메뉴 건너뛰기




Volumn 87, Issue 6, 2013, Pages 3003-3017

The feline calicivirus leader of the capsid protein is associated with cytopathic effect

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; COMPLEMENTARY DNA; CYSTEINE; LEADER OF THE CAPSID PROTEIN; LIPOCORTIN 2; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 84874678172     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02480-12     Document Type: Article
Times cited : (27)

References (54)
  • 1
    • 77649187275 scopus 로고    scopus 로고
    • Visualization of feline calicivirus replication in real-time with recombinant viruses engineered to express fluorescent reporter proteins
    • Abente EJ, Sosnovtsev SV, Bok K, Green KY. 2010. Visualization of feline calicivirus replication in real-time with recombinant viruses engineered to express fluorescent reporter proteins. Virology 400:18-31.
    • (2010) Virology , vol.400 , pp. 18-31
    • Abente, E.J.1    Sosnovtsev, S.V.2    Bok, K.3    Green, K.Y.4
  • 2
    • 16544395296 scopus 로고    scopus 로고
    • Mutagenesis of tyrosine 24 in the VPg protein is lethal for feline calicivirus
    • Mitra T, Sosnovtsev SV, Green KY. 2004. Mutagenesis of tyrosine 24 in the VPg protein is lethal for feline calicivirus. J. Virol. 78:4931-4935.
    • (2004) J. Virol. , vol.78 , pp. 4931-4935
    • Mitra, T.1    Sosnovtsev, S.V.2    Green, K.Y.3
  • 3
    • 0029134714 scopus 로고
    • RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity
    • Sosnovtsev S, Green KY. 1995. RNA transcripts derived from a cloned full-length copy of the feline calicivirus genome do not require VpG for infectivity. Virology 210:383-390.
    • (1995) Virology , vol.210 , pp. 383-390
    • Sosnovtsev, S.1    Green, K.Y.2
  • 4
    • 15244340443 scopus 로고    scopus 로고
    • Feline calicivirus VP2 is essential for the production of infectious virions
    • Sosnovtsev SV, Belliot G, Chang KO, Onwudiwe O, Green KY. 2005. Feline calicivirus VP2 is essential for the production of infectious virions. J. Virol. 79:4012-4024.
    • (2005) J. Virol. , vol.79 , pp. 4012-4024
    • Sosnovtsev, S.V.1    Belliot, G.2    Chang, K.O.3    Onwudiwe, O.4    Green, K.Y.5
  • 5
    • 0031900656 scopus 로고    scopus 로고
    • Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase
    • Sosnovtsev SV, Sosnovtseva SA, Green KY. 1998. Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase. J. Virol. 72:3051-3059.
    • (1998) J. Virol. , vol.72 , pp. 3051-3059
    • Sosnovtsev, S.V.1    Sosnovtseva, S.A.2    Green, K.Y.3
  • 7
    • 0030922351 scopus 로고    scopus 로고
    • Identification of a protein linked to the genomic and subgenomic mRNAs of feline calicivirus and its role in translation
    • Herbert TP, Brierley I, Brown TD. 1997. Identification of a protein linked to the genomic and subgenomic mRNAs of feline calicivirus and its role in translation. J. Gen. Virol. 78:1033-1040.
    • (1997) J. Gen. Virol. , vol.78 , pp. 1033-1040
    • Herbert, T.P.1    Brierley, I.2    Brown, T.D.3
  • 8
    • 0024061391 scopus 로고
    • Further characterization of the virusspecific RNAs in feline calicivirus infected cells
    • Neill JD, Mengeling WL. 1988. Further characterization of the virusspecific RNAs in feline calicivirus infected cells. Virus Res. 11:59-72.
    • (1988) Virus Res. , vol.11 , pp. 59-72
    • Neill, J.D.1    Mengeling, W.L.2
  • 10
    • 33744494819 scopus 로고    scopus 로고
    • X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity
    • Chen R, Neill JD, Estes MK, Prasad BV. 2006. X-ray structure of a native calicivirus: structural insights into antigenic diversity and host specificity. Proc. Natl. Acad. Sci. U. S. A. 103:8048-8053.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8048-8053
    • Chen, R.1    Neill, J.D.2    Estes, M.K.3    Prasad, B.V.4
  • 11
    • 0037292503 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of San Miguel sea lion virus: an animal calicivirus
    • Chen R, Neill JD, Prasad BV. 2003. Crystallization and preliminary crystallographic analysis of San Miguel sea lion virus: an animal calicivirus. J. Struct. Biol. 141:143-148.
    • (2003) J. Struct. Biol. , vol.141 , pp. 143-148
    • Chen, R.1    Neill, J.D.2    Prasad, B.V.3
  • 12
    • 0014900188 scopus 로고
    • Feline picornavirus: structure of the virus and electron microscopic observations on infected cell cultures
    • Peterson JE, Studdert MJ. 1970. Feline picornavirus: structure of the virus and electron microscopic observations on infected cell cultures. Arch. Gesamte Virusforsch. 32:249-260.
    • (1970) Arch. Gesamte Virusforsch. , vol.32 , pp. 249-260
    • Peterson, J.E.1    Studdert, M.J.2
  • 14
    • 0028136813 scopus 로고
    • Three-dimensional structure of calicivirus
    • Prasad BV, Matson DO, Smith AW. 1994. Three-dimensional structure of calicivirus. J. Mol. Biol. 240:256-264.
    • (1994) J. Mol. Biol. , vol.240 , pp. 256-264
    • Prasad, B.V.1    Matson, D.O.2    Smith, A.W.3
  • 15
    • 0034634331 scopus 로고    scopus 로고
    • Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions
    • Sosnovtsev SV, Green KY. 2000. Identification and genomic mapping of the ORF3 and VPg proteins in feline calicivirus virions. Virology 277:193-203.
    • (2000) Virology , vol.277 , pp. 193-203
    • Sosnovtsev, S.V.1    Green, K.Y.2
  • 16
    • 0036635341 scopus 로고    scopus 로고
    • Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome
    • Sosnovtsev SV, Garfield M, Green KY. 2002. Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome. J. Virol. 76:7060-7072.
    • (2002) J. Virol. , vol.76 , pp. 7060-7072
    • Sosnovtsev, S.V.1    Garfield, M.2    Green, K.Y.3
  • 17
    • 0032798396 scopus 로고    scopus 로고
    • Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinasepolymerase precursor protein
    • Sosnovtseva SA, Sosnovtsev SV, Green KY. 1999. Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinasepolymerase precursor protein. J. Virol. 73:6626-6633.
    • (1999) J. Virol. , vol.73 , pp. 6626-6633
    • Sosnovtseva, S.A.1    Sosnovtsev, S.V.2    Green, K.Y.3
  • 18
    • 0025946771 scopus 로고
    • Nucleotide sequence and expression of the capsid protein gene of feline calicivirus
    • Neill JD, Reardon IM, Heinrikson RL. 1991. Nucleotide sequence and expression of the capsid protein gene of feline calicivirus. J. Virol. 65: 5440-5447.
    • (1991) J. Virol. , vol.65 , pp. 5440-5447
    • Neill, J.D.1    Reardon, I.M.2    Heinrikson, R.L.3
  • 20
    • 0018183602 scopus 로고
    • Calicivirus proteins in infected cells: evidence for a capsid polypeptide precursor
    • Fretz M, Schaffer FL. 1978. Calicivirus proteins in infected cells: evidence for a capsid polypeptide precursor. Virology 89:318-321.
    • (1978) Virology , vol.89 , pp. 318-321
    • Fretz, M.1    Schaffer, F.L.2
  • 21
    • 0024819707 scopus 로고
    • Feline calicivirus protein synthesis investigated by Western blotting
    • Carter MJ. 1989. Feline calicivirus protein synthesis investigated by Western blotting. Arch. Virol. 108:69-79.
    • (1989) Arch. Virol. , vol.108 , pp. 69-79
    • Carter, M.J.1
  • 22
    • 0033193667 scopus 로고    scopus 로고
    • Analysis of the N-terminal polypeptide of the capsid precursor protein and the ORF3 product of feline calicivirus
    • Tohya Y, Shinchi H, Matsuura Y, Maeda K, Ishiguro S, Mochizuki M, Sugimura T. 1999. Analysis of the N-terminal polypeptide of the capsid precursor protein and the ORF3 product of feline calicivirus. J. Vet. Med. Sci. 61:1043-1047.
    • (1999) J. Vet. Med. Sci. , vol.61 , pp. 1043-1047
    • Tohya, Y.1    Shinchi, H.2    Matsuura, Y.3    Maeda, K.4    Ishiguro, S.5    Mochizuki, M.6    Sugimura, T.7
  • 23
    • 52649107667 scopus 로고    scopus 로고
    • Leader of the capsid protein in feline calicivirus promotes replication of Norwalk virus in cell culture
    • Chang KO, George DW, Patton JB, Green KY, Sosnovtsev SV. 2008. Leader of the capsid protein in feline calicivirus promotes replication of Norwalk virus in cell culture. J. Virol. 82:9306-9317.
    • (2008) J. Virol. , vol.82 , pp. 9306-9317
    • Chang, K.O.1    George, D.W.2    Patton, J.B.3    Green, K.Y.4    Sosnovtsev, S.V.5
  • 24
    • 69249208740 scopus 로고    scopus 로고
    • Role of cholesterol pathways in norovirus replication
    • Chang KO. 2009. Role of cholesterol pathways in norovirus replication. J. Virol. 83:8587-8595.
    • (2009) J. Virol. , vol.83 , pp. 8587-8595
    • Chang, K.O.1
  • 26
    • 0034040949 scopus 로고    scopus 로고
    • Norwalk-like virus infection in military forces: epidemic potential, sporadic disease, and the future direction of prevention and control efforts
    • McCarthy M, Estes MK, Hyams KC. 2000. Norwalk-like virus infection in military forces: epidemic potential, sporadic disease, and the future direction of prevention and control efforts. J. Infect. Dis. 181(Suppl 2): S387-S391.
    • (2000) J. Infect. Dis. , vol.181 , Issue.SUPPL 2
    • McCarthy, M.1    Estes, M.K.2    Hyams, K.C.3
  • 28
    • 0031736983 scopus 로고    scopus 로고
    • Molecular epidemiology of -Norwalk-like viruses- in outbreaks of gastroenteritis in the United States
    • Fankhauser RL, Noel JS, Monroe SS, Ando T, Glass RI. 1998. Molecular epidemiology of -Norwalk-like viruses- in outbreaks of gastroenteritis in the United States. J. Infect. Dis. 178:1571-1578.
    • (1998) J. Infect. Dis. , vol.178 , pp. 1571-1578
    • Fankhauser, R.L.1    Noel, J.S.2    Monroe, S.S.3    Ando, T.4    Glass, R.I.5
  • 29
    • 84860996781 scopus 로고    scopus 로고
    • Multiple antigenic sites are involved in blocking the interaction of GII.4 norovirus capsid with ABH histo-blood group antigens
    • Parra GI, Abente EJ, Sandoval-Jaime C, Sosnovtsev SV, Bok K, Green KY. 2012. Multiple antigenic sites are involved in blocking the interaction of GII.4 norovirus capsid with ABH histo-blood group antigens. J. Virol. 86:7414-7426.
    • (2012) J. Virol. , vol.86 , pp. 7414-7426
    • Parra, G.I.1    Abente, E.J.2    Sandoval-Jaime, C.3    Sosnovtsev, S.V.4    Bok, K.5    Green, K.Y.6
  • 30
  • 33
    • 15244359032 scopus 로고    scopus 로고
    • Recovery of feline calicivirus from plasmid DNA containing a full-length copy of the genome
    • European Society for Veterinary Virology and Central Veterinary Laboratory, Reading, United Kingdom
    • Sosnovtsev SV, Sosnovtseva S, Green KY. 1996. Recovery of feline calicivirus from plasmid DNA containing a full-length copy of the genome, p 125-130. In Chasey D, Gaskell RM, Clarke IN (ed), The 1st international symposium on caliciviruses. European Society for Veterinary Virology and Central Veterinary Laboratory, Reading, United Kingdom.
    • (1996) In Chasey D, Gaskell RM, Clarke IN (ed), The 1st international symposium on caliciviruses , pp. 125-130
    • Sosnovtsev, S.V.1    Sosnovtseva, S.2    Green, K.Y.3
  • 34
    • 31644450519 scopus 로고    scopus 로고
    • The mitochondrial pathway of apoptosis is triggered during feline calicivirus infection
    • Natoni A, Kass GE, Carter MJ, Roberts LO. 2006. The mitochondrial pathway of apoptosis is triggered during feline calicivirus infection. J. Gen. Virol. 87:357-361.
    • (2006) J. Gen. Virol. , vol.87 , pp. 357-361
    • Natoni, A.1    Kass, G.E.2    Carter, M.J.3    Roberts, L.O.4
  • 36
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: from structure to function
    • Gerke V, Moss SE. 2002. Annexins: from structure to function. Physiol. Rev. 82:331-371.
    • (2002) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 37
    • 48049120845 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of annexin A2 regulates Rho-mediated actin rearrangement and cell adhesion
    • Rescher U, Ludwig C, Konietzko V, Kharitonenkov A, Gerke V. 2008. Tyrosine phosphorylation of annexin A2 regulates Rho-mediated actin rearrangement and cell adhesion. J. Cell Sci. 121:2177-2185.
    • (2008) J. Cell Sci. , vol.121 , pp. 2177-2185
    • Rescher, U.1    Ludwig, C.2    Konietzko, V.3    Kharitonenkov, A.4    Gerke, V.5
  • 38
    • 59449109685 scopus 로고    scopus 로고
    • Annexin A2 binding to endosomes and functions in endosomal transport are regulated by tyrosine 23 phosphorylation
    • Morel E, Gruenberg J. 2009. Annexin A2 binding to endosomes and functions in endosomal transport are regulated by tyrosine 23 phosphorylation. J. Biol. Chem. 284:1604-1611.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1604-1611
    • Morel, E.1    Gruenberg, J.2
  • 39
    • 0036065127 scopus 로고    scopus 로고
    • The subgenomic RNA of feline calicivirus is packaged into viral particles during infection
    • Neill JD. 2002. The subgenomic RNA of feline calicivirus is packaged into viral particles during infection. Virus Res. 87:89-93.
    • (2002) Virus Res. , vol.87 , pp. 89-93
    • Neill, J.D.1
  • 40
    • 43349101238 scopus 로고    scopus 로고
    • Bioinformatic and functional analysis of RNA secondary structure elements among different genera of human and animal caliciviruses
    • Simmonds P, Karakasiliotis I, Bailey D, Chaudhry Y, Evans DJ, Goodfellow IG. 2008. Bioinformatic and functional analysis of RNA secondary structure elements among different genera of human and animal caliciviruses. Nucleic Acids Res. 36:2530-2546.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2530-2546
    • Simmonds, P.1    Karakasiliotis, I.2    Bailey, D.3    Chaudhry, Y.4    Evans, D.J.5    Goodfellow, I.G.6
  • 41
    • 2342435180 scopus 로고    scopus 로고
    • Synthesis in vitro of rabbit hemorrhagic disease virus subgenomic RNA by internal initiation on (G)sense genomic RNA: mapping of a subgenomic promoter
    • Morales M, Barcena J, Ramirez MA, Boga JA, Parra F, Torres JM. 2004. Synthesis in vitro of rabbit hemorrhagic disease virus subgenomic RNA by internal initiation on (G)sense genomic RNA: mapping of a subgenomic promoter. J. Biol. Chem. 279:17013-17018.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17013-17018
    • Morales, M.1    Barcena, J.2    Ramirez, M.A.3    Boga, J.A.4    Parra, F.5    Torres, J.M.6
  • 42
    • 0030068269 scopus 로고    scopus 로고
    • Translation of Sindbis virus mRNA: analysis of sequences downstream of the initiating AUG codon that enhance translation
    • Frolov I, Schlesinger S. 1996. Translation of Sindbis virus mRNA: analysis of sequences downstream of the initiating AUG codon that enhance translation. J. Virol. 70:1182-1190.
    • (1996) J. Virol. , vol.70 , pp. 1182-1190
    • Frolov, I.1    Schlesinger, S.2
  • 43
    • 0028171032 scopus 로고
    • Translation of Sindbis virus mRNA: effects of sequences downstream of the initiating codon
    • Frolov I, Schlesinger S. 1994. Translation of Sindbis virus mRNA: effects of sequences downstream of the initiating codon. J. Virol. 68:8111-8117.
    • (1994) J. Virol. , vol.68 , pp. 8111-8117
    • Frolov, I.1    Schlesinger, S.2
  • 45
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay BK, Williamson MP, Sudol M. 2000. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14:231-241.
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 48
    • 84858312078 scopus 로고    scopus 로고
    • Annexin A2 at the interface of actin and membrane dynamics: a focus on its roles in endocytosis and cell polarization
    • doi:10.1155/2012/852430
    • Grieve AG, Moss SE, Hayes MJ. 2012. Annexin A2 at the interface of actin and membrane dynamics: a focus on its roles in endocytosis and cell polarization. Int. J. Cell Biol. 2012:852430. doi:10.1155/2012/852430.
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 852430
    • Grieve, A.G.1    Moss, S.E.2    Hayes, M.J.3
  • 50
    • 50149114689 scopus 로고    scopus 로고
    • Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A
    • Lai CK, Jeng KS, Machida K, Lai MM. 2008. Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A. J. Virol. 82:8838-8848.
    • (2008) J. Virol. , vol.82 , pp. 8838-8848
    • Lai, C.K.1    Jeng, K.S.2    Machida, K.3    Lai, M.M.4
  • 51
    • 84861388566 scopus 로고    scopus 로고
    • Annexin A2 is involved in the formation of hepatitis C virus replication complex on the lipid raft
    • Saxena V, Lai CK, Chao TC, Jeng KS, Lai MM. 2012. Annexin A2 is involved in the formation of hepatitis C virus replication complex on the lipid raft. J. Virol. 86:4139-4150.
    • (2012) J. Virol. , vol.86 , pp. 4139-4150
    • Saxena, V.1    Lai, C.K.2    Chao, T.C.3    Jeng, K.S.4    Lai, M.M.5
  • 53
    • 77956799975 scopus 로고    scopus 로고
    • Annexin 2 is not required for human immunodeficiency virus type 1 particle production but plays a cell typedependent role in regulating infectivity
    • Rai T, Mosoian A, Resh MD. 2010. Annexin 2 is not required for human immunodeficiency virus type 1 particle production but plays a cell typedependent role in regulating infectivity. J. Virol. 84:9783-9792.
    • (2010) J. Virol. , vol.84 , pp. 9783-9792
    • Rai, T.1    Mosoian, A.2    Resh, M.D.3
  • 54
    • 33644768131 scopus 로고    scopus 로고
    • Annexin 2: a novel human immunodeficiency virus type 1 Gag binding protein involved in replication in monocyte-derived macrophages
    • Ryzhova EV, Vos RM, Albright AV, Harrist AV, Harvey T, Gonzalez- Scarano F. 2006. Annexin 2: a novel human immunodeficiency virus type 1 Gag binding protein involved in replication in monocyte-derived macrophages. J. Virol. 80:2694-2704.
    • (2006) J. Virol. , vol.80 , pp. 2694-2704
    • Ryzhova, E.V.1    Vos, R.M.2    Albright, A.V.3    Harrist, A.V.4    Harvey, T.5    Gonzalez-Scarano, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.