메뉴 건너뛰기




Volumn 187, Issue 2, 2013, Pages 406-412

Efficient production of foot-and-mouth disease virus empty capsids in insect cells following down regulation of 3C protease activity

Author keywords

3C protease; Empty capsids; Foot and mouth disease virus; Frameshift; Protein processing; Recombinant baculovirus; Vaccine

Indexed keywords

3C PROTEASE; CELL PROTEIN; PROTEIN VP0; PROTEIN VP1; PROTEIN VP3; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84872681669     PISSN: 01660934     EISSN: 18790984     Source Type: Journal    
DOI: 10.1016/j.jviromet.2012.11.011     Document Type: Article
Times cited : (46)

References (45)
  • 1
    • 0029582760 scopus 로고
    • Assembly of foot-and-mouth disease virus empty capsids synthesized by a vaccinia virus expression system
    • Abrams C.C., King A.M., Belsham G.J. Assembly of foot-and-mouth disease virus empty capsids synthesized by a vaccinia virus expression system. J. Gen. Virol. 1995, 76:3089-3098.
    • (1995) J. Gen. Virol. , vol.76 , pp. 3089-3098
    • Abrams, C.C.1    King, A.M.2    Belsham, G.J.3
  • 2
    • 0345269268 scopus 로고    scopus 로고
    • Control of human immunodeficiency virus type-1 protease activity in insect cells expressing gag-pol rescues assembly of immature but not mature virus-like particles
    • Adamson C.S., Nermut M., Jones I.M. Control of human immunodeficiency virus type-1 protease activity in insect cells expressing gag-pol rescues assembly of immature but not mature virus-like particles. Virology 2003, 308:157-165.
    • (2003) Virology , vol.308 , pp. 157-165
    • Adamson, C.S.1    Nermut, M.2    Jones, I.M.3
  • 3
    • 10644274416 scopus 로고    scopus 로고
    • Translation and replication of FMDV RNA
    • Belsham G.J. Translation and replication of FMDV RNA. Curr. Top. Microbiol. Immunol. 2005, 288:43-70.
    • (2005) Curr. Top. Microbiol. Immunol. , vol.288 , pp. 43-70
    • Belsham, G.J.1
  • 5
    • 0027185673 scopus 로고
    • Formation of poliovirus-like particles by recombinant baculoviruses expressing the individual VP0, VP3, and VP1 proteins by comparison to particles derived from the expressed poliovirus polyprotein
    • Brautigam S., Snezhkov E., Bishop D.H. Formation of poliovirus-like particles by recombinant baculoviruses expressing the individual VP0, VP3, and VP1 proteins by comparison to particles derived from the expressed poliovirus polyprotein. Virology 1993, 192:512-524.
    • (1993) Virology , vol.192 , pp. 512-524
    • Brautigam, S.1    Snezhkov, E.2    Bishop, D.H.3
  • 6
    • 65449181209 scopus 로고    scopus 로고
    • Synthesis of empty capsid-like particles of asia i foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs
    • Cao Y., Lu Z., Sun J., Bai X., Sun P., Bao H., Chen Y., Guo J., Li D., Liu X., Liu Z. Synthesis of empty capsid-like particles of asia i foot-and-mouth disease virus in insect cells and their immunogenicity in guinea pigs. Vet. Microbiol. 2009, 137:10-17.
    • (2009) Vet. Microbiol. , vol.137 , pp. 10-17
    • Cao, Y.1    Lu, Z.2    Sun, J.3    Bai, X.4    Sun, P.5    Bao, H.6    Chen, Y.7    Guo, J.8    Li, D.9    Liu, X.10    Liu, Z.11
  • 7
    • 77955716399 scopus 로고    scopus 로고
    • Formation of virus-like particles from O-type foot-and-mouth disease virus in insect cells using codon-optimized synthetic genes
    • Cao Y., Sun P., Fu Y., Bai X., Tian F., Liu X., Lu Z., Liu Z. Formation of virus-like particles from O-type foot-and-mouth disease virus in insect cells using codon-optimized synthetic genes. Biotechnol. Lett. 2010, 32:1223-1229.
    • (2010) Biotechnol. Lett. , vol.32 , pp. 1223-1229
    • Cao, Y.1    Sun, P.2    Fu, Y.3    Bai, X.4    Tian, F.5    Liu, X.6    Lu, Z.7    Liu, Z.8
  • 11
    • 84855906967 scopus 로고    scopus 로고
    • Control of gene expression by translational recoding
    • Dinman J.D. Control of gene expression by translational recoding. Adv. Protein Chem. Struct. Biol. 2012, 86:129-149.
    • (2012) Adv. Protein Chem. Struct. Biol. , vol.86 , pp. 129-149
    • Dinman, J.D.1
  • 12
    • 0035015174 scopus 로고    scopus 로고
    • Analysis of the aphthovirus 2a/2b polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: a putative ribosomal 'skip'
    • Donnelly M.L., Luke G., Mehrotra A., Li X., Hughes L.E., Gani D., Ryan M.D. Analysis of the aphthovirus 2a/2b polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: a putative ribosomal 'skip'. J. Gen. Virol. 2001, 82:1013-1025.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1013-1025
    • Donnelly, M.L.1    Luke, G.2    Mehrotra, A.3    Li, X.4    Hughes, L.E.5    Gani, D.6    Ryan, M.D.7
  • 13
    • 67651152725 scopus 로고    scopus 로고
    • The campoletis sonorensis ichnovirus vankyrin protein p-vank-1 inhibits apoptosis in insect Sf9 cells
    • Fath-Goodin A., Kroemer J.A., Webb B.A. The campoletis sonorensis ichnovirus vankyrin protein p-vank-1 inhibits apoptosis in insect Sf9 cells. Insect Mol. Biol. 2009, 18:497-506.
    • (2009) Insect Mol. Biol. , vol.18 , pp. 497-506
    • Fath-Goodin, A.1    Kroemer, J.A.2    Webb, B.A.3
  • 15
    • 77954146431 scopus 로고    scopus 로고
    • Ao38, a new cell line from eggs of the black witch moth, ascalapha odorata (lepidoptera: Noctuidae), is permissive for AcMNPV infection and produces high levels of recombinant proteins
    • Hashimoto Y., Zhang S., Blissard G.W. Ao38, a new cell line from eggs of the black witch moth, ascalapha odorata (lepidoptera: Noctuidae), is permissive for AcMNPV infection and produces high levels of recombinant proteins. BMC Biotechnol. 2010, 10:50.
    • (2010) BMC Biotechnol. , vol.10 , pp. 50
    • Hashimoto, Y.1    Zhang, S.2    Blissard, G.W.3
  • 16
    • 84859928855 scopus 로고    scopus 로고
    • Correction: Bti-tnao38, a new cell line derived from trichoplusia ni, is permissive for AcMNPV infection and produces high levels of recombinant proteins
    • Hashimoto Y., Zhang S., Chen Y.R., Blissard G.W. Correction: Bti-tnao38, a new cell line derived from trichoplusia ni, is permissive for AcMNPV infection and produces high levels of recombinant proteins. BMC Biotechnol. 2012, 12:12.
    • (2012) BMC Biotechnol. , vol.12 , pp. 12
    • Hashimoto, Y.1    Zhang, S.2    Chen, Y.R.3    Blissard, G.W.4
  • 18
    • 0025789925 scopus 로고
    • Expression, processing, and assembly of foot-and-mouth disease virus capsid structures in heterologous systems: induction of a neutralizing antibody response in guinea pigs
    • Lewis S.A., Morgan D.O., Grubman M.J. Expression, processing, and assembly of foot-and-mouth disease virus capsid structures in heterologous systems: induction of a neutralizing antibody response in guinea pigs. J. Virol. 1991, 65:6572-6580.
    • (1991) J. Virol. , vol.65 , pp. 6572-6580
    • Lewis, S.A.1    Morgan, D.O.2    Grubman, M.J.3
  • 19
    • 0035913956 scopus 로고    scopus 로고
    • Cleavage of translation initiation factor 4ai (eif4ai) but not eif4aii by foot-and-mouth disease virus 3C protease: identification of the eif4ai cleavage site
    • Li W., Ross-Smith N., Proud C.G., Belsham G.J. Cleavage of translation initiation factor 4ai (eif4ai) but not eif4aii by foot-and-mouth disease virus 3C protease: identification of the eif4ai cleavage site. FEBS Lett. 2001, 507:1-5.
    • (2001) FEBS Lett. , vol.507 , pp. 1-5
    • Li, W.1    Ross-Smith, N.2    Proud, C.G.3    Belsham, G.J.4
  • 20
    • 84862154186 scopus 로고    scopus 로고
    • Evaluation of the solid phase competition elisa for detecting antibodies against the six foot-and-mouth disease virus non-O serotypes
    • Li Y., Swabey K.G., Gibson D., Keel P.J., Hamblin P., Wilsden G., Corteyn M., Ferris N.P. Evaluation of the solid phase competition elisa for detecting antibodies against the six foot-and-mouth disease virus non-O serotypes. J. Virol. Methods 2012, 183:125-131.
    • (2012) J. Virol. Methods , vol.183 , pp. 125-131
    • Li, Y.1    Swabey, K.G.2    Gibson, D.3    Keel, P.J.4    Hamblin, P.5    Wilsden, G.6    Corteyn, M.7    Ferris, N.P.8
  • 21
    • 48349103233 scopus 로고    scopus 로고
    • Expression of foot-and-mouth disease virus capsid proteins in silkworm-baculovirus expression system and its utilization as a subunit vaccine
    • Li Z., Yi Y., Yin X., Zhang Z., Liu J. Expression of foot-and-mouth disease virus capsid proteins in silkworm-baculovirus expression system and its utilization as a subunit vaccine. PloS ONE 2008, 3:e2273.
    • (2008) PloS ONE , vol.3
    • Li, Z.1    Yi, Y.2    Yin, X.3    Zhang, Z.4    Liu, J.5
  • 22
    • 79952083641 scopus 로고    scopus 로고
    • FMD subunit vaccine produced using a silkworm-baculovirus expression system: protective efficacy against two type asia1 isolates in cattle
    • Li Z., Yin X., Yi Y., Li X., Li B., Lan X., Zhang Z., Liu J. FMD subunit vaccine produced using a silkworm-baculovirus expression system: protective efficacy against two type asia1 isolates in cattle. Vet. Microbiol. 2011, 149:99-103.
    • (2011) Vet. Microbiol. , vol.149 , pp. 99-103
    • Li, Z.1    Yin, X.2    Yi, Y.3    Li, X.4    Li, B.5    Lan, X.6    Zhang, Z.7    Liu, J.8
  • 24
    • 80054000375 scopus 로고    scopus 로고
    • Enterovirus 71 and coxsackievirus a16 3c proteases: binding to rupintrivir and their substrates and anti-hand, foot, and mouth disease virus drug design
    • Lu G., Qi J., Chen Z., Xu X., Gao F., Lin D., Qian W., Liu H., Jiang H., Yan J., Gao G.F. Enterovirus 71 and coxsackievirus a16 3c proteases: binding to rupintrivir and their substrates and anti-hand, foot, and mouth disease virus drug design. J. Virol. 2011, 85:10319-10331.
    • (2011) J. Virol. , vol.85 , pp. 10319-10331
    • Lu, G.1    Qi, J.2    Chen, Z.3    Xu, X.4    Gao, F.5    Lin, D.6    Qian, W.7    Liu, H.8    Jiang, H.9    Yan, J.10    Gao, G.F.11
  • 27
    • 0028873693 scopus 로고
    • Strong buffering capacity of insect cells. Implications for the baculovirus expression system
    • Medina M., Lopez-Rivas A., Zuidema D., Belsham G.J., Domingo E., Vlak J.M. Strong buffering capacity of insect cells. Implications for the baculovirus expression system. Cytotechnology 1995, 17:21-26.
    • (1995) Cytotechnology , vol.17 , pp. 21-26
    • Medina, M.1    Lopez-Rivas, A.2    Zuidema, D.3    Belsham, G.J.4    Domingo, E.5    Vlak, J.M.6
  • 29
    • 34247401333 scopus 로고    scopus 로고
    • Characterization of recombinant foot-and-mouth disease virus pentamer-like structures expressed by baculovirus and their use as diagnostic antigens in a blocking ELISA
    • Oem J.K., Park J.H., Lee K.N., Kim Y.J., Kye S.J., Park J.Y., Song H.J. Characterization of recombinant foot-and-mouth disease virus pentamer-like structures expressed by baculovirus and their use as diagnostic antigens in a blocking ELISA. Vaccine 2007, 25:4112-4121.
    • (2007) Vaccine , vol.25 , pp. 4112-4121
    • Oem, J.K.1    Park, J.H.2    Lee, K.N.3    Kim, Y.J.4    Kye, S.J.5    Park, J.Y.6    Song, H.J.7
  • 30
    • 37049034482 scopus 로고    scopus 로고
    • Foliar extracts from transgenic tomato plants expressing the structural polyprotein, p1-2a, and protease, 3C, from foot-and-mouth disease virus elicit a protective response in guinea pigs
    • Pan L., Zhang Y., Wang Y., Wang B., Wang W., Fang Y., Jiang S., Lv J., Sun Y., Xie Q. Foliar extracts from transgenic tomato plants expressing the structural polyprotein, p1-2a, and protease, 3C, from foot-and-mouth disease virus elicit a protective response in guinea pigs. Vet. Immunol. Immunopathol. 2008, 121:83-90.
    • (2008) Vet. Immunol. Immunopathol. , vol.121 , pp. 83-90
    • Pan, L.1    Zhang, Y.2    Wang, Y.3    Wang, B.4    Wang, W.5    Fang, Y.6    Jiang, S.7    Lv, J.8    Sun, Y.9    Xie, Q.10
  • 32
    • 84872677168 scopus 로고    scopus 로고
    • Method for producing non-infectious recombinant picornavirus particles
    • US Patent 6,440,718 B1.
    • Probst, C., 2002. Method for producing non-infectious recombinant picornavirus particles. United Stated Patent Office, US Patent 6,440,718 B1.
    • (2002) United Stated Patent Office
    • Probst, C.1
  • 33
    • 77954458311 scopus 로고    scopus 로고
    • Foot and mouth disease virus vaccines
    • Rodriguez L.L., Grubman M.J. Foot and mouth disease virus vaccines. Vaccine 2009, 27(Suppl. 4):90-94.
    • (2009) Vaccine , vol.27 , Issue.SUPPL. 4 , pp. 90-94
    • Rodriguez, L.L.1    Grubman, M.J.2
  • 34
    • 34249899152 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus infection induces proteolytic cleavage of PTB, eIF3a,b, and PABP RNA-binding proteins
    • Rodriguez Pulido M., Serrano P., Saiz M., Martinez-Salas E. Foot-and-mouth disease virus infection induces proteolytic cleavage of PTB, eIF3a,b, and PABP RNA-binding proteins. Virology 2007, 364:466-474.
    • (2007) Virology , vol.364 , pp. 466-474
    • Rodriguez Pulido, M.1    Serrano, P.2    Saiz, M.3    Martinez-Salas, E.4
  • 35
    • 0025101935 scopus 로고
    • Synthesis of foot-and-mouth disease virus capsid proteins in insect cells using baculovirus expression vectors
    • Roosien J., Belsham G.J., Ryan M.D., King A.M., Vlak J.M. Synthesis of foot-and-mouth disease virus capsid proteins in insect cells using baculovirus expression vectors. J. Gen. Virol. 1990, 71:1703-1711.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1703-1711
    • Roosien, J.1    Belsham, G.J.2    Ryan, M.D.3    King, A.M.4    Vlak, J.M.5
  • 36
    • 0027299276 scopus 로고
    • Synthesis of immunogenic hepatitis a virus particles by recombinant baculoviruses
    • Rosen E., Stapleton J.T., McLinden J. Synthesis of immunogenic hepatitis a virus particles by recombinant baculoviruses. Vaccine 1993, 11:706-712.
    • (1993) Vaccine , vol.11 , pp. 706-712
    • Rosen, E.1    Stapleton, J.T.2    McLinden, J.3
  • 37
    • 0016611424 scopus 로고
    • A comparative chemical and serological study of the full and empty particles of foot-and mouth disease virus
    • Rowlands D.J., Sangar D.V., Brown F. A comparative chemical and serological study of the full and empty particles of foot-and mouth disease virus. J. Gen. Virol. 1975, 26:227-238.
    • (1975) J. Gen. Virol. , vol.26 , pp. 227-238
    • Rowlands, D.J.1    Sangar, D.V.2    Brown, F.3
  • 38
    • 2942635636 scopus 로고    scopus 로고
    • The Rhopalosiphum padi virus 5' internal ribosome entry site is functional in Spodoptera frugiperda 21 cells and in their cell-free lysates: implications for the baculovirus expression system
    • Royall E., Woolaway K.E., Schacherl J., Kubick S., Belsham G.J., Roberts L.O. The Rhopalosiphum padi virus 5' internal ribosome entry site is functional in Spodoptera frugiperda 21 cells and in their cell-free lysates: implications for the baculovirus expression system. J. Gen. Virol. 2004, 85:1565-1569.
    • (2004) J. Gen. Virol. , vol.85 , pp. 1565-1569
    • Royall, E.1    Woolaway, K.E.2    Schacherl, J.3    Kubick, S.4    Belsham, G.J.5    Roberts, L.O.6
  • 39
    • 0018377563 scopus 로고
    • Stability and immunogenicity of empty particles of foot-and-mouth disease virus
    • Rweyemamu M.M., Terry G., Pay T.W. Stability and immunogenicity of empty particles of foot-and-mouth disease virus. Arch. Virol. 1979, 59:69-79.
    • (1979) Arch. Virol. , vol.59 , pp. 69-79
    • Rweyemamu, M.M.1    Terry, G.2    Pay, T.W.3
  • 40
    • 5444256167 scopus 로고    scopus 로고
    • Sequential modification of translation initiation factor eIF4GI by two different foot-and-mouth disease virus proteases within infected baby hamster kidney cells: Identification of the 3CPro cleavage site
    • Strong R., Belsham G.J. Sequential modification of translation initiation factor eIF4GI by two different foot-and-mouth disease virus proteases within infected baby hamster kidney cells: Identification of the 3CPro cleavage site. J. Gen. Virol. 2004, 85:2953-2962.
    • (2004) J. Gen. Virol. , vol.85 , pp. 2953-2962
    • Strong, R.1    Belsham, G.J.2
  • 41
    • 33845759346 scopus 로고    scopus 로고
    • Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis
    • Sweeney T.R., Roque-Rosell N., Birtley J.R., Leatherbarrow R.J., Curry S. Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis. J. Virol. 2007, 81:115-124.
    • (2007) J. Virol. , vol.81 , pp. 115-124
    • Sweeney, T.R.1    Roque-Rosell, N.2    Birtley, J.R.3    Leatherbarrow, R.J.4    Curry, S.5
  • 43
    • 0024230701 scopus 로고
    • HIV expression strategies: ribosomal frameshifting is directed by a short sequence in both mammalian and yeast systems
    • Wilson W., Braddock M., Adams S.E., Rathjen P.D., Kingsman S.M., Kingsman A.J. HIV expression strategies: ribosomal frameshifting is directed by a short sequence in both mammalian and yeast systems. Cell 1988, 55:1159-1169.
    • (1988) Cell , vol.55 , pp. 1159-1169
    • Wilson, W.1    Braddock, M.2    Adams, S.E.3    Rathjen, P.D.4    Kingsman, S.M.5    Kingsman, A.J.6
  • 45
    • 73149105706 scopus 로고    scopus 로고
    • Insights into cleavage specificity from the crystal structure of foot-and-mouth disease virus 3C protease complexed with a peptide substrate
    • Zunszain P.A., Knox S.R., Sweeney T.R., Yang J., Roque-Rosell N., Belsham G.J., Leatherbarrow R.J., Curry S. Insights into cleavage specificity from the crystal structure of foot-and-mouth disease virus 3C protease complexed with a peptide substrate. J. Mol. Biol. 2010, 395:375-389.
    • (2010) J. Mol. Biol. , vol.395 , pp. 375-389
    • Zunszain, P.A.1    Knox, S.R.2    Sweeney, T.R.3    Yang, J.4    Roque-Rosell, N.5    Belsham, G.J.6    Leatherbarrow, R.J.7    Curry, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.