 78: 5233-5243.
    • (2004) J Virol , vol.78 , pp. 5233-5243
    • Barrera, A.1    Guerra, B.2    Lee, H.3    Lanford, R.E.4
  • 30
    • 33947408707 scopus 로고    scopus 로고
    • Assembly of hepatitis delta virus: Particle characterization, including the ability to infect primary human hepatocytes
    • Gudima S, He Y, Meier A, Chang J, Chen R, et al. (2007) Assembly of hepatitis delta virus: particle characterization, including the ability to infect primary human hepatocytes. J Virol 81: 3608-3617.
    • (2007) J Virol , vol.81 , pp. 3608-3617
    • Gudima, S.1    He, Y.2    Meier, A.3    Chang, J.4    Chen, R.5
  • 31
    • 0037180522 scopus 로고    scopus 로고
    • Infection of a human hepatoma cell line by hepatitis B virus
    • Gripon P, Rumin S, Urban S, Le Seyec J, Glaise D, et al. (2002) Infection of a human hepatoma cell line by hepatitis B virus. Proc Natl Acad Sci USA 99: 15655-15660.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15655-15660
    • Gripon, P.1    Rumin, S.2    Urban, S.3    Le, S.J.4    Glaise, D.5
  • 33
    • 70350339068 scopus 로고    scopus 로고
    • Mammalian P2X7 receptor pharmacology: Comparison of recombinant mouse, rat and human P2X7 receptors
    • Donnelly-Roberts DL, Namovic MT, Han P, Jarvis MF (2009) Mammalian P2X7 receptor pharmacology: comparison of recombinant mouse, rat and human P2X7 receptors. Br J Pharmacol 157: 1203-1214.
    • (2009) Br J Pharmacol , vol.157 , pp. 1203-1214
    • Donnelly-Roberts, D.L.1    Namovic, M.T.2    Han, P.3    Jarvis, M.F.4
  • 34
    • 0037851027 scopus 로고    scopus 로고
    • P2X7 receptor-dependent blebbing and the activation of Rho-effector kinases, caspases, and IL-1 beta release
    • Verhoef PA, Estacion M, Schilling W, Dubyak GR (2003) P2X7 receptor-dependent blebbing and the activation of Rho-effector kinases, caspases, and IL-1 beta release. J Immunol 170: 5728-5738.
    • (2003) J Immunol , vol.170 , pp. 5728-5738
    • Verhoef, P.A.1    Estacion, M.2    Schilling, W.3    Dubyak, G.R.4
  • 35
    • 65449120034 scopus 로고    scopus 로고
    • Virus entry by macropinocytosis
    • Mercer J, Helenius A (2009) Virus entry by macropinocytosis. Nat Cell Biol 11: 510-520.
    • (2009) Nat Cell Biol , vol.11 , pp. 510-520
    • Mercer, J.1    Helenius, A.2
  • 38
    • 0042827962 scopus 로고    scopus 로고
    • P2X7 receptor activates extracellular signal-regulated kinases ERK1 and ERK2 independently of Ca2+ influx
    • Amstrup J, Novak I (2003) P2X7 receptor activates extracellular signal-regulated kinases ERK1 and ERK2 independently of Ca2+ influx. Biochem J 374: 51-61.
    • (2003) Biochem J , vol.374 , pp. 51-61
    • Amstrup, J.1    Novak, I.2
  • 39
    • 75449106643 scopus 로고    scopus 로고
    • Fine mapping of pre-S sequence requirements for hepatitis B virus large envelope protein-mediated receptor interaction
    • Schulze A, Schieck A, Ni Y, Mier W, Urban S (2009) Fine mapping of pre-S sequence requirements for hepatitis B virus large envelope protein-mediated receptor interaction. J Virol 84: 1989-2000.
    • (2009) J Virol , vol.84 , pp. 1989-2000
    • Schulze, A.1    Schieck, A.2    Ni, Y.3    Mier, W.4    Urban, S.5
  • 41
    • 39549091300 scopus 로고    scopus 로고
    • Characterization of ionotrophic purinergic receptors in hepatocytes
    • Emmett DS, Feranchak A, Kilic G, Puljak L, Miller B, et al. (2008) Characterization of ionotrophic purinergic receptors in hepatocytes. Hepatology 47: 698-705.
    • (2008) Hepatology , vol.47 , pp. 698-705
    • Emmett, D.S.1    Feranchak, A.2    Kilic, G.3    Puljak, L.4    Miller, B.5
  • 42
    • 0031052095 scopus 로고    scopus 로고
    • The permeabilizing ATP receptor, P2X7. Cloning and expression of a human cDNA
    • Rassendren F, Buell GN, Virginio C, Collo G, North RA, et al. (1997) The permeabilizing ATP receptor, P2X7. Cloning and expression of a human cDNA. J Biol Chem 272: 5482-5486.
    • (1997) J Biol Chem , vol.272 , pp. 5482-5486
    • Rassendren, F.1    Buell, G.N.2    Virginio, C.3    Collo, G.4    North, R.A.5
  • 44
    • 60449100436 scopus 로고    scopus 로고
    • Selective P2X(7) receptor antagonists for chronic inflammation and pain
    • Carroll WA, Donnelly-Roberts D, Jarvis MF (2009) Selective P2X(7) receptor antagonists for chronic inflammation and pain. Purinergic Signal 5: 63-73.
    • (2009) Purinergic Signal , vol.5 , pp. 63-73
    • Carroll, W.A.1    Donnelly-Roberts, D.2    Jarvis, M.F.3
  • 45
    • 13744257618 scopus 로고    scopus 로고
    • Efficient inhibition of hepatitis B virus infection by acylated peptides derived from the large viral surface protein
    • Gripon P, Cannie I, Urban S (2005) Efficient inhibition of hepatitis B virus infection by acylated peptides derived from the large viral surface protein. J Virol 79: 1613-1622.
    • (2005) J Virol , vol.79 , pp. 1613-1622
    • Gripon, P.1    Cannie, I.2    Urban, S.3
  • 46
    • 0019966544 scopus 로고
    • Growth of human hepatoma cell lines with differentiated functions in chemically defined medium
    • Nakabayashi H, Taketa K, Miyano K, Yamane T, Sato J (1982) Growth of human hepatoma cell lines with differentiated functions in chemically defined medium. Canc Res 42: 3858-3863.
    • (1982) Canc Res , vol.42 , pp. 3858-3863
    • Nakabayashi, H.1    Taketa, K.2    Miyano, K.3    Yamane, T.4    Sato, J.5
  • 47
    • 0030842540 scopus 로고    scopus 로고
    • Inducible expression of human hepatitis B virus (HBV) in stably transfected hepatoblas-toma cells: A novel system for screening potential inhibitors of HBV replication
    • Ladner SK, Otto MJ, Barker CS, Zaifert K, Wang GH, et al. (1997) Inducible expression of human hepatitis B virus (HBV) in stably transfected hepatoblas-toma cells: a novel system for screening potential inhibitors of HBV replication. Antimicrob Agents Chemother 41: 1715-1720.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 1715-1720
    • Ladner, S.K.1    Otto, M.J.2    Barker, C.S.3    Zaifert, K.4    Wang, G.H.5
  • 48
    • 33846538587 scopus 로고    scopus 로고
    • Viral and cellular determinants involved in hepadnaviral entry
    • Glebe D, Urban S (2007) Viral and cellular determinants involved in hepadnaviral entry. World J Gastroenterol 13: 22-38.
    • (2007) World J Gastroenterol , vol.13 , pp. 22-38
    • Glebe, D.1    Urban, S.2
  • 49
    • 0033848882 scopus 로고    scopus 로고
    • High-throughput quantitative analysis of hepatitis B virus DNA in serum using the TaqMan fluorogenic detection system
    • Loeb KR, Jerome KR, Goddard J, Huang M, Cent A, et al. (2000) High-throughput quantitative analysis of hepatitis B virus DNA in serum using the TaqMan fluorogenic detection system. Hepatology 32: 626-629.
    • (2000) Hepatology , vol.32 , pp. 626-629
    • Loeb, K.R.1    Jerome, K.R.2    Goddard, J.3    Huang, M.4    Cent, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.