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Volumn 4, Issue NOV, 2013, Pages

Engineering production of functional scfv antibody in E. coli by co-expressing the molecule chaperone skp

Author keywords

Co expression; Production; ScFv; Solubility; Vibrio parahaemolyticus

Indexed keywords

CHAPERONE; CHAPERONE SKP; IMMUNOGLOBULIN LIGHT CHAIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; PROTEIN BINDING; SKP PROTEIN, E COLI;

EID: 84897923580     PISSN: None     EISSN: 22352988     Source Type: Journal    
DOI: 10.3389/fcimb.2013.00072     Document Type: Article
Times cited : (45)

References (41)
  • 1
    • 79953699669 scopus 로고    scopus 로고
    • Chronic intranasal treatment with an anti-AÂ30-42 scFv antibody ameliorates amyloid pathology in a transgenic mouse model of alzheimer's disease
    • doi: 10.1371/journal.pone.0018296
    • Cattepoel, S., Hanenberg, M., Kulic, L., and Nitsch, R. M. (2011). Chronic intranasal treatment with an anti-AÂ30-42 scFv antibody ameliorates amyloid pathology in a transgenic mouse model of alzheimer's disease. PLoS ONE 6:e18296. doi: 10.1371/journal.pone.0018296
    • (2011) PLoS ONE , vol.6
    • Cattepoel, S.1    Hanenberg, M.2    Kulic, L.3    Nitsch, R.M.4
  • 2
    • 0035342588 scopus 로고    scopus 로고
    • Protein affinity maturation in vivo using Ecoli mutator cells
    • doi: 10.1016/S0022-1759(01)00300-3
    • Coia, G., Hudson, P. J., and Irving, R. A. (2001). Protein affinity maturation in vivo using E. coli mutator cells. J. Immun. Methods 251, 187-193. doi: 10.1016/S0022-1759(01)00300-3
    • (2001) J. Immun. Methods , vol.251 , pp. 187-193
    • Coia, G.1    Hudson, P.J.2    Irving, R.A.3
  • 3
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production
    • doi: 10.1002/jmr.687
    • Daly, R., and Hearn, M. T. (2005). Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J. Mol. Recognit. 18, 119-138. doi: 10.1002/jmr.687
    • (2005) J. Mol. Recognit , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.2
  • 4
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • doi: 10.1002/(SICI)1097-0290(19991120)65:4382::AID-BIT23.3.CO;2-9
    • Davis, G. D., Elisee, C., Newham, D. M., and Harrison, R. G. (1999). New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol. Bioeng. 65, 382-388. doi: 10.1002/(SICI)1097-0290(19991120)65:4382::AID-BIT23.3.CO;2-9
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 5
    • 84954358425 scopus 로고    scopus 로고
    • Mocr: a novel fusion tag for enhancing solubility that is compatible with structural biology applications
    • doi: 10.1016/j.pep.2008.08.011
    • DelProposto, J., Majmudar, C. Y., Smith, J. L., and Brown, W. C. (2009). Mocr: a novel fusion tag for enhancing solubility that is compatible with structural biology applications. Protein Expr. Purif. 63, 40-49. doi: 10.1016/j.pep.2008.08.011
    • (2009) Protein Expr. Purif. , vol.63 , pp. 40-49
    • DelProposto, J.1    Majmudar, C.Y.2    Smith, J.L.3    Brown, W.C.4
  • 6
    • 1842582929 scopus 로고    scopus 로고
    • Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning
    • doi: 10.1016/j.jbiotec.2003.10.025
    • De Marco, A., and De Marco, V. (2004). Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning. J. Biotechnol. 109, 45-52. doi: 10.1016/j.jbiotec.2003.10.025
    • (2004) J. Biotechnol. , vol.109 , pp. 45-52
    • De Marco, A.1    De Marco, V.2
  • 7
    • 34147152321 scopus 로고    scopus 로고
    • Generation of activation-specific human anti-{alpha} M {beta} 2 single-chain antibodies as potential diagnostic tools and therapeutic agents
    • doi: 10.1182/blood-2006-03-007179
    • Eisenhardt, S. U., Schwarz, M., Schallner, N., Soosairajah, J., Bassler, N., Huang, D. X., et al. (2007). Generation of activation-specific human anti-{alpha} M {beta} 2 single-chain antibodies as potential diagnostic tools and therapeutic agents. Blood 109, 3521-3528. doi: 10.1182/blood-2006-03-007179
    • (2007) Blood , vol.109 , pp. 3521-3528
    • Eisenhardt, S.U.1    Schwarz, M.2    Schallner, N.3    Soosairajah, J.4    Bassler, N.5    Huang, D.X.6
  • 8
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • doi: 10.1016/j.copbio.2006.06.003
    • Esposito, D., and Chatterjee, D. K. (2006). Enhancement of soluble protein expression through the use of fusion tags. Curr. Opin. Biotechnol. 17, 353-358. doi: 10.1016/j.copbio.2006.06.003
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 9
    • 0037208811 scopus 로고    scopus 로고
    • Maltose-binding protein as a solubility enhancer
    • doi: 10.1385/1-59259-301-1:99
    • Fox, J. D., and Waugh, D. S. (2003). Maltose-binding protein as a solubility enhancer. Methods Mol. Biol. 205, 99-117. doi: 10.1385/1-59259-301-1:99
    • (2003) Methods Mol. Biol. , vol.205 , pp. 99-117
    • Fox, J.D.1    Waugh, D.S.2
  • 10
    • 77955847863 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant protein by Escherichia coli in a defined medium
    • doi: 10.1007/s00253-010-2718-9
    • Fu, X. Y. (2010). Extracellular accumulation of recombinant protein by Escherichia coli in a defined medium. Appl Microbiol. Biotechnol. 88, 75-86. doi: 10.1007/s00253-010-2718-9
    • (2010) Appl Microbiol. Biotechnol. , vol.88 , pp. 75-86
    • Fu, X.Y.1
  • 11
    • 0037395157 scopus 로고    scopus 로고
    • Protein production in Escherichia coli for structural studies by X-ray crystallography
    • doi: 10.1016/S1047-8477(03)00044-3
    • Goulding, C. W., and Perry, L. J. (2003). Protein production in Escherichia coli for structural studies by X-ray crystallography. J Struct Biol 142, 133-143. doi: 10.1016/S1047-8477(03)00044-3
    • (2003) J Struct Biol , vol.142 , pp. 133-143
    • Goulding, C.W.1    Perry, L.J.2
  • 12
    • 4644273937 scopus 로고    scopus 로고
    • Host cell compatibility in protein expression
    • doi: 10.1385/1-59259-774-2:003
    • Greene, J. J. (2004). Host cell compatibility in protein expression. Methods Mol. Biol. 267, 3-14. doi: 10.1385/1-59259-774-2:003
    • (2004) Methods Mol. Biol. , vol.267 , pp. 3-14
    • Greene, J.J.1
  • 13
    • 80052639750 scopus 로고    scopus 로고
    • Wheat germ cell-free expression system as a pathway to improve protein yield and solubility for the SSGCID pipeline
    • doi: 10.1107/S1744309111032143
    • Guild, K., Zhang, Y., Stacy, R., Mundt, E., Benbow, S., Green, A., et al. (2011). Wheat germ cell-free expression system as a pathway to improve protein yield and solubility for the SSGCID pipeline. Acta Cryst. F67, 1027-1031. doi: 10.1107/S1744309111032143
    • (2011) Acta Cryst. , vol.F67 , pp. 1027-1031
    • Guild, K.1    Zhang, Y.2    Stacy, R.3    Mundt, E.4    Benbow, S.5    Green, A.6
  • 14
    • 0037406621 scopus 로고    scopus 로고
    • Isolation and expression of recombinant antibody fragments to the biological warfare pathogen Brucella melitensis
    • doi: 10.1016/S0022-1759(03)00100-5
    • Hayhurst, A., Happe, S., Mabry, R., Koch, Z., Iverson, B. L., and Georgiou, G. (2003). Isolation and expression of recombinant antibody fragments to the biological warfare pathogen Brucella melitensis. J. Immunol. Methods 276, 185-196. doi: 10.1016/S0022-1759(03)00100-5
    • (2003) J. Immunol. Methods , vol.276 , pp. 185-196
    • Hayhurst, A.1    Happe, S.2    Mabry, R.3    Koch, Z.4    Iverson, B.L.5    Georgiou, G.6
  • 15
    • 0033117352 scopus 로고    scopus 로고
    • Escherichia coli skp chaperone co-expression improves solubility and phage display of single-chain antibody fragments
    • doi: 10.1006/prep.1999.1035
    • Hayhurst, A., and Harris, W. J. (1999). Escherichia coli skp chaperone co-expression improves solubility and phage display of single-chain antibody fragments. Protein Expr. Purif. 15, 336-343. doi: 10.1006/prep.1999.1035
    • (1999) Protein Expr. Purif. , vol.15 , pp. 336-343
    • Hayhurst, A.1    Harris, W.J.2
  • 16
    • 33644759558 scopus 로고    scopus 로고
    • Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of E. Coli: evidence that chaperone activity is the prime effect of thioredoxin
    • doi: 10.1016/j.jmb.2005.12.058
    • Jurado, P., de Lorenzo, V., and Fernández, L. A. (2006). Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of E. coli: evidence that chaperone activity is the prime effect of thioredoxin. J. Mol. Biol. 357, 49-61. doi: 10.1016/j.jmb.2005.12.058
    • (2006) J. Mol. Biol. , vol.357 , pp. 49-61
    • Jurado, P.1    de Lorenzo, V.2    Fernández, L.A.3
  • 17
    • 33747890567 scopus 로고    scopus 로고
    • Selection of tumor-binding ligands in cancer patients with phage display libraries
    • doi: 10.1158/0008-5472.CAN-05-4441
    • Krag, D. N., Shukla, G. S., Shen, G. P., Pero, S., Ashikaga, T., Fuller, S., et al. (2006). Selection of tumor-binding ligands in cancer patients with phage display libraries. Cancer Res. 66, 7724-7733. doi: 10.1158/0008-5472.CAN-05-4441
    • (2006) Cancer Res. , vol.66 , pp. 7724-7733
    • Krag, D.N.1    Shukla, G.S.2    Shen, G.P.3    Pero, S.4    Ashikaga, T.5    Fuller, S.6
  • 18
    • 79951949970 scopus 로고    scopus 로고
    • Refolding single-chain antibody (scFv) using lauroyl-L-glutamate as a solubilization detergent and arginine as a refolding additive
    • doi: 10.1016/j.pep.2010.12.007
    • Kudou, M., Ejima, D., Sato, H., Yumioka, R., Arakawa, T., and Tsumoto, K. (2011). Refolding single-chain antibody (scFv) using lauroyl-L-glutamate as a solubilization detergent and arginine as a refolding additive. Protein Expr. Purif. 77, 68-74. doi: 10.1016/j.pep.2010.12.007
    • (2011) Protein Expr. Purif. , vol.77 , pp. 68-74
    • Kudou, M.1    Ejima, D.2    Sato, H.3    Yumioka, R.4    Arakawa, T.5    Tsumoto, K.6
  • 19
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO
    • doi: 10.1110/ps.051812706
    • Marblestone, J. G., Edavettal, S. C., Lim, Y., Lim, P., Zuo, X., and Butt, T. R. (2006). Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO. Protein Sci. 15, 182-189. doi: 10.1110/ps.051812706
    • (2006) Protein Sci. , vol.15 , pp. 182-189
    • Marblestone, J.G.1    Edavettal, S.C.2    Lim, Y.3    Lim, P.4    Zuo, X.5    Butt, T.R.6
  • 20
    • 28844481147 scopus 로고    scopus 로고
    • Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners
    • doi: 10.1016/j.pep.2005.06.012
    • Nallamsetty, S., and Waugh, D. S. (2006). Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. Protein Expr. Purif. 45, 175-182. doi: 10.1016/j.pep.2005.06.012
    • (2006) Protein Expr. Purif. , vol.45 , pp. 175-182
    • Nallamsetty, S.1    Waugh, D.S.2
  • 21
    • 0028287188 scopus 로고
    • Engineering proteins to facilitate bioprocessing
    • doi: 10.1016/0167-7799(94)90080-9
    • Nygren, P. A., Stahl, S., and Uhlen, M. (1994). Engineering proteins to facilitate bioprocessing. Trends Biotechnol. 12, 184-188. doi: 10.1016/0167-7799(94)90080-9
    • (1994) Trends Biotechnol. , vol.12 , pp. 184-188
    • Nygren, P.A.1    Stahl, S.2    Uhlen, M.3
  • 22
    • 77950630983 scopus 로고    scopus 로고
    • Co-Expression of Skp and FkpA chaperones improves cell viability and alters the global expression of stress response genes during scFvD1 3 production
    • doi: 10.1186/1475-2859-9-22
    • Ow, D. S. W., Lim, D. Y. X., Nissom, P. M., Camattari, A., and Wong, V. V. T. (2010). Co-Expression of Skp and FkpA chaperones improves cell viability and alters the global expression of stress response genes during scFvD1.3 production. Microb. Cell Fact. 9, 22-36. doi: 10.1186/1475-2859-9-22
    • (2010) Microb. Cell Fact. , vol.9 , pp. 22-36
    • Ow, D.S.W.1    Lim, D.Y.X.2    Nissom, P.M.3    Camattari, A.4    Wong, V.V.T.5
  • 23
    • 3042825336 scopus 로고    scopus 로고
    • Cold-shock induced high yield protein production in Escherichia coli
    • doi: 10.1038/nbt984
    • Qing, G., Ma, L. C., Khorchid, A., Swapna, G. Y. T., Mal, T. K., Takayama, M. M., et al. (2004). Cold-shock induced high yield protein production in Escherichia coli. Nat. Biotechnol. 22, 877-882. doi: 10.1038/nbt984
    • (2004) Nat. Biotechnol. , vol.22 , pp. 877-882
    • Qing, G.1    Ma, L.C.2    Khorchid, A.3    Swapna, G.Y.T.4    Mal, T.K.5    Takayama, M.M.6
  • 24
    • 77957768682 scopus 로고    scopus 로고
    • Phage-derived fully human monoclonal antibody fragments to human vascular endothelial growth factor-C block its interaction with VEGF receptor-2 and 3
    • doi: 10.1371/journal.pone.0011941
    • Rinderknecht, M., Villa, A., Ballmer-Hofer, K., Neri, D., and Detmar, M. (2010). Phage-derived fully human monoclonal antibody fragments to human vascular endothelial growth factor-C block its interaction with VEGF receptor-2 and 3. PLoS ONE 5:e11941. doi: 10.1371/journal.pone.0011941
    • (2010) PLoS ONE , vol.5
    • Rinderknecht, M.1    Villa, A.2    Ballmer-Hofer, K.3    Neri, D.4    Detmar, M.5
  • 25
    • 34447100309 scopus 로고    scopus 로고
    • Selection of human anti-CD28 scFvs from a T-NHL related scFv library using ribosome display
    • doi: 10.1016/j.jbiotec.2007.05.012
    • Rothe, A., Nathanielsz, A., Hosse, R. J., Oberh, F., Strandmann, E. P., Engert, A., et al. (2007). Selection of human anti-CD28 scFvs from a T-NHL related scFv library using ribosome display. J. Biotechnol. 130, 448-454. doi: 10.1016/j.jbiotec.2007.05.012
    • (2007) J. Biotechnol. , vol.130 , pp. 448-454
    • Rothe, A.1    Nathanielsz, A.2    Hosse, R.J.3    Oberh, F.4    Strandmann, E.P.5    Engert, A.6
  • 26
    • 40049094697 scopus 로고    scopus 로고
    • Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains
    • doi: 10.1016/j.jmb.2008.01.022
    • Saerens, D., Conrath, K., Govaert, J., and Muyldermans, S. (2008). Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains. J. Mol. Biol. 377, 478-488. doi: 10.1016/j.jmb.2008.01.022
    • (2008) J. Mol. Biol. , vol.377 , pp. 478-488
    • Saerens, D.1    Conrath, K.2    Govaert, J.3    Muyldermans, S.4
  • 27
    • 77953714330 scopus 로고    scopus 로고
    • Isolation and characterization of antibodies against three consecutive Tn-antigen clusters from a phage library displaying human single-chain variable fragments
    • doi: 10.1093/jb/mvq014
    • Sakai, K., Yuasa, N., Tsukamoto, K., Takasaki-Matsumoto, A., Yajima, Y., Sato, R., et al. (2010). Isolation and characterization of antibodies against three consecutive Tn-antigen clusters from a phage library displaying human single-chain variable fragments. J. Biochem. 147, 809-817. doi: 10.1093/jb/mvq014
    • (2010) J. Biochem. , vol.147 , pp. 809-817
    • Sakai, K.1    Yuasa, N.2    Tsukamoto, K.3    Takasaki-Matsumoto, A.4    Yajima, Y.5    Sato, R.6
  • 28
    • 78650373185 scopus 로고    scopus 로고
    • Construction of a single-chain variable-fragment antibody against the superantigen staphylococcal enterotoxin B
    • doi: 10.1128/AEM.01441-10
    • Singh, P. K., Agrawal, R., Kamboj, D. V., Gupta, G., Boopathi, M., Goel, A. K., et al. (2010). Construction of a single-chain variable-fragment antibody against the superantigen staphylococcal enterotoxin B. Appl. Environ. Microbiol. 76, 8184-8191. doi: 10.1128/AEM.01441-10
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 8184-8191
    • Singh, P.K.1    Agrawal, R.2    Kamboj, D.V.3    Gupta, G.4    Boopathi, M.5    Goel, A.K.6
  • 29
    • 79960712070 scopus 로고    scopus 로고
    • Highly efficient production of anti-HER2 scFv antibody variant for targeting breast cancer cells
    • doi: 10.1007/s00253-011-3306-3
    • Sommaruga, S., Lombardi, A., Salvadè, A., Mazzucchelli, S., Corsi, F., Galeffi, P., et al. (2011). Highly efficient production of anti-HER2 scFv antibody variant for targeting breast cancer cells. Appl. Microbiol. Biotechnol. 91, 613-621. doi: 10.1007/s00253-011-3306-3
    • (2011) Appl. Microbiol. Biotechnol. , vol.91 , pp. 613-621
    • Sommaruga, S.1    Lombardi, A.2    Salvadè, A.3    Mazzucchelli, S.4    Corsi, F.5    Galeffi, P.6
  • 30
    • 79953307855 scopus 로고    scopus 로고
    • Effects of cytoplasmic and periplasmic chaperones on secretory production of single-chain Fv antibody in Escherichia coli
    • doi: 10.1016/j.jbiosc.2010.12.015
    • Sonoda, H., Kumada, Y., Katsuda, T., and Yamaji, H. (2011). Effects of cytoplasmic and periplasmic chaperones on secretory production of single-chain Fv antibody in Escherichia coli. J. Biosci. Bioeng. 111, 465-470. doi: 10.1016/j.jbiosc.2010.12.015
    • (2011) J. Biosci. Bioeng. , vol.111 , pp. 465-470
    • Sonoda, H.1    Kumada, Y.2    Katsuda, T.3    Yamaji, H.4
  • 31
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • doi: 10.1016/j.jbiotec.2004.08.004
    • Sørensen, H. P., and Mortensen, K. K. (2011). Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115, 113-128. doi: 10.1016/j.jbiotec.2004.08.004
    • (2011) J. Biotechnol. , vol.115 , pp. 113-128
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 32
    • 84856105895 scopus 로고    scopus 로고
    • Overproduction of anti-Tn antibody MLS128 single-chain Fv fragment in Escherichia coli cytoplasm using a novel pCold-PDI vector
    • doi: 10.1016/j.pep.2011.12.010
    • Subedi, G. P., Satoh, T., Hanashima, S., Ikefda, A., Nakada, H., Sato, R., et al. (2012). Overproduction of anti-Tn antibody MLS128 single-chain Fv fragment in Escherichia coli cytoplasm using a novel pCold-PDI vector. Protein Expr. Purif. 82, 197-204. doi: 10.1016/j.pep.2011.12.010
    • (2012) Protein Expr. Purif. , vol.82 , pp. 197-204
    • Subedi, G.P.1    Satoh, T.2    Hanashima, S.3    Ikefda, A.4    Nakada, H.5    Sato, R.6
  • 33
    • 82955187801 scopus 로고    scopus 로고
    • Cloning, expression, purification and characterization of a single chain variable fragment specific to tumor necrosis factor alpha in Escherichia coli
    • doi: 10.1016/j.jbiotec.2011.06.039
    • Sushma, K., Vijayalakshmia, M. A., Krishnana, V., and Satheeshkumara, P. K. (2011). Cloning, expression, purification and characterization of a single chain variable fragment specific to tumor necrosis factor alpha in Escherichia coli. J. Biotechnol. 156, 238-244. doi: 10.1016/j.jbiotec.2011.06.039
    • (2011) J. Biotechnol. , vol.156 , pp. 238-244
    • Sushma, K.1    Vijayalakshmia, M.A.2    Krishnana, V.3    Satheeshkumara, P.K.4
  • 34
    • 77951687530 scopus 로고    scopus 로고
    • Construction and characterization of a novel fusion protein MG7-scFv/SEB against gastric cancer
    • doi: 10.1155/2010/121094
    • Tong, Q., Liu, K., Lu, X. M., Shu, X. G., and Wang, G. B. (2010). Construction and characterization of a novel fusion protein MG7-scFv/SEB against gastric cancer. J. Biomed. Biotechnol. 1, 121094-121102. doi: 10.1155/2010/121094
    • (2010) J. Biomed. Biotechnol. , vol.1 , pp. 121094-121102
    • Tong, Q.1    Liu, K.2    Lu, X.M.3    Shu, X.G.4    Wang, G.B.5
  • 35
    • 38349122119 scopus 로고    scopus 로고
    • Expression, purification, and characterization of an immunotoxin containing a humanized anti-CD25 single chain fragment variable antibody fused to a modified truncated Pseudomonas exotoxin A
    • doi: 10.1016/j.pep.2007.09.009
    • Wang, H. J., Dai, J. X., Li, B. H., Fan, K. X., Peng, L., Zhang, D. P., et al. (2008a). Expression, purification, and characterization of an immunotoxin containing a humanized anti-CD25 single chain fragment variable antibody fused to a modified truncated Pseudomonas exotoxin A. Protein Expr. Purif. 58, 140-147. doi: 10.1016/j.pep.2007.09.009
    • (2008) Protein Expr. Purif. , vol.58 , pp. 140-147
    • Wang, H.J.1    Dai, J.X.2    Li, B.H.3    Fan, K.X.4    Peng, L.5    Zhang, D.P.6
  • 36
    • 48349093825 scopus 로고    scopus 로고
    • Zearalenone (ZEN) detection by a single chain fragment variable (scFv) antibody
    • doi: 10.1007/s11274-008-9657-y
    • Wang, S. H., Du, X. Y., Lin, L., Huang, Y. M., and Wang, Z. H. (2008b). Zearalenone (ZEN) detection by a single chain fragment variable (scFv) antibody. World J. Microbiol. Biotechnol. 24, 1681-1685. doi: 10.1007/s11274-008-9657-y
    • (2008) World J. Microbiol. Biotechnol. , vol.24 , pp. 1681-1685
    • Wang, S.H.1    Du, X.Y.2    Lin, L.3    Huang, Y.M.4    Wang, Z.H.5
  • 37
    • 84863771608 scopus 로고    scopus 로고
    • Screening of a single-chain variable- fragment antibody that can neutralize effectively the cytotoxicity of Vibrio parahaemolyticus TLH
    • doi: 10.1128/AEM.00435-12
    • Wang, R. Z., Fang, S., Wu, D. L., Lian, J. W., Fan, J., Zhang, Y. F., et al. (2012). Screening of a single-chain variable- fragment antibody that can neutralize effectively the cytotoxicity of Vibrio parahaemolyticus TLH. Appl. Environ. Microbiol. 78, 4967-4975. doi: 10.1128/AEM.00435-12
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 4967-4975
    • Wang, R.Z.1    Fang, S.2    Wu, D.L.3    Lian, J.W.4    Fan, J.5    Zhang, Y.F.6
  • 38
    • 79953713207 scopus 로고    scopus 로고
    • Detection and identification of Vibrio parahaemolyticus by multiplex PCR and DNA-DNA hybridization on a microarray
    • doi: 10.1016/j.jgg.2011.02.002
    • Wang, R. Z., Huang, J. D., Zhang, W., Lin, G. M., Lian, J. W., Jiang, L. B., et al. (2011). Detection and identification of Vibrio parahaemolyticus by multiplex PCR and DNA-DNA hybridization on a microarray. J. Genet. Genomics 38, 129-135. doi: 10.1016/j.jgg.2011.02.002
    • (2011) J. Genet. Genomics , vol.38 , pp. 129-135
    • Wang, R.Z.1    Huang, J.D.2    Zhang, W.3    Lin, G.M.4    Lian, J.W.5    Jiang, L.B.6
  • 39
    • 34447519152 scopus 로고    scopus 로고
    • Detection of deoxynivalenol based on a single chain fragment variable(scFv) of the antideoxynivalenol antibody
    • doi: 10.1111/j.1574-6968.2007.00765.x
    • Wang, S. H., Du, X. Y., Huang, Y. M., Lin, D. S., Hart, P. L., and Wang, Z. H. (2007). Detection of deoxynivalenol based on a single chain fragment variable(scFv) of the antideoxynivalenol antibody. FEMS Microbiol. Lett. 272, 214-219. doi: 10.1111/j.1574-6968.2007.00765.x
    • (2007) FEMS Microbiol. Lett. , vol.272 , pp. 214-219
    • Wang, S.H.1    Du, X.Y.2    Huang, Y.M.3    Lin, D.S.4    Hart, P.L.5    Wang, Z.H.6
  • 40
    • 33144455961 scopus 로고    scopus 로고
    • Construction of Single chain variable fragment (ScFv) and biscFv-alkaline phosphatase fusion protein for detection of Bacillus anthracis
    • doi: 10.1021/ac0512352
    • Wang, S. H., Zhang, J. B., Zhang, Z. P., Zhou, Y. F., Yang, R. F., Chen, J., et al. (2006). Construction of Single chain variable fragment (ScFv) and biscFv-alkaline phosphatase fusion protein for detection of Bacillus anthracis. Anal. Chem. 78, 997-1004. doi: 10.1021/ac0512352
    • (2006) Anal. Chem. , vol.78 , pp. 997-1004
    • Wang, S.H.1    Zhang, J.B.2    Zhang, Z.P.3    Zhou, Y.F.4    Yang, R.F.5    Chen, J.6
  • 41
    • 77957906369 scopus 로고    scopus 로고
    • Preparation and cytotoxicity effect of anti- hepatocellular carcinoma scFv immunoliposome on hepatocarcinoma cell in vitro
    • Zhang, G., Liu, Y., and Hu, H. (2010). Preparation and cytotoxicity effect of anti- hepatocellular carcinoma scFv immunoliposome on hepatocarcinoma cell in vitro. Eur. J. Inflamm. 8, 75-82.
    • (2010) Eur. J. Inflamm. , vol.8 , pp. 75-82
    • Zhang, G.1    Liu, Y.2    Hu, H.3


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