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Volumn 146, Issue 1-2, 2010, Pages 1-8

SUMO fusion facilitates expression and purification of garlic leaf lectin but modifies some of its properties

Author keywords

ASAL; Glycan array; Haemagglutination; Insecticidal protein; Lectin; Sugar specificity; SUMO

Indexed keywords

ALLIUM SATIVUM; ARRAY ANALYSIS; ASAL; CARBOHYDRATE BINDING; E. COLI; FUSION PROTEINS; HOMODIMERS; IMMOBILIZED METAL AFFINITY COLUMNS; INCLUSION BODIES; INSECTICIDAL PROTEIN; N-TERMINALS; OVER-EXPRESSION; SMALL UBIQUITIN-RELATED MODIFIERS; STERIC HINDRANCES; TRANSGENIC PLANTS;

EID: 77249104438     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2010.01.013     Document Type: Article
Times cited : (29)

References (35)
  • 1
    • 0035937095 scopus 로고    scopus 로고
    • On the stringent requirement of mannosyl substitution in mannooligosaccharides for the recognition by garlic (Allium sativum) Lectin
    • Bachhawat K., Thomas C.J., Amutha B., Krishnasastry M.V., Khan M.I., and Surolia A. On the stringent requirement of mannosyl substitution in mannooligosaccharides for the recognition by garlic (Allium sativum) Lectin. J. Biol. Chem. 276 (2001) 5541-5546
    • (2001) J. Biol. Chem. , vol.276 , pp. 5541-5546
    • Bachhawat, K.1    Thomas, C.J.2    Amutha, B.3    Krishnasastry, M.V.4    Khan, M.I.5    Surolia, A.6
  • 2
    • 0034778904 scopus 로고    scopus 로고
    • Binding of garlic (Allium sativum) leaf lectin to the gut receptors of homopteran pests is correlated to its insecticidal activity
    • Bandyopadhyay S., Roy A., and Das S. Binding of garlic (Allium sativum) leaf lectin to the gut receptors of homopteran pests is correlated to its insecticidal activity. Plant Sci. 161 (2001) 1025-1033
    • (2001) Plant Sci. , vol.161 , pp. 1025-1033
    • Bandyopadhyay, S.1    Roy, A.2    Das, S.3
  • 5
    • 0032489373 scopus 로고    scopus 로고
    • Garlic (Allium sativum) Lectins bind to high mannose oligosaccharide chains
    • Dam T.K., Bachhawat K., Rani P.G., and Surolia A. Garlic (Allium sativum) Lectins bind to high mannose oligosaccharide chains. J. Biol. Chem. 273 (1998) 5528-5535
    • (1998) J. Biol. Chem. , vol.273 , pp. 5528-5535
    • Dam, T.K.1    Bachhawat, K.2    Rani, P.G.3    Surolia, A.4
  • 6
    • 0035013453 scopus 로고    scopus 로고
    • In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae; mechanisms of insecticidal action
    • Fitches E., Woodhouse S.D., Edwards J.P., and Gatehouse J.A. In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae; mechanisms of insecticidal action. J. Insect Physiol. 47 (2001) 777-787
    • (2001) J. Insect Physiol. , vol.47 , pp. 777-787
    • Fitches, E.1    Woodhouse, S.D.2    Edwards, J.P.3    Gatehouse, J.A.4
  • 8
    • 0031922529 scopus 로고    scopus 로고
    • Effect of wheat germ agglutinin on formation and structure of the peritrophic membrane in European corn borer (Ostrina nubilalis) larvae
    • Harper S.M., Hopkins T.L., and Czapala T.H. Effect of wheat germ agglutinin on formation and structure of the peritrophic membrane in European corn borer (Ostrina nubilalis) larvae. Tissue Cell. 30 (1998) 166-176
    • (1998) Tissue Cell. , vol.30 , pp. 166-176
    • Harper, S.M.1    Hopkins, T.L.2    Czapala, T.H.3
  • 9
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson E.S., and Blobel G. Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J. Cell Biol. 147 (1999) 981-994
    • (1999) J. Cell Biol. , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 10
    • 0036204976 scopus 로고    scopus 로고
    • Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli
    • Jonasson P., Liljeqvist S., Nygren P.A., and Ståhl S. Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli. Biotechnol. Appl. Biochem. 35 (2002) 91-105
    • (2002) Biotechnol. Appl. Biochem. , vol.35 , pp. 91-105
    • Jonasson, P.1    Liljeqvist, S.2    Nygren, P.A.3    Ståhl, S.4
  • 12
    • 29144477680 scopus 로고    scopus 로고
    • Functional GNA expressed in Escherichia coli with high efficiency and its effect on Ceratovacuna lanigera Zehntner
    • Luo S., Zhangsun D., and Tang K. Functional GNA expressed in Escherichia coli with high efficiency and its effect on Ceratovacuna lanigera Zehntner. Appl. Microbial. Biotechnol. 69 (2005) 184-191
    • (2005) Appl. Microbial. Biotechnol. , vol.69 , pp. 184-191
    • Luo, S.1    Zhangsun, D.2    Tang, K.3
  • 13
    • 16644393420 scopus 로고    scopus 로고
    • Identification of receptors responsible for binding of the mannose specific lectin to the gut epithelial membrane of the target insects
    • Majumder P., Banerjee S., and Das S. Identification of receptors responsible for binding of the mannose specific lectin to the gut epithelial membrane of the target insects. Glycoconj. J. 20 (2004) 525-530
    • (2004) Glycoconj. J. , vol.20 , pp. 525-530
    • Majumder, P.1    Banerjee, S.2    Das, S.3
  • 15
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO
    • Marblestone J.G., Edavettal S.C., Lim Y., Lim P., Zuo X., and Butt T.R. Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO. Protein Sci. 15 (2006) 182-189
    • (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
  • 16
    • 0033584950 scopus 로고    scopus 로고
    • Xanthosoma sagittifolium tubers contain a lectin with two different types of carbohydrate-binding sites
    • Mo H., Rice K.G., Evers D.L., Winter H.C., Peumans W.J., Van Damme E.J.M., and Goldstein I.J. Xanthosoma sagittifolium tubers contain a lectin with two different types of carbohydrate-binding sites. J. Biol. Chem. 274 (1999) 33300-33305
    • (1999) J. Biol. Chem. , vol.274 , pp. 33300-33305
    • Mo, H.1    Rice, K.G.2    Evers, D.L.3    Winter, H.C.4    Peumans, W.J.5    Van Damme, E.J.M.6    Goldstein, I.J.7
  • 17
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova E., and Lima C.D. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell. 5 (2000) 865-876
    • (2000) Mol. Cell. , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 18
    • 0031259833 scopus 로고    scopus 로고
    • Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins
    • Nilsson J., Stahl S., and Lundeberg J. Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins. Protein Expr. Purif. 11 (1997) 1-16
    • (1997) Protein Expr. Purif. , vol.11 , pp. 1-16
    • Nilsson, J.1    Stahl, S.2    Lundeberg, J.3
  • 20
    • 37549068959 scopus 로고    scopus 로고
    • Ectopically expressed leaf and bulb lectins from garlic (Allium sativum L.) protect transgenic tobacco plants against cotton leaf worm (Spodoptera littoralis)
    • Sadeghi A., Smagghe G., Broeders S., Hernalsteens J.P., DeGreve H., Peumans W.J., and VanDamme E.J. Ectopically expressed leaf and bulb lectins from garlic (Allium sativum L.) protect transgenic tobacco plants against cotton leaf worm (Spodoptera littoralis). Transgenic Res. 17 (2008) 9-18
    • (2008) Transgenic Res. , vol.17 , pp. 9-18
    • Sadeghi, A.1    Smagghe, G.2    Broeders, S.3    Hernalsteens, J.P.4    DeGreve, H.5    Peumans, W.J.6    VanDamme, E.J.7
  • 21
    • 33750440536 scopus 로고    scopus 로고
    • A novel approach for developing resistance in rice against phloem limited viruses by antagonizing the phloem feeding hemipteran vectors
    • Saha P., Dasgupta I., and Das S. A novel approach for developing resistance in rice against phloem limited viruses by antagonizing the phloem feeding hemipteran vectors. Plant Mol. Biol. 62 (2006) 735-752
    • (2006) Plant Mol. Biol. , vol.62 , pp. 735-752
    • Saha, P.1    Dasgupta, I.2    Das, S.3
  • 22
    • 12544252993 scopus 로고    scopus 로고
    • Binding of the insecticidal lectin concanavalin A in pea aphid, Acyrthosiphon pisum (Harris) and induced effects on the structure of midgut epithelial cells
    • Sauvion N., Nardon C., Febvay G., Gatehouse A.M.R., and Rahbe Y. Binding of the insecticidal lectin concanavalin A in pea aphid, Acyrthosiphon pisum (Harris) and induced effects on the structure of midgut epithelial cells. J. Insect Physiol. 50 (2004) 1137-1150
    • (2004) J. Insect Physiol. , vol.50 , pp. 1137-1150
    • Sauvion, N.1    Nardon, C.2    Febvay, G.3    Gatehouse, A.M.R.4    Rahbe, Y.5
  • 23
    • 0030317426 scopus 로고    scopus 로고
    • A facile method for the construction of synthetic genes
    • Singh P.K., Sarangi B.K., and Tuli R. A facile method for the construction of synthetic genes. J. Biosci. 21 (1996) 735-741
    • (1996) J. Biosci. , vol.21 , pp. 735-741
    • Singh, P.K.1    Sarangi, B.K.2    Tuli, R.3
  • 25
    • 0031282638 scopus 로고    scopus 로고
    • Isolation, characterization and molecular cloning of a leaf-specific lectin from ramsons (Allium ursinum L.)
    • Smeets K., Van Damme E.J.M., Van Leuven F., and Peumans W.J. Isolation, characterization and molecular cloning of a leaf-specific lectin from ramsons (Allium ursinum L.). Plant Mol. Biol. 35 (1997) 531-535
    • (1997) Plant Mol. Biol. , vol.35 , pp. 531-535
    • Smeets, K.1    Van Damme, E.J.M.2    Van Leuven, F.3    Peumans, W.J.4
  • 26
    • 0030942938 scopus 로고    scopus 로고
    • Isolation, characterization and molecular cloning of the mannose-binding lectins from leaves and roots of garlic (Allium sativum L.)
    • Smeets K., Van Damme E.J.M., Verhaert P., Barre A., Rouge P., Van Leuven F., and Peumans W.J. Isolation, characterization and molecular cloning of the mannose-binding lectins from leaves and roots of garlic (Allium sativum L.). Plant Mol. Biol. 33 (1997) 223-234
    • (1997) Plant Mol. Biol. , vol.33 , pp. 223-234
    • Smeets, K.1    Van Damme, E.J.M.2    Verhaert, P.3    Barre, A.4    Rouge, P.5    Van Leuven, F.6    Peumans, W.J.7
  • 27
    • 51549108188 scopus 로고    scopus 로고
    • Functional characterization of HFR1, a high-mannose N-glycan-specific wheat lectin induced by Hessian Fly Larvae
    • Subramanyam S., Smith D.F., Clemens J.C., Webb M.A., Sardesai N., and Williams C.E. Functional characterization of HFR1, a high-mannose N-glycan-specific wheat lectin induced by Hessian Fly Larvae. Plant Physiol. 147 (2008) 1412-1426
    • (2008) Plant Physiol. , vol.147 , pp. 1412-1426
    • Subramanyam, S.1    Smith, D.F.2    Clemens, J.C.3    Webb, M.A.4    Sardesai, N.5    Williams, C.E.6
  • 28
    • 39149114403 scopus 로고    scopus 로고
    • Expression and purification of human urodilatin by small ubiquitin-related modifier fusion in Escherichia coli
    • Sun Z., Xia Z., Bi F., and Liu J.N. Expression and purification of human urodilatin by small ubiquitin-related modifier fusion in Escherichia coli. Appl. Microbiol. Biotechnol. 78 (2008) 495-502
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 495-502
    • Sun, Z.1    Xia, Z.2    Bi, F.3    Liu, J.N.4
  • 29
    • 33749036841 scopus 로고    scopus 로고
    • Cloning and expression of a mannose-binding jacalin-related lectin from leaves of Japanese Cycad (Cycas revoluta Thunb.)
    • Tomokazu H., Keiichi N., and Fumio Y. Cloning and expression of a mannose-binding jacalin-related lectin from leaves of Japanese Cycad (Cycas revoluta Thunb.). Biosci. Biotechnol. Biochem. 9 (2006) 2222-2229
    • (2006) Biosci. Biotechnol. Biochem. , vol.9 , pp. 2222-2229
    • Tomokazu, H.1    Keiichi, N.2    Fumio, Y.3
  • 32
    • 0032422738 scopus 로고    scopus 로고
    • Plant lectins: a composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles
    • Van Damme E.J.M., Peumans W.J., Barre A., and Rougé P. Plant lectins: a composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. CRC Crit. Rev. Plant Sci. 17 (1998) 575-692
    • (1998) CRC Crit. Rev. Plant Sci. , vol.17 , pp. 575-692
    • Van Damme, E.J.M.1    Peumans, W.J.2    Barre, A.3    Rougé, P.4
  • 33
    • 0026578451 scopus 로고
    • The closely related homomeric and heterodimeric mannose-binding lectins from garlic are encoded by one-domain and two-domain lectin genes, respectively
    • Van Damme E.J.M., Smeets K., Torrekens S., Van Leuven F., Goldstein I.J., and Peumans W.J. The closely related homomeric and heterodimeric mannose-binding lectins from garlic are encoded by one-domain and two-domain lectin genes, respectively. Eur. J. Biochem. 206 (1992) 413-420
    • (1992) Eur. J. Biochem. , vol.206 , pp. 413-420
    • Van Damme, E.J.M.1    Smeets, K.2    Torrekens, S.3    Van Leuven, F.4    Goldstein, I.J.5    Peumans, W.J.6
  • 34
    • 4043059351 scopus 로고    scopus 로고
    • Antinutritional properties of plant lectins
    • Vasconcelos I.M., and Oliveira J.T.A. Antinutritional properties of plant lectins. Toxicon 44 (2004) 385-403
    • (2004) Toxicon , vol.44 , pp. 385-403
    • Vasconcelos, I.M.1    Oliveira, J.T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.