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Volumn 97, Issue 2, 2013, Pages 761-766

High production of llama variable heavy-chain antibody fragment (VHH) fused to various reader proteins by Aspergillus oryzae

Author keywords

Aspergillus oryzae; His tagged protein; Llama variable heavy chain antibody fragment (VHH); Overproduction; Reader protein

Indexed keywords

ASPERGILLUS ORYZAE; CULTURE MEDIUM; FUSION PROTEINS; GLUCOAMYLASE; HEAVY-CHAIN ANTIBODY FRAGMENTS; HIGH MOLECULAR WEIGHT; HIS-TAG; HIS-TAGGED PROTEINS; HUMAN CHORIONIC GONADOTROPINS; N-TERMINALS; OVERPRODUCTION; POTASSIUM PHOSPHATE; PRODUCTION OF; SDS-PAGE ANALYSIS; TETRAMETHYLBENZIDINE;

EID: 84873992167     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4211-0     Document Type: Article
Times cited : (12)

References (27)
  • 2
    • 0031307441 scopus 로고    scopus 로고
    • The molecular biology of secreted enzyme production by fungi
    • 10.3109/07388559709146616 1:CAS:528:DyaK2sXotVCku78%3D
    • Archer DB, Peberdy JF (1997) The molecular biology of secreted enzyme production by fungi. Crit Rev Biotechnol 17:273-306
    • (1997) Crit Rev Biotechnol , vol.17 , pp. 273-306
    • Archer, D.B.1    Peberdy, J.F.2
  • 3
    • 82355182085 scopus 로고    scopus 로고
    • Isolation of a novel promoter for efficient protein expression by Aspergillus oryzae in solid-state culture
    • 10.1007/s00253-011-3446-5 1:CAS:528:DC%2BC3MXht1yhur3M
    • Bando H, Hisada H, Ishida H, Hata Y, Katakura Y, Kondo A (2011) Isolation of a novel promoter for efficient protein expression by Aspergillus oryzae in solid-state culture. Appl Microbiol Biotechnol 92:561-569
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 561-569
    • Bando, H.1    Hisada, H.2    Ishida, H.3    Hata, Y.4    Katakura, Y.5    Kondo, A.6
  • 4
    • 77951252446 scopus 로고    scopus 로고
    • A highly sensitive caffeine immunoassay based on a monoclonal antibody
    • 10.1007/s00216-010-3506-1 1:CAS:528:DC%2BC3cXhvFGmtr8%3D
    • Carvalho JJ, Weller MG, Panne U, Schneider RJ (2010) A highly sensitive caffeine immunoassay based on a monoclonal antibody. Anal Bioanal Chem 396:2617-2628
    • (2010) Anal Bioanal Chem , vol.396 , pp. 2617-2628
    • Carvalho, J.J.1    Weller, M.G.2    Panne, U.3    Schneider, R.J.4
  • 5
    • 0029563040 scopus 로고
    • A sensitive enzyme-linked immunosorbent assay used for quantitation of epidermal growth factor receptor protein in head and neck carcinomas: Evaluation, interpretations and limitations
    • 10.1038/bjc.1995.534 1:CAS:528:DyaK28XhsVOitLs%3D
    • Christensen ME, Engbaek F, Therkildsen MH, Bretlau P, Nexø E (1995) A sensitive enzyme-linked immunosorbent assay used for quantitation of epidermal growth factor receptor protein in head and neck carcinomas: evaluation, interpretations and limitations. Br J Cancer 72:1487-1493
    • (1995) Br J Cancer , vol.72 , pp. 1487-1493
    • Christensen, M.E.1    Engbaek, F.2    Therkildsen, M.H.3    Bretlau, P.4    Nexø, E.5
  • 6
    • 80052341911 scopus 로고    scopus 로고
    • A case of convergence: Why did a simple alternative to canonical antibodies arise in sharks and camels?
    • 10.1371/journal.pbio.1001120 1:CAS:528:DC%2BC3MXhtV2mtLfO
    • Flajnik MF, Deschacht N, Muyldermans S (2011) A case of convergence: why did a simple alternative to canonical antibodies arise in sharks and camels? PLoS Biol 9:e1001120
    • (2011) PLoS Biol , vol.9 , pp. 1001120
    • Flajnik, M.F.1    Deschacht, N.2    Muyldermans, S.3
  • 7
    • 85004562322 scopus 로고
    • Integrative transformation of Aspergillus oryzae with a plasmid containing the Aspergillus nidulans argB gene
    • 10.1271/bbb1961.51.2549 1:CAS:528:DyaL2sXls12qtrc%3D
    • Gomi K, Iimura Y, Hara S (1987) Integrative transformation of Aspergillus oryzae with a plasmid containing the Aspergillus nidulans argB gene. Agric Biol Chem 51:2549-2555
    • (1987) Agric Biol Chem , vol.51 , pp. 2549-2555
    • Gomi, K.1    Iimura, Y.2    Hara, S.3
  • 8
    • 21644434170 scopus 로고    scopus 로고
    • Cellular quality control screening to identify amino acid pairs for substituting the disulfide bonds in immunoglobulin fold domains
    • 10.1074/jbc.M503963200 1:CAS:528:DC%2BD2MXlsFyqs7o%3D
    • Hagihara Y, Matsuda T, Yumoto N (2005) Cellular quality control screening to identify amino acid pairs for substituting the disulfide bonds in immunoglobulin fold domains. J Biol Chem 280:24752-24758
    • (2005) J Biol Chem , vol.280 , pp. 24752-24758
    • Hagihara, Y.1    Matsuda, T.2    Yumoto, N.3
  • 9
    • 37549067001 scopus 로고    scopus 로고
    • Stabilization of an immunoglobulin fold domain by an engineered disulfide bond at the buried hydrophobic region
    • 10.1074/jbc.M707078200 1:CAS:528:DC%2BD2sXhsVSgtrvP
    • Hagihara Y, Mine S, Uegaki K (2007) Stabilization of an immunoglobulin fold domain by an engineered disulfide bond at the buried hydrophobic region. J Biol Chem 282:36489-36495
    • (2007) J Biol Chem , vol.282 , pp. 36489-36495
    • Hagihara, Y.1    Mine, S.2    Uegaki, K.3
  • 11
    • 77956037495 scopus 로고    scopus 로고
    • Purification and characterization of termite endogenous β-1,4-endoglucanases produced in Aspergillus oryzae
    • Hirayama K, Watanabe H, Tokuda G, Kitamoto K, Arioka M (2010) Purification and characterization of termite endogenous β-1,4- endoglucanases produced in Aspergillus oryzae. Biosci Biotechnol Biochem 74:1680-1686
    • (2010) Biosci Biotechnol Biochem , vol.74 , pp. 1680-1686
    • Hirayama, K.1    Watanabe, H.2    Tokuda, G.3    Kitamoto, K.4    Arioka, M.5
  • 12
    • 82355161910 scopus 로고    scopus 로고
    • Engineered single-domain antibodies with high protease resistance and thermal stability
    • 10.1371/journal.pone.0028218 10.1371/journal.pone.0028218 1:CAS:528:DC%2BC3MXhs1Ggtb3E
    • Hussack G, Hirama T, Ding W, MacKenzie R, Tanha J (2011) Engineered single-domain antibodies with high protease resistance and thermal stability. PLoS One 6:e28218. doi: 10.1371/journal.pone.0028218
    • (2011) PLoS One , vol.6 , pp. 28218
    • Hussack, G.1    Hirama, T.2    Ding, W.3    MacKenzie, R.4    Tanha, J.5
  • 17
    • 79951771512 scopus 로고    scopus 로고
    • Aspergillus as a multi-purpose cell factory: Current status and perspectives
    • 10.1007/s10529-010-0473-8 1:CAS:528:DC%2BC3MXitFGntL4%3D
    • Meyer V, Wu B, Ram AF (2011) Aspergillus as a multi-purpose cell factory: current status and perspectives. Biotechnol Lett 33:469-476
    • (2011) Biotechnol Lett , vol.33 , pp. 469-476
    • Meyer, V.1    Wu, B.2    Ram, A.F.3
  • 18
    • 0035715877 scopus 로고    scopus 로고
    • Single domain camel antibodies: Current status
    • 1:CAS:528:DC%2BD3MXmt1Whs70%3D
    • Muyldermans S (2001) Single domain camel antibodies: current status. J Biotechnol 74:277-302
    • (2001) J Biotechnol , vol.74 , pp. 277-302
    • Muyldermans, S.1
  • 19
    • 0038166958 scopus 로고    scopus 로고
    • Toxicity, pharmacokinetics, and dose-finding study of repetitive treatment with the humanized anti-interleukin 6 receptor antibody MRA in rheumatoid arthritis. Phase I/II clinical study
    • 1:CAS:528:DC%2BD3sXmtFSqs7Y%3D
    • Nishimoto N, Yoshizaki K, Maeda K, Kuritani T, Deguchi H, Sato B, Imai N, Suemura M, Kakehi T, Takagi N, Kishimoto T (2003) Toxicity, pharmacokinetics, and dose-finding study of repetitive treatment with the humanized anti-interleukin 6 receptor antibody MRA in rheumatoid arthritis. Phase I/II clinical study. J Rheumatol 30:1426-1435
    • (2003) J Rheumatol , vol.30 , pp. 1426-1435
    • Nishimoto, N.1    Yoshizaki, K.2    Maeda, K.3    Kuritani, T.4    Deguchi, H.5    Sato, B.6    Imai, N.7    Suemura, M.8    Kakehi, T.9    Takagi, N.10    Kishimoto, T.11
  • 20
    • 77950848197 scopus 로고    scopus 로고
    • Review of ustekinumab, an interleukin-12 and interleukin-23 inhibitor used for the treatment of plaque psoriasis
    • Nora K, Jason E, Mark L (2010) Review of ustekinumab, an interleukin-12 and interleukin-23 inhibitor used for the treatment of plaque psoriasis. Ther Clin Risk Manag 6:123-141
    • (2010) Ther Clin Risk Manag , vol.6 , pp. 123-141
    • Nora, K.1    Jason, E.2    Mark, L.3
  • 21
    • 82455210919 scopus 로고    scopus 로고
    • A carrier fusion significantly induces unfolded protein response in heterologous protein production by Aspergillus oryzae
    • 10.1007/s00253-011-3487-9 1:CAS:528:DC%2BC3MXhsFegurbK
    • Ohno A, Maruyama JI, Nemoto T, Arioka M, Kitamoto K (2011) A carrier fusion significantly induces unfolded protein response in heterologous protein production by Aspergillus oryzae. Appl Microbiol Biotechnol 92:1197-1206
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 1197-1206
    • Ohno, A.1    Maruyama, J.I.2    Nemoto, T.3    Arioka, M.4    Kitamoto, K.5
  • 22
    • 84873999138 scopus 로고    scopus 로고
    • Expression, purification and development of neutralizing antibodies from synthetic BoNT/B LC and its application in detection of botulinum toxin serotype B
    • Ponmariappan S, Jain S, Sijoria R, Tomar A, Kumar O (2011) Expression, purification and development of neutralizing antibodies from synthetic BoNT/B LC and its application in detection of botulinum toxin serotype B. Protein Pept Lett. PMID 21933129
    • (2011) Protein Pept Lett. PMID , pp. 21933129
    • Ponmariappan, S.1    Jain, S.2    Sijoria, R.3    Tomar, A.4    Kumar, O.5
  • 23
    • 77249093008 scopus 로고    scopus 로고
    • A novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger
    • 10.1007/s00253-009-2252-9 1:CAS:528:DC%2BC3cXit1amt7w%3D
    • Roth AH, Dersch P (2010) A novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger. Appl Microbiol Biotechnol 86:659-670
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 659-670
    • Roth, A.H.1    Dersch, P.2
  • 24
    • 82355183585 scopus 로고    scopus 로고
    • Identification of potential cell wall component that allows Taka-amylase A adsorption in submerged cultures of Aspergillus oryzae
    • 10.1007/s00253-011-3422-0 1:CAS:528:DC%2BC3MXhsVelt7bJ
    • Sato H, Toyoshima Y, Shintani T, Gomi K (2011) Identification of potential cell wall component that allows Taka-amylase A adsorption in submerged cultures of Aspergillus oryzae. Appl Microbiol Biotechnol 92:961-969
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 961-969
    • Sato, H.1    Toyoshima, Y.2    Shintani, T.3    Gomi, K.4
  • 25
    • 8744279988 scopus 로고    scopus 로고
    • Omalizumab: Efficacy in allergic disease
    • 1:STN:280:DC%2BD2crjs12hsw%3D%3D
    • Spector S (2004) Omalizumab: efficacy in allergic disease. Panminerva Med 46:141-148
    • (2004) Panminerva Med , vol.46 , pp. 141-148
    • Spector, S.1
  • 26
    • 70349931648 scopus 로고    scopus 로고
    • Development of a novel immunoaffinity column for aflatoxin analysis using an organic solvent-tolerant monoclonal antibody
    • 10.1021/jf901826a 1:CAS:528:DC%2BD1MXhtFWhsb3F
    • Uchigashima M, Saigusa M, Yamashita H, Miyake S, Fujita K, Nakajima M, Nishijima M (2009) Development of a novel immunoaffinity column for aflatoxin analysis using an organic solvent-tolerant monoclonal antibody. J Agric Food Chem 57:8728-8734
    • (2009) J Agric Food Chem , vol.57 , pp. 8728-8734
    • Uchigashima, M.1    Saigusa, M.2    Yamashita, H.3    Miyake, S.4    Fujita, K.5    Nakajima, M.6    Nishijima, M.7
  • 27
    • 79251569555 scopus 로고    scopus 로고
    • Disruption of ten protease genes in the filamentous fungus Aspergillus oryzae highly improves production of heterologous proteins
    • 10.1007/s00253-010-2937-0 1:CAS:528:DC%2BC3MXnsVWktg%3D%3D
    • Yoon J, Maruyama J, Kitamoto K (2011) Disruption of ten protease genes in the filamentous fungus Aspergillus oryzae highly improves production of heterologous proteins. Appl Microbiol Biotechnol 89:747-759
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 747-759
    • Yoon, J.1    Maruyama, J.2    Kitamoto, K.3


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