메뉴 건너뛰기




Volumn 98, Issue 2, 2017, Pages 190-200

Feline coronavirus replication is affected by both cyclophilin A and cyclophilin B

Author keywords

Cyclophilin; Feline coronavirus; Feline infectious peritonitis; Peptidyl prolyl cis trans isomerase

Indexed keywords

CYCLOPHILIN A; CYCLOPHILIN B; PEPTIDYLPROLYL ISOMERASE; SHORT HAIRPIN RNA; VIRAL PROTEIN; CYCLOPHILIN; CYCLOSPORIN;

EID: 85015628901     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/jgv.0.000663     Document Type: Article
Times cited : (25)

References (27)
  • 1
    • 0141618496 scopus 로고    scopus 로고
    • Persistence and transmission of natural type I feline coronavirus infection
    • Addie DD, Schaap IA, Nicolson L, Jarrett O. Persistence and transmission of natural type I feline coronavirus infection. J Gen Virol 2003;84:2735-2744.
    • (2003) J Gen Virol , vol.84 , pp. 2735-2744
    • Addie, D.D.1    Schaap, I.A.2    Nicolson, L.3    Jarrett, O.4
  • 2
    • 67349158649 scopus 로고    scopus 로고
    • Coronaviruses post-SARS: Update on replication and pathogenesis
    • Perlman S, Netland J. Coronaviruses post-SARS: update on replication and pathogenesis. Nat Rev Microbiol 2009;7:439-450.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 439-450
    • Perlman, S.1    Netland, J.2
  • 3
    • 61749103803 scopus 로고    scopus 로고
    • A review of feline infectious peritonitis virus infection: 1963-2008
    • Pedersen NC. A review of feline infectious peritonitis virus infection: 1963-2008. J Feline Med Surg 2009;11:225-258.
    • (2009) J Feline Med Surg , vol.11 , pp. 225-258
    • Pedersen, N.C.1
  • 4
    • 0015470174 scopus 로고
    • Extraperitoneal lesions in feline infectious peritonitis
    • Montali RJ, Strandberg JD. Extraperitoneal lesions in feline infectious peritonitis. Vet Pathol 1972;9:109-121.
    • (1972) Vet Pathol , vol.9 , pp. 109-121
    • Montali, R.J.1    Strandberg, J.D.2
  • 5
    • 33745754923 scopus 로고    scopus 로고
    • Hosting the severe acute respiratory syndrome coronavirus: Specific cell factors required for infection
    • de Haan CA, Rottier PJ. Hosting the severe acute respiratory syndrome coronavirus: specific cell factors required for infection. Cell Microbiol 2006;8:1211-1218.
    • (2006) Cell Microbiol , vol.8 , pp. 1211-1218
    • De Haan, C.A.1    Rottier, P.J.2
  • 6
    • 78650357434 scopus 로고    scopus 로고
    • Identification of host factors involved in coronavirus replication by quantitative proteomics analysis
    • Vogels MW, van Balkom BW, Kaloyanova DV, Batenburg JJ, Heck AJ et al. Identification of host factors involved in coronavirus replication by quantitative proteomics analysis. Proteomics 2011;11: 64-80.
    • (2011) Proteomics , vol.11 , pp. 64-80
    • Vogels, M.W.1    Van Balkom, B.W.2    Kaloyanova, D.V.3    Batenburg, J.J.4    Heck, A.J.5
  • 7
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • Siekierka JJ, Hung SH, Poe M, Lin CS, Sigal NH. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin. Nature 1989; 341:755-757.
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekierka, J.J.1    Hung, S.H.2    Poe, M.3    Lin, C.S.4    Sigal, N.H.5
  • 8
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi N, Hayano T, Suzuki M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 1989;337:473-475.
    • (1989) Nature , vol.337 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 10
    • 80055081525 scopus 로고    scopus 로고
    • The SARS-coronavirus-host interactome: Identification of cyclophilins as target for pan-coronavirus inhibitors
    • Pfefferle S, Schöpf J, Kögl M, Friedel CC, Müller MA et al. The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors. PLoS Pathog 2011;7:e1002331.
    • (2011) Plos Pathog , vol.7
    • Pfefferle, S.1    Schöpf, J.2    Kögl, M.3    Friedel, C.C.4    Müller, M.A.5
  • 11
    • 84873029451 scopus 로고    scopus 로고
    • Suppression of feline coronavirus replication in vitro by cyclosporin A
    • Tanaka Y, Sato Y, Osawa S, Inoue M, Tanaka S et al. Suppression of feline coronavirus replication in vitro by cyclosporin A. Vet Res 2012;43:41.
    • (2012) Vet Res , vol.43 , pp. 41
    • Tanaka, Y.1    Sato, Y.2    Osawa, S.3    Inoue, M.4    Tanaka, S.5
  • 12
    • 84939182174 scopus 로고    scopus 로고
    • Genetic deficiency and polymorphisms of cyclophilin A reveal its essential role for human coronavirus 229E replication
    • von Brunn A, Ciesek S, von Brunn B, Carbajo-Lozoya J. Genetic deficiency and polymorphisms of cyclophilin A reveal its essential role for human coronavirus 229E replication. Curr Opin Virol 2015; 14:56-61.
    • (2015) Curr Opin Virol , vol.14 , pp. 56-61
    • Von Brunn, A.1    Ciesek, S.2    Von Brunn, B.3    Carbajo-Lozoya, J.4
  • 13
    • 84863421314 scopus 로고    scopus 로고
    • Replication of human coronaviruses SARS-CoV, HCoV-NL63 and HCoV-229E is inhibited by the drug FK506
    • Carbajo-Lozoya J, Müller MA, Kallies S, Thiel V, Drosten C et al. Replication of human coronaviruses SARS-CoV, HCoV-NL63 and HCoV-229E is inhibited by the drug FK506. Virus Res 2012;165: 112-117.
    • (2012) Virus Res , vol.165 , pp. 112-117
    • Carbajo-Lozoya, J.1    Müller, M.A.2    Kallies, S.3    Thiel, V.4    Drosten, C.5
  • 14
    • 84898619532 scopus 로고    scopus 로고
    • Human coronavirus NL63 replication is cyclophilin A-dependent and inhibited by non-immunosuppressive cyclosporine A-derivatives including Alisporivir
    • Carbajo-Lozoya J, Ma-Lauer Y, Maleševic´ M, Theuerkorn M, Kahlert V et al. Human coronavirus NL63 replication is cyclophilin A-dependent and inhibited by non-immunosuppressive cyclosporine A-derivatives including Alisporivir. Virus Res 2014;184:44-53.
    • (2014) Virus Res , vol.184 , pp. 44-53
    • Carbajo-Lozoya, J.1    Ma-Lauer, Y.2    Maleševic´, M.3    Theuerkorn, M.4    Kahlert, V.5
  • 16
    • 0027071803 scopus 로고
    • Active site mutants of human cyclophilin A separate peptidylprolyl isomerase activity from cyclosporin A binding and calcineurin inhibition
    • Zydowsky LD, Etzkorn FA, Chang HY, Ferguson SB, Stolz LA et al. Active site mutants of human cyclophilin A separate peptidylprolyl isomerase activity from cyclosporin A binding and calcineurin inhibition. Protein Sci 1992;1:1092-1099.
    • (1992) Protein Sci , vol.1 , pp. 1092-1099
    • Zydowsky, L.D.1    Etzkorn, F.A.2    Chang, H.Y.3    Ferguson, S.B.4    Stolz, L.A.5
  • 17
    • 0033574413 scopus 로고    scopus 로고
    • Two distinct regions of cyclophilin B are involved in the recognition of a functional receptor and of glycosaminoglycans on T lymphocytes
    • Carpentier M, Allain F, Haendler B, Denys A, Mariller C et al. Two distinct regions of cyclophilin B are involved in the recognition of a functional receptor and of glycosaminoglycans on T lymphocytes. J Biol Chem 1999;274:10990-10998.
    • (1999) J Biol Chem , vol.274 , pp. 10990-10998
    • Carpentier, M.1    Allain, F.2    Haendler, B.3    Denys, A.4    Mariller, C.5
  • 18
    • 84949569602 scopus 로고    scopus 로고
    • Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
    • Tanaka Y, Amano A, Morisaki M, Sato Y, Sasaki T. Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus. Antiviral Res 2016;126:1-7.
    • (2016) Antiviral Res , vol.126 , pp. 1-7
    • Tanaka, Y.1    Amano, A.2    Morisaki, M.3    Sato, Y.4    Sasaki, T.5
  • 19
    • 84940594846 scopus 로고    scopus 로고
    • The role of immunophilins in viral infection
    • Hopkins S, Gallay PA. The role of immunophilins in viral infection. Biochim Biophys Acta 2015;1850:2103-2110.
    • (2015) Biochim Biophys Acta , vol.1850 , pp. 2103-2110
    • Hopkins, S.1    Gallay, P.A.2
  • 20
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 1989;337:476-478.
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 21
    • 33750083654 scopus 로고    scopus 로고
    • Characterisation of the RNA binding properties of the coronavirus infectious bronchitis virus nucleocapsid protein amino-terminal region
    • Spencer KA, Hiscox JA. Characterisation of the RNA binding properties of the coronavirus infectious bronchitis virus nucleocapsid protein amino-terminal region. FEBS Lett 2006;580:5993-5998.
    • (2006) FEBS Lett , vol.580 , pp. 5993-5998
    • Spencer, K.A.1    Hiscox, J.A.2
  • 23
    • 75449101470 scopus 로고    scopus 로고
    • Coronavirus nucleocapsid protein facilitates template switching and is required for efficient transcription
    • Zúñiga S, Cruz JL, Sola I, Mateos-Gómez PA, Palacio L et al. Coronavirus nucleocapsid protein facilitates template switching and is required for efficient transcription. J Virol 2010;84:2169-2175.
    • (2010) J Virol , vol.84 , pp. 2169-2175
    • Zúñiga, S.1    Cruz, J.L.2    Sola, I.3    Mateos-Gómez, P.A.4    Palacio, L.5
  • 24
    • 84908060960 scopus 로고    scopus 로고
    • Nucleocapsid phosphorylation and RNA helicase DDX1 recruitment enables coronavirus transition from discontinuous to continuous transcription
    • Wu CH, Chen PJ, Yeh SH. Nucleocapsid phosphorylation and RNA helicase DDX1 recruitment enables coronavirus transition from discontinuous to continuous transcription. Cell Host Microbe 2014; 16:462-472.
    • (2014) Cell Host Microbe , vol.16 , pp. 462-472
    • Wu, C.H.1    Chen, P.J.2    Yeh, S.H.3
  • 25
    • 4344612246 scopus 로고    scopus 로고
    • Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A
    • Luo C, Luo H, Zheng S, Gui C, Yue L et al. Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A. Biochem Biophys Res Commun 2004;321:557-565.
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 557-565
    • Luo, C.1    Luo, H.2    Zheng, S.3    Gui, C.4    Yue, L.5
  • 27
    • 43949123575 scopus 로고    scopus 로고
    • Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro
    • Yang F, Robotham JM, Nelson HB, Irsigler A, Kenworthy R et al. Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro. J Virol 2008;82:5269-5278
    • (2008) J Virol , vol.82 , pp. 5269-5278
    • Yang, F.1    Robotham, J.M.2    Nelson, H.B.3    Irsigler, A.4    Kenworthy, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.