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Volumn 91, Issue 1, 2013, Pages 42-48

High yield purification of nanobodies from the periplasm of E. coli as fusions with the maltose binding protein

Author keywords

Affinity chromatography; E. coli; MBP; Nanobodies; Recombinant antibodies

Indexed keywords

ANTIGEN; ESCHERICHIA COLI PROTEIN; HIS HIS HIS HIS HIS HIS; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; HYBRID PROTEIN; MALE PROTEIN, E COLI; NANOBODY; OLIGOPEPTIDE; PERIPLASMIC BINDING PROTEIN;

EID: 84880897111     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.07.001     Document Type: Article
Times cited : (49)

References (34)
  • 3
    • 84934444785 scopus 로고    scopus 로고
    • Introduction to heavy chain antibodies and derived nanobodies
    • C. Vincke, and S. Muyldermans Introduction to heavy chain antibodies and derived nanobodies Methods Mol. Biol. 911 2012 15 26
    • (2012) Methods Mol. Biol. , vol.911 , pp. 15-26
    • Vincke, C.1    Muyldermans, S.2
  • 4
    • 0035312546 scopus 로고    scopus 로고
    • Recognition of antigens by single-domain antibody fragments: The superfluous luxury of paired domains
    • DOI 10.1016/S0968-0004(01)01790-X, PII S096800040101790X
    • S. Muyldermans, C. Cambillau, and L. Wyns Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains Trends Biochem. Sci. 26 2001 230 235 (Pubitemid 32289241)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.4 , pp. 230-235
    • Muyldermans, S.1    Cambillau, C.2    Wyns, L.3
  • 5
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: Natural single-domain antibodies
    • S. Muyldermans Nanobodies: natural single-domain antibodies Annu. Rev. Biochem 82 2013 775 797
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 13
    • 84857642791 scopus 로고    scopus 로고
    • Phagemid vectors for phage display: Properties, characteristics and construction
    • H. Qi, H. Lu, H.-J. Qiu, V. Petrenko, and A. Liu Phagemid vectors for phage display: properties, characteristics and construction J. Mol. Biol. 417 2012 129 143
    • (2012) J. Mol. Biol. , vol.417 , pp. 129-143
    • Qi, H.1    Lu, H.2    Qiu, H.-J.3    Petrenko, V.4    Liu, A.5
  • 14
    • 44049095603 scopus 로고    scopus 로고
    • SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. Coli
    • DOI 10.1016/j.nbt.2008.01.001, PII S1871678408000022
    • H. Thie, T. Schirrmann, M. Paschke, S. Dubel, and M. Hust SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. coli New Biotechnol. 25 2008 49 54 (Pubitemid 351713600)
    • (2008) New Biotechnology , vol.25 , Issue.1 , pp. 49-54
    • Thie, H.1    Schirrmann, T.2    Paschke, M.3    Dubel, S.4    Hust, M.5
  • 15
    • 84873291177 scopus 로고    scopus 로고
    • Immunoglobulin domains in Escherichia coli and other enterobacteria: From pathogenesis to applications in antibody technologies
    • G. Bodelón, C. Palomino, and L.A. Fernández Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies FEMS Microbiol. Rev. 37 2013 204 250
    • (2013) FEMS Microbiol. Rev. , vol.37 , pp. 204-250
    • Bodelón, G.1    Palomino, C.2    Fernández, L.A.3
  • 16
    • 79952473873 scopus 로고    scopus 로고
    • Periplasmic chaperones used to enhance functional secretion of proteins in E. Coli
    • M. Schlapschy, and A. Skerra Periplasmic chaperones used to enhance functional secretion of proteins in E. coli Methods Mol. Biol. 705 2011 211 224
    • (2011) Methods Mol. Biol. , vol.705 , pp. 211-224
    • Schlapschy, M.1    Skerra, A.2
  • 19
    • 0345195967 scopus 로고    scopus 로고
    • Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment
    • DOI 10.1021/bi9810407
    • K.M. Arndt, K.M. Muller, and A. Plückthun Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment Biochemistry 37 1998 12918 12926 (Pubitemid 28433525)
    • (1998) Biochemistry , vol.37 , Issue.37 , pp. 12918-12926
    • Arndt, K.M.1    Muller, K.M.2    Pluckthun, A.3
  • 20
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • DOI 10.1006/jmbi.2000.4265
    • A. Wörn, and A. Plückthun Stability engineering of antibody single-chain Fv fragments J. Mol. Biol. 305 2001 989 1010 (Pubitemid 33028934)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.5 , pp. 989-1010
    • Worn, A.1    Pluckthun, A.2
  • 22
    • 0021252896 scopus 로고
    • Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12
    • P. Duplay, H. Bedouelle, A. Fowler, I. Zabin, W. Saurin, and M. Hofnung Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12 J. Biol. Chem. 259 1984 10606 10613 (Pubitemid 14064164)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.16 , pp. 10606-10613
    • Duplay, P.1    Bedouelle, H.2    Fowler, A.3
  • 23
    • 0023959219 scopus 로고
    • Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space
    • H. Bedouelle, and P. Duplay Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space Eur. J. Biochem. 171 1988 541 549
    • (1988) Eur. J. Biochem. , vol.171 , pp. 541-549
    • Bedouelle, H.1    Duplay, P.2
  • 24
    • 0028354878 scopus 로고
    • Characterization of the C-terminal domains of intimin-like proteins of enteropathogenic and enterohemorrhagic Escherichia coli, Citrobacter freundii, and Hafnia alvei
    • G. Frankel, D.C. Candy, P. Everest, and G. Dougan Characterization of the C-terminal domains of intimin-like proteins of enteropathogenic and enterohemorrhagic Escherichia coli, Citrobacter freundii, and Hafnia alvei Infect. Immun. 62 1994 1835 1842 (Pubitemid 24136984)
    • (1994) Infection and Immunity , vol.62 , Issue.5 , pp. 1835-1842
    • Frankel, G.1    Candy, D.C.A.2    Everest, P.3    Dougan, G.4
  • 25
    • 0034142296 scopus 로고    scopus 로고
    • Improved expression characteristics of single-chain Fv fragments when fused downstream of the Escherichia coli maltose-binding protein or upstream of a single immunoglobulin-constant domain
    • DOI 10.1006/prep.1999.1164
    • A. Hayhurst Improved expression characteristics of single-chain Fv fragments when fused downstream of the Escherichia coli maltose-binding protein or upstream of a single immunoglobulin-constant domain Protein Expr. Purif. 18 2000 1 10 (Pubitemid 30097767)
    • (2000) Protein Expression and Purification , vol.18 , Issue.1 , pp. 1-10
    • Hayhurst, A.1
  • 26
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies
    • DOI 10.1006/jmbi.2001.4914
    • H. Bach, Y. Mazor, S. Shaky, A. Shoham-Lev, Y. Berdichevsky, D.L. Gutnick, and I. Benhar Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies J. Mol. Biol. 312 2001 79 93 (Pubitemid 32835677)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.1 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3    Shoham-Lev, A.4    Berdichevsky, Y.5    Gutnick, D.L.6    Benhar, I.7
  • 27
    • 0001890686 scopus 로고    scopus 로고
    • Construction and screening of antibody display libraries
    • B.K. Kay, J. Winter, J. McCafferty, Academic Press, Inc. San Diego, California
    • J. McCafferty, and K.S. Johnson Construction and screening of antibody display libraries B.K. Kay, J. Winter, J. McCafferty, Phage display of peptides and proteins 1996 Academic Press, Inc. San Diego, California 79 111
    • (1996) Phage Display of Peptides and Proteins , pp. 79-111
    • McCafferty, J.1    Johnson, K.S.2
  • 29
    • 0028143313 scopus 로고
    • Construction and characterization of a set of E. Coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins
    • H.J. Meerman, and G. Georgiou Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins Nat. Biotech. 12 1994 1107 1110
    • (1994) Nat. Biotech. , vol.12 , pp. 1107-1110
    • Meerman, H.J.1    Georgiou, G.2
  • 30
    • 0036296338 scopus 로고    scopus 로고
    • Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli
    • DOI 10.1016/S0022-2836(02)00405-9
    • P. Jurado, D. Ritz, J. Beckwith, V. de Lorenzo, and L.A. Fernández Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli J. Mol. Biol. 320 2002 1 10 (Pubitemid 34722230)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.1 , pp. 1-10
    • Jurado, P.1    Ritz, D.2    Beckwith, J.3    De Lorenzo, V.4    Fernandez, L.A.5
  • 32
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • DOI 10.1016/S0014-5793(97)01062-4, PII S0014579397010624
    • M. Arbabi Ghahroudi, A. Desmyter, L. Wyns, R. Hamers, and S. Muyldermans Selection and identification of single domain antibody fragments from camel heavy-chain antibodies FEBS Lett. 414 1997 521 526 (Pubitemid 27390659)
    • (1997) FEBS Letters , vol.414 , Issue.3 , pp. 521-526
    • Arbabi Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 33
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • F.W. Studier, and B.A. Moffatt Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes J. Mol. Biol. 189 1986 113 130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 34
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • DOI 10.1038/nbt1126, PII N1126
    • H.R. Hoogenboom Selecting and screening recombinant antibody libraries Nat. Biotechnol. 23 2005 1105 1116 (Pubitemid 41486392)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1105-1116
    • Hoogenboom, H.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.