메뉴 건너뛰기




Volumn 991, Issue , 2015, Pages 21-28

Purification of recombinant virus-like particles of porcine circovirus type 2 capsid protein using ion-exchange monolith chromatography

Author keywords

Ion exchange chromatography; Monolith; Porcine circovirus type 2; Virus like particles

Indexed keywords

CHROMATOGRAPHIC ANALYSIS; DIAGNOSIS; ION CHROMATOGRAPHY; IONS; NUCLEIC ACIDS; POLYSACCHARIDES; PORE SIZE; PURIFICATION; RECOMBINANT PROTEINS; SELF ASSEMBLY; VIRUSES; YEAST;

EID: 84928136393     PISSN: 15700232     EISSN: 1873376X     Source Type: Journal    
DOI: 10.1016/j.jchromb.2015.04.004     Document Type: Article
Times cited : (38)

References (40)
  • 2
    • 0035350580 scopus 로고    scopus 로고
    • Postweaning multisystemic wasting syndrome induced after experimental inoculation of cesarean-derived, colostrum-deprived piglets with type 2 porcine circovirus
    • Bolin S.R., Stoffregen W.C., Nayar G.P., Hamel A.L. Postweaning multisystemic wasting syndrome induced after experimental inoculation of cesarean-derived, colostrum-deprived piglets with type 2 porcine circovirus. J. Vet. Diagn. Invest. 2001, 13:185-194.
    • (2001) J. Vet. Diagn. Invest. , vol.13 , pp. 185-194
    • Bolin, S.R.1    Stoffregen, W.C.2    Nayar, G.P.3    Hamel, A.L.4
  • 3
    • 0035461746 scopus 로고    scopus 로고
    • Experimental reproduction of severe disease in CD/CD pigs concurrently infected with type 2 porcine circovirus and porcine reproductive and respiratory syndrome virus
    • Harms P.A., Sorden S.D., Halbur P.G., Bolin S., Lager K., Morozov I., Paul P.S. Experimental reproduction of severe disease in CD/CD pigs concurrently infected with type 2 porcine circovirus and porcine reproductive and respiratory syndrome virus. Vet. Pathol. 2001, 38:528-539.
    • (2001) Vet. Pathol. , vol.38 , pp. 528-539
    • Harms, P.A.1    Sorden, S.D.2    Halbur, P.G.3    Bolin, S.4    Lager, K.5    Morozov, I.6    Paul, P.S.7
  • 4
    • 0036729072 scopus 로고    scopus 로고
    • Postweaning multisystemic wasting syndrome (PMWS) in pigs. A review
    • Segales J., Domingo M. Postweaning multisystemic wasting syndrome (PMWS) in pigs. A review. Vet. Q. 2002, 24:109-124.
    • (2002) Vet. Q. , vol.24 , pp. 109-124
    • Segales, J.1    Domingo, M.2
  • 6
    • 0345599153 scopus 로고    scopus 로고
    • Comparison of the structures of three circoviruses: chicken anemia virus, porcine circovirus type 2, and beak and feather disease virus
    • Crowther R.A., Berriman J.A., Curran W.L., Allan G.M., Todd D. Comparison of the structures of three circoviruses: chicken anemia virus, porcine circovirus type 2, and beak and feather disease virus. J. Virol. 2003, 77:13036-13041.
    • (2003) J. Virol. , vol.77 , pp. 13036-13041
    • Crowther, R.A.1    Berriman, J.A.2    Curran, W.L.3    Allan, G.M.4    Todd, D.5
  • 9
    • 0142199970 scopus 로고    scopus 로고
    • Protection of swine against post-weaning multisystemic wasting syndrome (PMWS) by porcine circovirus type 2 (PCV2) proteins
    • Blanchard P., Mahe D., Cariolet R., Keranflec'h A., Baudouard M.A., Cordioli P., Albina E., Jestin A. Protection of swine against post-weaning multisystemic wasting syndrome (PMWS) by porcine circovirus type 2 (PCV2) proteins. Vaccine 2003, 21:4565-4575.
    • (2003) Vaccine , vol.21 , pp. 4565-4575
    • Blanchard, P.1    Mahe, D.2    Cariolet, R.3    Keranflec'h, A.4    Baudouard, M.A.5    Cordioli, P.6    Albina, E.7    Jestin, A.8
  • 10
    • 33947114477 scopus 로고    scopus 로고
    • Expression of porcine circovirus 2 ORF2 gene requires codon optimized E. coli cells
    • Trundova M., Celer V. Expression of porcine circovirus 2 ORF2 gene requires codon optimized E. coli cells. Virus Genes 2007, 34:199-204.
    • (2007) Virus Genes , vol.34 , pp. 199-204
    • Trundova, M.1    Celer, V.2
  • 11
    • 70349745170 scopus 로고    scopus 로고
    • Heterologous expression of full-length capsid protein of porcine circovirus 2 in Escherichia coli and its potential use for detection of antibodies
    • Marcekova Z., Psikal I., Kosinova E., Benada O., Sebo P., Bumba L. Heterologous expression of full-length capsid protein of porcine circovirus 2 in Escherichia coli and its potential use for detection of antibodies. J. Virol. Methods 2009, 162:133-141.
    • (2009) J. Virol. Methods , vol.162 , pp. 133-141
    • Marcekova, Z.1    Psikal, I.2    Kosinova, E.3    Benada, O.4    Sebo, P.5    Bumba, L.6
  • 12
    • 84872034033 scopus 로고    scopus 로고
    • Characterization of porcine circovirus type 2 (PCV2) capsid particle assembly and its application to virus-like particle vaccine development
    • Wu P.-C., Lin W.-L., Wu C.-M., Chi J.-N., Chien M.-S., Huang C. Characterization of porcine circovirus type 2 (PCV2) capsid particle assembly and its application to virus-like particle vaccine development. Appl. Microbiol. Biotechnol. 2012, 95:1501-1507.
    • (2012) Appl. Microbiol. Biotechnol. , vol.95 , pp. 1501-1507
    • Wu, P.-C.1    Lin, W.-L.2    Wu, C.-M.3    Chi, J.-N.4    Chien, M.-S.5    Huang, C.6
  • 14
    • 69749101697 scopus 로고    scopus 로고
    • The optimized capsid gene of porcine circovirus type 2 expressed in yeast forms virus-like particles and elicits antibody responses in mice fed with recombinant yeast extracts
    • Bucarey S.A., Noriega J., Reyes P., Tapia C., Saenz L., Zuniga A., Tobar J.A. The optimized capsid gene of porcine circovirus type 2 expressed in yeast forms virus-like particles and elicits antibody responses in mice fed with recombinant yeast extracts. Vaccine 2009, 27:5781-5790.
    • (2009) Vaccine , vol.27 , pp. 5781-5790
    • Bucarey, S.A.1    Noriega, J.2    Reyes, P.3    Tapia, C.4    Saenz, L.5    Zuniga, A.6    Tobar, J.A.7
  • 15
  • 17
    • 84871650149 scopus 로고    scopus 로고
    • Construction and characterization of virus-like particles: a review
    • Zeltins A. Construction and characterization of virus-like particles: a review. Mol. Biotechnol. 2013, 53:92-107.
    • (2013) Mol. Biotechnol. , vol.53 , pp. 92-107
    • Zeltins, A.1
  • 18
    • 84870680670 scopus 로고    scopus 로고
    • Recognition of the different structural forms of the capsid protein determines the outcome following infection with porcine circovirus type 2
    • Trible B.R., Suddith A.W., Kerrigan M.A., Cino-Ozuna A.G., Hesse R.A., Rowland R.R.R. Recognition of the different structural forms of the capsid protein determines the outcome following infection with porcine circovirus type 2. J. Virol. 2012, 86:13508-13514.
    • (2012) J. Virol. , vol.86 , pp. 13508-13514
    • Trible, B.R.1    Suddith, A.W.2    Kerrigan, M.A.3    Cino-Ozuna, A.G.4    Hesse, R.A.5    Rowland, R.R.R.6
  • 19
    • 77954661650 scopus 로고    scopus 로고
    • Self-assembly of virus-like particles of porcine circovirus type 2 capsid protein expressed from Escherichia coli
    • Yin S., Sun S., Yang S., Shang Y., Cai X., Liu X. Self-assembly of virus-like particles of porcine circovirus type 2 capsid protein expressed from Escherichia coli. Virol. J. 2010, 7:166.
    • (2010) Virol. J. , vol.7 , pp. 166
    • Yin, S.1    Sun, S.2    Yang, S.3    Shang, Y.4    Cai, X.5    Liu, X.6
  • 21
    • 33845223389 scopus 로고    scopus 로고
    • Primary recovery and chromatographic purification of adeno-associated virus type 2 produced by baculovirus/insect cell system
    • Chahal P.S., Aucoin M.G., Kamen A. Primary recovery and chromatographic purification of adeno-associated virus type 2 produced by baculovirus/insect cell system. J. Virol. Methods 2007, 139:61-70.
    • (2007) J. Virol. Methods , vol.139 , pp. 61-70
    • Chahal, P.S.1    Aucoin, M.G.2    Kamen, A.3
  • 22
    • 78649326009 scopus 로고    scopus 로고
    • Production and purification of human papillomavirus type 33 L1 virus-like particles from Spodoptera frugiperda 9 cells using two-step column chromatography
    • Baek J.-O., Seo J.-W., Kim I.-H., Kim C.H. Production and purification of human papillomavirus type 33 L1 virus-like particles from Spodoptera frugiperda 9 cells using two-step column chromatography. Protein Express. Purif. 2011, 75:211-217.
    • (2011) Protein Express. Purif. , vol.75 , pp. 211-217
    • Baek, J.-O.1    Seo, J.-W.2    Kim, I.-H.3    Kim, C.H.4
  • 23
    • 78149252754 scopus 로고    scopus 로고
    • Purification of cell culture-derived modified vaccinia ankara virus by pseudo-affinity membrane adsorbers and hydrophobic interaction chromatography
    • Wolff M.W., Siewert C., Hansen S.P., Faber R., Reichl U. Purification of cell culture-derived modified vaccinia ankara virus by pseudo-affinity membrane adsorbers and hydrophobic interaction chromatography. Biotechnol. Bioeng. 2010, 107:312-320.
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 312-320
    • Wolff, M.W.1    Siewert, C.2    Hansen, S.P.3    Faber, R.4    Reichl, U.5
  • 24
    • 0029982158 scopus 로고    scopus 로고
    • Superporous agarose, a new material for chromatography
    • Gustavsson P.-E., Larsson P.-O. Superporous agarose, a new material for chromatography. J. Chromatogr. A 1996, 734:231-240.
    • (1996) J. Chromatogr. A , vol.734 , pp. 231-240
    • Gustavsson, P.-E.1    Larsson, P.-O.2
  • 25
    • 33747756225 scopus 로고    scopus 로고
    • Pore size distributions of ion exchangers and relation to protein binding capacity
    • Yao Y., Lenhoff A.M. Pore size distributions of ion exchangers and relation to protein binding capacity. J. Chromatogr. A 2006, 1126:107-119.
    • (2006) J. Chromatogr. A , vol.1126 , pp. 107-119
    • Yao, Y.1    Lenhoff, A.M.2
  • 26
    • 84896707282 scopus 로고    scopus 로고
    • Improving stability of virus-like particles by ion-exchange chromatographic supports with large pore size: advantages of gigaporous media beyond enhanced binding capacity
    • Yu M., Li Y., Zhang S., Li X., Yang Y., Chen Y., Ma G., Su Z. Improving stability of virus-like particles by ion-exchange chromatographic supports with large pore size: advantages of gigaporous media beyond enhanced binding capacity. J. Chromatogr. A 2014, 1331:69-79.
    • (2014) J. Chromatogr. A , vol.1331 , pp. 69-79
    • Yu, M.1    Li, Y.2    Zhang, S.3    Li, X.4    Yang, Y.5    Chen, Y.6    Ma, G.7    Su, Z.8
  • 27
    • 39749156913 scopus 로고    scopus 로고
    • Polymethacrylate monoliths for preparative and industrial separation of biomolecular assemblies
    • Jungbauer A., Hahn R. Polymethacrylate monoliths for preparative and industrial separation of biomolecular assemblies. J. Chromatogr. A 2008, 1184:62-79.
    • (2008) J. Chromatogr. A , vol.1184 , pp. 62-79
    • Jungbauer, A.1    Hahn, R.2
  • 28
    • 79953299871 scopus 로고    scopus 로고
    • Purification of recombinant adenovirus type 3 dodecahedric virus-like particles for biomedical applications using short monolithic columns
    • Urbas L., Jarc B.L., Barut M., Zochowska M., Chroboczek J., Pihlar B., Szolajska E. Purification of recombinant adenovirus type 3 dodecahedric virus-like particles for biomedical applications using short monolithic columns. J. Chromatogr. A 2011, 1218:2451-2459.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 2451-2459
    • Urbas, L.1    Jarc, B.L.2    Barut, M.3    Zochowska, M.4    Chroboczek, J.5    Pihlar, B.6    Szolajska, E.7
  • 29
    • 84855204481 scopus 로고    scopus 로고
    • A monolith purification process for virus-like particles from yeast homogenate
    • Burden C.S., Jin J., Podgornik A., Bracewell D.G. A monolith purification process for virus-like particles from yeast homogenate. J. Chromatogr. B 2012, 880:82-89.
    • (2012) J. Chromatogr. B , vol.880 , pp. 82-89
    • Burden, C.S.1    Jin, J.2    Podgornik, A.3    Bracewell, D.G.4
  • 30
    • 0030606881 scopus 로고    scopus 로고
    • Apparent pore size distributions of chromatography media
    • Hagel L., Ostberg M., Andersson T. Apparent pore size distributions of chromatography media. J. Chromatogr. A 1996, 743:33-42.
    • (1996) J. Chromatogr. A , vol.743 , pp. 33-42
    • Hagel, L.1    Ostberg, M.2    Andersson, T.3
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 42649133821 scopus 로고    scopus 로고
    • Expression of the capsid protein of porcine circovirus type 2 in Lactococcus lactis for oral vaccination
    • Wang K., Huang L., Kong J., Zhang X. Expression of the capsid protein of porcine circovirus type 2 in Lactococcus lactis for oral vaccination. J. Virol. Methods 2008, 150:1-6.
    • (2008) J. Virol. Methods , vol.150 , pp. 1-6
    • Wang, K.1    Huang, L.2    Kong, J.3    Zhang, X.4
  • 34
    • 33645229143 scopus 로고    scopus 로고
    • Porcine circovirus 2 uses heparin sulfate and chondroitin sulfate B glycosaminoglycans as receptors for its attachment to host cells
    • Misinzo G., Delputte P.L., Meerts P., Lefebvre D.J., Nauwynck H.J. Porcine circovirus 2 uses heparin sulfate and chondroitin sulfate B glycosaminoglycans as receptors for its attachment to host cells. J. Virol. 2006, 80:3487-3494.
    • (2006) J. Virol. , vol.80 , pp. 3487-3494
    • Misinzo, G.1    Delputte, P.L.2    Meerts, P.3    Lefebvre, D.J.4    Nauwynck, H.J.5
  • 36
    • 1842843148 scopus 로고    scopus 로고
    • Heterologous expression of the modified coat protein of Cowpea chlorotic mottle bromovirus results in the assembly of protein cages with altered architectures and function
    • Brumfield S., Willits D., Tang L., Johnson J.E., Douglas T., Young M. Heterologous expression of the modified coat protein of Cowpea chlorotic mottle bromovirus results in the assembly of protein cages with altered architectures and function. J. Gen. Virol. 2004, 85:1049-1053.
    • (2004) J. Gen. Virol. , vol.85 , pp. 1049-1053
    • Brumfield, S.1    Willits, D.2    Tang, L.3    Johnson, J.E.4    Douglas, T.5    Young, M.6
  • 38
    • 77953291167 scopus 로고    scopus 로고
    • Critical evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the measurement of nanoparticles and protein aggregates
    • Filipe V., Hawe A., Jiskoot W. Critical evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the measurement of nanoparticles and protein aggregates. Pharm. Res. 2010, 27:796-810.
    • (2010) Pharm. Res. , vol.27 , pp. 796-810
    • Filipe, V.1    Hawe, A.2    Jiskoot, W.3
  • 39
    • 84868641569 scopus 로고    scopus 로고
    • Evaluation of nanoparticle tracking analysis for total virus particle determination
    • Kramberger P., Ciringer M., Štrancar A., Peterka M. Evaluation of nanoparticle tracking analysis for total virus particle determination. Virol. J. 2012, 9:265.
    • (2012) Virol. J. , vol.9 , pp. 265
    • Kramberger, P.1    Ciringer, M.2    Štrancar, A.3    Peterka, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.