메뉴 건너뛰기




Volumn 69, Issue 1, 2010, Pages 68-75

Pichia pastoris is superior to E. coli for the production of recombinant allergenic non-specific lipid-transfer proteins

Author keywords

Cor a 8; Hazelnut; Heterologous over expression; Non specific lipid transfer proteins; nsLTP; Recombinant allergen

Indexed keywords

ALLERGEN; CARRIER PROTEIN; COR A 8 ALLERGEN, CORYLUS AVELLANA; IMMUNOGLOBULIN E; LIPID TRANSFER PROTEIN; PLANT ANTIGEN; RECOMBINANT PROTEIN;

EID: 70449127064     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.08.014     Document Type: Article
Times cited : (32)

References (40)
  • 1
    • 44649174308 scopus 로고    scopus 로고
    • Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes
    • Steckelbroeck S., Ballmer-Weber B.K., and Vieths S. Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes. J. Allergy Clin. Immunol. 121 (2008) 1323-1330
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 1323-1330
    • Steckelbroeck, S.1    Ballmer-Weber, B.K.2    Vieths, S.3
  • 2
    • 8744295783 scopus 로고    scopus 로고
    • Clinical role of lipid transfer proteins in food allergy
    • Pastorello E.A., and Robino A.M. Clinical role of lipid transfer proteins in food allergy. Mol. Nutr. Food Res. 48 (2004) 356-362
    • (2004) Mol. Nutr. Food Res. , vol.48 , pp. 356-362
    • Pastorello, E.A.1    Robino, A.M.2
  • 8
    • 0141921988 scopus 로고    scopus 로고
    • Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degrees C, as demonstrated in anaphylactic patients and patients with positive double-blind, placebo-controlled food challenge results
    • Pastorello E.A., Pompei C., Pravettoni V., Farioli L., Calamari A.M., Scibilia J., Robino A.M., Conti A., Iametti S., Fortunato D., Bonomi S., and Ortolani C. Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degrees C, as demonstrated in anaphylactic patients and patients with positive double-blind, placebo-controlled food challenge results. J. Allergy Clin. Immunol. 112 (2003) 775-783
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 775-783
    • Pastorello, E.A.1    Pompei, C.2    Pravettoni, V.3    Farioli, L.4    Calamari, A.M.5    Scibilia, J.6    Robino, A.M.7    Conti, A.8    Iametti, S.9    Fortunato, D.10    Bonomi, S.11    Ortolani, C.12
  • 10
  • 13
    • 33646397302 scopus 로고    scopus 로고
    • Standardization of allergen-specific immunotherapy vaccines
    • 1vi
    • Spangfort M.D., and Larsen J.N. Standardization of allergen-specific immunotherapy vaccines. Immunol. Allergy Clin. North Am. 26 (2006) 191 1vi
    • (2006) Immunol. Allergy Clin. North Am. , vol.26 , pp. 191
    • Spangfort, M.D.1    Larsen, J.N.2
  • 17
    • 0035038558 scopus 로고    scopus 로고
    • Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy
    • Scheurer S., Pastorello E.A., Wangorsch A., Kastner M., Haustein D., and Vieths S. Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy. J. Allergy Clin. Immunol. 107 (2001) 724-731
    • (2001) J. Allergy Clin. Immunol. , vol.107 , pp. 724-731
    • Scheurer, S.1    Pastorello, E.A.2    Wangorsch, A.3    Kastner, M.4    Haustein, D.5    Vieths, S.6
  • 19
    • 0034966491 scopus 로고    scopus 로고
    • Accurate disulfide formation in Escherichia coli: overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKTI
    • Lauber T., Marx U.C., Schulz A., Kreutzmann P., Rosch P., and Hoffmann S. Accurate disulfide formation in Escherichia coli: overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKTI. Protein Expr. Purif. 22 (2001) 108-112
    • (2001) Protein Expr. Purif. , vol.22 , pp. 108-112
    • Lauber, T.1    Marx, U.C.2    Schulz, A.3    Kreutzmann, P.4    Rosch, P.5    Hoffmann, S.6
  • 20
    • 0042324336 scopus 로고    scopus 로고
    • Effect of codon optimization on expression levels of a functionally folded malaria vaccine candidate in prokaryotic and eukaryotic expression systems
    • Yadava A., and Ockenhouse C.F. Effect of codon optimization on expression levels of a functionally folded malaria vaccine candidate in prokaryotic and eukaryotic expression systems. Infect. Immun. 71 (2003) 4961-4969
    • (2003) Infect. Immun. , vol.71 , pp. 4961-4969
    • Yadava, A.1    Ockenhouse, C.F.2
  • 21
    • 0036675623 scopus 로고    scopus 로고
    • Expression systems for production of recombinant allergens
    • Schmidt M., and Hoffman D.R. Expression systems for production of recombinant allergens. Int. Arch. Allergy Immunol. 128 (2002) 264-270
    • (2002) Int. Arch. Allergy Immunol. , vol.128 , pp. 264-270
    • Schmidt, M.1    Hoffman, D.R.2
  • 22
    • 0033561258 scopus 로고    scopus 로고
    • Production and detailed characterization of biologically active olive pollen allergen Ole e 1 secreted by the yeast Pichia pastoris
    • Huecas S., Villalba M., Gonzalez E., Martinez-Ruiz A., and Rodriguez R. Production and detailed characterization of biologically active olive pollen allergen Ole e 1 secreted by the yeast Pichia pastoris. Eur. J. Biochem. 261 (1999) 539-546
    • (1999) Eur. J. Biochem. , vol.261 , pp. 539-546
    • Huecas, S.1    Villalba, M.2    Gonzalez, E.3    Martinez-Ruiz, A.4    Rodriguez, R.5
  • 23
  • 26
    • 0036121820 scopus 로고    scopus 로고
    • CDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family
    • Diaz-Perales A., Garcia-Casado G., Sanchez-Monge R., Garcia-Selles F.J., Barber D., and Salcedo G. CDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family. Clin. Exp. Allergy 32 (2002) 87-92
    • (2002) Clin. Exp. Allergy , vol.32 , pp. 87-92
    • Diaz-Perales, A.1    Garcia-Casado, G.2    Sanchez-Monge, R.3    Garcia-Selles, F.J.4    Barber, D.5    Salcedo, G.6
  • 30
    • 0027291355 scopus 로고
    • Position paper: allergen standardization and skin tests. The European academy of allergology and clinical immunology
    • Dreborg S., and Frew A. Position paper: allergen standardization and skin tests. The European academy of allergology and clinical immunology. Allergy 48 (1993) 48-82
    • (1993) Allergy , vol.48 , pp. 48-82
    • Dreborg, S.1    Frew, A.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0035705215 scopus 로고    scopus 로고
    • The stripped basophil histamine release bioassay as a tool for the detection of allergen-specific IgE in serum
    • Kleine-Budde B., I, de Heer P.G., van der Zee J.S., and Aalberse R.C. The stripped basophil histamine release bioassay as a tool for the detection of allergen-specific IgE in serum. Int. Arch. Allergy Immunol. 126 (2001) 277-285
    • (2001) Int. Arch. Allergy Immunol. , vol.126 , pp. 277-285
    • Kleine-Budde, I.1    De Heer, P.G.2    van der Zee, J.S.3    Aalberse, R.C.4
  • 35
    • 7444229728 scopus 로고    scopus 로고
    • Hazelnut (Corylus avellana) vicilin Cor a 11: molecular characterization of a glycoprotein and its allergenic activity
    • Lauer I., Foetisch K., Kolarich D., Ballmer-Weber B.K., Conti A., Altmann F., Vieths S., and Scheurer S. Hazelnut (Corylus avellana) vicilin Cor a 11: molecular characterization of a glycoprotein and its allergenic activity. Biochem. J. 383 (2004) 327-334
    • (2004) Biochem. J. , vol.383 , pp. 327-334
    • Lauer, I.1    Foetisch, K.2    Kolarich, D.3    Ballmer-Weber, B.K.4    Conti, A.5    Altmann, F.6    Vieths, S.7    Scheurer, S.8
  • 36
    • 0024636430 scopus 로고
    • Functional characterization of the two alcohol oxidase genes from the yeast Pichia pastoris
    • Cregg J.M., Madden K.R., Barringer K.J., Thill G.P., and Stillman C.A. Functional characterization of the two alcohol oxidase genes from the yeast Pichia pastoris. Mol. Cell Biol. 9 (1989) 1316-1323
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1316-1323
    • Cregg, J.M.1    Madden, K.R.2    Barringer, K.J.3    Thill, G.P.4    Stillman, C.A.5
  • 40
    • 31344451312 scopus 로고    scopus 로고
    • Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens
    • Pasquato N., Berni R., Folli C., Folloni S., Cianci M., Pantano S., Helliwell J.R., and Zanotti G. Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens. J. Mol. Biol. 356 (2006) 684-694
    • (2006) J. Mol. Biol. , vol.356 , pp. 684-694
    • Pasquato, N.1    Berni, R.2    Folli, C.3    Folloni, S.4    Cianci, M.5    Pantano, S.6    Helliwell, J.R.7    Zanotti, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.