메뉴 건너뛰기




Volumn 11, Issue 3, 2013, Pages 881-895

Improved detection of domoic acid using covalently immobilised antibody fragments

Author keywords

Covalent immobilisation; Cysteine; Domoic acid; Protein engineering; ScFv antibody fragment

Indexed keywords

CYSTEINE; DOMOIC ACID; MALEIMIDE; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

EID: 84875771762     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md11030881     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 57749182661 scopus 로고    scopus 로고
    • Firm-Level economic effects of HABS: A tool for business loss assessment
    • Morgan, K.L.; Larkin, S.L.; Adams, C.M. Firm-Level economic effects of HABS: A tool for business loss assessment. Harmful Algae 2009, 8, 212-218.
    • (2009) Harmful Algae , vol.8 , pp. 212-218
    • Morgan, K.L.1    Larkin, S.L.2    Adams, C.M.3
  • 2
    • 41649093625 scopus 로고    scopus 로고
    • The economic effect of harmful algal blooms
    • Graneli, E.T.T., Ed.; Springer: Berlin, Germany
    • Hoagland, P.; Scatasta, S. The Economic Effect of Harmful Algal Blooms. In Ecology on Harmful Algae; Graneli, E.T.T., Ed.; Springer: Berlin, Germany, 2006; Volume 189, pp. 391-402.
    • (2006) Ecology on Harmful Algae , vol.189 , pp. 391-402
    • Hoagland, P.1    Scatasta, S.2
  • 3
    • 0035463459 scopus 로고    scopus 로고
    • Review and assessment of in vitro detection methods for algal toxins
    • Van Dolah, F.M.; Ramsdell, J.S. Review and assessment of in vitro detection methods for algal toxins. J. AOAC Int. 2001, 84, 1617-1625.
    • (2001) J. AOAC Int. , vol.84 , pp. 1617-1625
    • Van Dolah, F.M.1    Ramsdell, J.S.2
  • 4
    • 0035123231 scopus 로고    scopus 로고
    • Domoic acid: A fascinating marine toxin
    • Mos, L. Domoic acid: A fascinating marine toxin. Environ. Toxicol. Pharmacol. 2001, 9, 79-85.
    • (2001) Environ. Toxicol. Pharmacol. , vol.9 , pp. 79-85
    • Mos, L.1
  • 5
    • 0024550624 scopus 로고
    • Domoic acid the alleged "mussel toxin, " might produce its neurotoxic effect through kainate receptor activation: An electrophysiological study in the dorsal hippocampus
    • Debonnel, G.; Beauchesne, L.; de Montigny, C. Domoic acid, the alleged "mussel toxin, " might produce its neurotoxic effect through kainate receptor activation: An electrophysiological study in the dorsal hippocampus. Can. J. Physiol. Pharmacol. 1989, 67, 29-33.
    • (1989) Can. J. Physiol. Pharmacol. , vol.67 , pp. 29-33
    • Debonnel, G.1    Beauchesne, L.2    De Montigny, C.3
  • 6
    • 77649272411 scopus 로고    scopus 로고
    • Domoic acid: Neurobehavioral consequences of exposure to a prevalent marine biotoxin
    • Grant, K.S.; Burbacher, T.M.; Faustman, E.M.; Gratttan, L. Domoic acid: Neurobehavioral consequences of exposure to a prevalent marine biotoxin. Neurotoxicol. Teratol. 2010, 32, 132-141.
    • (2010) Neurotoxicol. Teratol. , vol.32 , pp. 132-141
    • Grant, K.S.1    Burbacher, T.M.2    Faustman, E.M.3    Gratttan, L.4
  • 7
    • 0024971235 scopus 로고
    • The amnesic shellfish poisoning mystery
    • Quilliam, M.A.; Wright, J.L. The amnesic shellfish poisoning mystery. Anal. Chem. 1989, 61, 1053A-1106A.
    • (1989) Anal. Chem. , vol.61
    • Quilliam, M.A.1    Wright, J.L.2
  • 8
    • 79751527114 scopus 로고    scopus 로고
    • A European perspective on progress in moving away from the mouse bioassay for marine-toxin analysis
    • Campbell, K.; Vilariño, N.; Botana, L.M.; Elliott, C.T. A European perspective on progress in moving away from the mouse bioassay for marine-toxin analysis. TrAC Trends Anal. Chem. 2011, 30, 239-253.
    • (2011) TrAC Trends Anal. Chem. , vol.30 , pp. 239-253
    • Campbell, K.1    Vilariño, N.2    Botana, L.M.3    Elliott, C.T.4
  • 9
    • 77955983182 scopus 로고    scopus 로고
    • Marine toxins: Chemistry, toxicity, occurrence and detection, with special reference to the Dutch situation
    • Gerssen, A.; Pol-Hofstad, I.E.; Poelman, M.; Mulder, P.P.; van den Top, H.J.; de Boer, J. Marine toxins: Chemistry, toxicity, occurrence and detection, with special reference to the Dutch situation. Toxins 2010, 2, 878-904.
    • (2010) Toxins , vol.2 , pp. 878-904
    • Gerssen, A.1    Pol-Hofstad, I.E.2    Poelman, M.3    Mulder, P.P.4    Van Den Top, H.J.5    De Boer, J.6
  • 10
    • 77956341549 scopus 로고    scopus 로고
    • Scientific Opinion of the Panel on Contaminants in the Food Chain on a request from the European Commission on marine biotoxins in shellfish-domoic acid
    • EFSA Panel on Contaminants in the Food Chain
    • EFSA Panel on Contaminants in the Food Chain. Scientific Opinion of the Panel on Contaminants in the Food Chain on a request from the European Commission on marine biotoxins in shellfish-domoic acid. EFSA J. 2009, 1181, 1-61.
    • (2009) EFSA J. , vol.1181 , pp. 1-61
  • 13
    • 85015934117 scopus 로고    scopus 로고
    • Analysis of marine toxins - Techniques, method validation, calibration standards and screening methods
    • 2nd ed.; Botana, L.M., Ed.; CRC Press: Boca Raton, FL, USA
    • Holland, P. Analysis of Marine Toxins - Techniques, Method Validation, Calibration Standards and Screening Methods. In Seafood and Freshwater Toxins: Pharmacology, Physiology and Detection, 2nd ed.; Botana, L.M., Ed.; CRC Press: Boca Raton, FL, USA, 2008; pp. 21-49.
    • (2008) Seafood and Freshwater Toxins: Pharmacology, Physiology and Detection , pp. 21-49
    • Holland, P.1
  • 14
    • 33750736092 scopus 로고    scopus 로고
    • Immunobiosensor detection of domoic acid as a screening test in bivalve molluscs: Comparison with liquid chromatography-based analysis
    • Traynor, I.M.; Plumpton, L.; Fodey, T.L.; Higgins, C.; Elliott, C.T. Immunobiosensor detection of domoic acid as a screening test in bivalve molluscs: Comparison with liquid chromatography-based analysis. J. AOAC Int. 2006, 89, 868-872.
    • (2006) J. AOAC Int. , vol.89 , pp. 868-872
    • Traynor, I.M.1    Plumpton, L.2    Fodey, T.L.3    Higgins, C.4    Elliott, C.T.5
  • 15
    • 77953360576 scopus 로고    scopus 로고
    • In situ passive solid-phase adsorption of micro-algal biotoxins as a monitoring tool
    • MacKenzie, L.A. In situ passive solid-phase adsorption of micro-algal biotoxins as a monitoring tool. Curr. Opin. Biotechnol. 2010, 21, 326-331.
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 326-331
    • Mackenzie, L.A.1
  • 17
    • 84874912368 scopus 로고    scopus 로고
    • Antibody immobilization on solid surfaces: Methods and applications
    • The Royal Society of Chemistry: Cambridge, UK
    • Hu, X.; O'Connor, I.B.; Wall, J.G. Antibody Immobilization on Solid Surfaces: Methods and Applications. In Biological Interactions with Surface Charge in Biomaterials; The Royal Society of Chemistry: Cambridge, UK, 2012; pp. 90-104.
    • (2012) Biological Interactions with Surface Charge in Biomaterials , pp. 90-104
    • Hu, X.1    O'Connor, I.B.2    Wall, J.G.3
  • 18
    • 25644448227 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of a single-chain Fv antibody fragment against domoic acid in Escherichia coli
    • Hu, X.; O'Dwyer, R.; Wall, J.G. Cloning, expression and characterisation of a single-chain Fv antibody fragment against domoic acid in Escherichia coli. J. Biotechnol. 2005, 120, 38-45.
    • (2005) J. Biotechnol. , vol.120 , pp. 38-45
    • Hu, X.1    O'Dwyer, R.2    Wall, J.G.3
  • 19
    • 33845957062 scopus 로고    scopus 로고
    • Optimisation of production of a domoic acid-binding scFv antibody fragment in Escherichia coli using molecular chaperones and functional immobilisation on a mesoporous silicate support
    • Hu, X.; O'Hara, L.; White, S.; Magner, E.; Kane, M.; Wall, J.G. Optimisation of production of a domoic acid-binding scFv antibody fragment in Escherichia coli using molecular chaperones and functional immobilisation on a mesoporous silicate support. Protein Expr. Purif. 2007, 52, 194-201.
    • (2007) Protein Expr. Purif. , vol.52 , pp. 194-201
    • Hu, X.1    O'Hara, L.2    White, S.3    Magner, E.4    Kane, M.5    Wall, J.G.6
  • 20
    • 33749614883 scopus 로고    scopus 로고
    • Adsorption and activity of a domoic acid binding antibody fragment on mesoporous silicates
    • Hu, X.; Spada, S.; White, S.; Hudson, S.; Magner, E.; Wall, J.G. Adsorption and activity of a domoic acid binding antibody fragment on mesoporous silicates. J. Phys. Chem. B 2006, 110, 18703-18709.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 18703-18709
    • Hu, X.1    Spada, S.2    White, S.3    Hudson, S.4    Magner, E.5    Wall, J.G.6
  • 21
    • 0004032583 scopus 로고
    • U.S. Department of Health and Human Services, Public Health Service, National Institutes of Health: Bethesda, MD, USA
    • Kabat, E.A. Sequences of Proteins of Immunological Interest; U.S. Department of Health and Human Services, Public Health Service, National Institutes of Health: Bethesda, MD, USA, 1983.
    • (1983) Sequences of Proteins of Immunological Interest
    • Kabat, E.A.1
  • 22
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier, F.W. Protein production by auto-induction in high-density shaking cultures. Protein Expr. Purif. 2005, 41, 207-234.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 23
    • 0035151833 scopus 로고    scopus 로고
    • Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli
    • Bessette, P.H.; Qiu, J.; Bardwell, J.C.; Swartz, J.R.; Georgiou, G. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. J. Bacteriol. 2001, 183, 980-988.
    • (2001) J. Bacteriol. , vol.183 , pp. 980-988
    • Bessette, P.H.1    Qiu, J.2    Bardwell, J.C.3    Swartz, J.R.4    Georgiou, G.5
  • 24
    • 33646792199 scopus 로고    scopus 로고
    • Expression of soluble and functional snake venom fibrinolytic enzyme fibrolase via the co-expression of DsbC in Escherichia coli
    • Zhang, S.T.; Shi, J.; Zhao, J.; Qi, Y.F.; Guo, A.G. Expression of soluble and functional snake venom fibrinolytic enzyme fibrolase via the co-expression of DsbC in Escherichia coli. Protein Peptide Lett. 2006, 13, 559-563.
    • (2006) Protein Peptide Lett. , vol.13 , pp. 559-563
    • Zhang, S.T.1    Shi, J.2    Zhao, J.3    Qi, Y.F.4    Guo, A.G.5
  • 25
    • 0037229810 scopus 로고    scopus 로고
    • DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo
    • Maskos, K.; Huber-Wunderlich, M.; Glockshuber, R. DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo. J. Mol. Biol. 2003, 325, 495-513.
    • (2003) J. Mol. Biol. , vol.325 , pp. 495-513
    • Maskos, K.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 27
    • 27644571313 scopus 로고    scopus 로고
    • Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system
    • Liu, Y.; Zhao, T.-J.; Yan, Y.-B.; Zhou, H.-M. Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Protein Expr. Purif. 2005, 44, 155-161.
    • (2005) Protein Expr. Purif. , vol.44 , pp. 155-161
    • Liu, Y.1    Zhao, T.-J.2    Yan, Y.-B.3    Zhou, H.-M.4
  • 28
    • 62149096127 scopus 로고    scopus 로고
    • Use of folding modulators to improve heterologous protein production in Escherichia coli
    • Kolaj, O.; Spada, S.; Robin, S.; Wall, J.G. Use of folding modulators to improve heterologous protein production in Escherichia coli. Microb. Cell Fact. 2009, 8, 9.
    • (2009) Microb. Cell Fact. , vol.8 , pp. 9
    • Kolaj, O.1    Spada, S.2    Robin, S.3    Wall, J.G.4
  • 29
    • 0842263617 scopus 로고    scopus 로고
    • Production of soluble ScFvs with C-terminal-free thiol for site-specific conjugation or stable dimeric ScFvs on demand
    • Albrecht, H.; Burke, P.A.; Natarajan, A.; Xiong, C.-Y.; Kalicinsky, M.; DeNardo, G.L.; DeNardo, S.J. Production of soluble ScFvs with C-terminal-free thiol for site-specific conjugation or stable dimeric ScFvs on demand. Bioconjug. Chem. 2003, 15, 16-26.
    • (2003) Bioconjug. Chem. , vol.15 , pp. 16-26
    • Albrecht, H.1    Burke, P.A.2    Natarajan, A.3    Xiong, C.-Y.4    Kalicinsky, M.5    Denardo, G.L.6    Denardo, S.J.7
  • 30
    • 70350568907 scopus 로고    scopus 로고
    • Engineering of cysteine residues leads to improved production of a human dipeptidase enzyme in E. coli
    • O'Dwyer, R.; Razzaque, R.; Hu, X.; Hollingshead, S.K.; Wall, J.G. Engineering of cysteine residues leads to improved production of a human dipeptidase enzyme in E. coli. Appl. Biochem. Biotechnol. 2009, 159, 178-190.
    • (2009) Appl. Biochem. Biotechnol. , vol.159 , pp. 178-190
    • O'Dwyer, R.1    Razzaque, R.2    Hu, X.3    Hollingshead, S.K.4    Wall, J.G.5
  • 31
    • 43449097187 scopus 로고    scopus 로고
    • Expression, purification and crystallization of cysteine-rich human protein muskelin in Escherichia coli
    • Kiedzierska, A.; Czepczynska, H.; Smietana, K.; Otlewski, J. Expression, purification and crystallization of cysteine-rich human protein muskelin in Escherichia coli. Protein Expr. Purif. 2008, 60, 82-88.
    • (2008) Protein Expr. Purif. , vol.60 , pp. 82-88
    • Kiedzierska, A.1    Czepczynska, H.2    Smietana, K.3    Otlewski, J.4
  • 32
  • 33
    • 0031042551 scopus 로고    scopus 로고
    • Optimization of Conditions for formation and analysis of Anti-CD19 FVS191 single-chain Fv homodimer (scFv')2
    • Wang, D.; Berven, E.; Li, Q.; Uckun, F.; Kersey, J.H. Optimization of Conditions for formation and analysis of Anti-CD19 FVS191 single-chain Fv homodimer (scFv')2. Bioconjug. Chem. 1997, 8, 64-70.
    • (1997) Bioconjug. Chem. , vol.8 , pp. 64-70
    • Wang, D.1    Berven, E.2    Li, Q.3    Uckun, F.4    Kersey, J.H.5
  • 34
    • 42949153379 scopus 로고    scopus 로고
    • Development of a high-affinity anti-domoic acid sheep scFv and its use in detection of the toxin in shellfish
    • Shaw, I.; O'Reilly, A.; Charleton, M.; Kane, M. Development of a high-affinity anti-domoic acid sheep scFv and its use in detection of the toxin in shellfish. Anal. Chem. 2008, 80, 3205-3212.
    • (2008) Anal. Chem. , vol.80 , pp. 3205-3212
    • Shaw, I.1    O'Reilly, A.2    Charleton, M.3    Kane, M.4
  • 35
    • 84866256053 scopus 로고    scopus 로고
    • Interfacial recognition of human prostate-specific antigen by immobilized monoclonal antibody: Effects of solution conditions and surface chemistry
    • Zhao, X.; Pan, F.; Garcia-Gancedo, L.; Flewitt, A.J.; Ashley, G.M.; Luo, J.; Lu, J.R. Interfacial recognition of human prostate-specific antigen by immobilized monoclonal antibody: Effects of solution conditions and surface chemistry. J. R. Soc. Interface 2012, 9, 2457-2467.
    • (2012) J. R. Soc. Interface , vol.9 , pp. 2457-2467
    • Zhao, X.1    Pan, F.2    Garcia-Gancedo, L.3    Flewitt, A.J.4    Ashley, G.M.5    Luo, J.6    Lu, J.R.7
  • 36
    • 0036300818 scopus 로고    scopus 로고
    • Intradomain disulfide bonds impede formation of the alternatively folded state of antibody chains
    • Buchner, J.; Rudolph, R.; Lilie, H. Intradomain disulfide bonds impede formation of the alternatively folded state of antibody chains. J. Mol. Biol. 2002, 318, 829-836.
    • (2002) J. Mol. Biol. , vol.318 , pp. 829-836
    • Buchner, J.1    Rudolph, R.2    Lilie, H.3
  • 37
    • 84864429708 scopus 로고    scopus 로고
    • Key factors influencing the optical detection of biomolecules by their evaporative assembly on diatom frustules
    • Yang, Y.; Addai-Mensah, J.; Losic, D. Key factors influencing the optical detection of biomolecules by their evaporative assembly on diatom frustules. J. Mater. Sci. 2012, 47, 6315.
    • (2012) J. Mater. Sci. , vol.47 , pp. 6315
    • Yang, Y.1    Addai-Mensah, J.2    Losic, D.3
  • 39
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A.; Kucukural, A.; Zhang, Y. I-TASSER: A unified platform for automated protein structure and function prediction. Nat. Protoc. 2010, 5, 725-738.
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 40
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. I-TASSER server for protein 3D structure prediction. BMC Bioinforma. 2008, 9, 40.
    • (2008) BMC Bioinforma , vol.9 , pp. 40
    • Zhang, Y.1
  • 41
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N.; Peitsch, M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 1997, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.