Recombinant protein expression in Pichia pastoris

被引:932
作者
Cregg, JM
Cereghino, JL
Shi, JY
Higgins, DR
机构
[1] Keck Grad Inst Appl Life Sci, Claremont, CA 91711 USA
[2] Oregon Grad Inst Sci & Technol, Beaverton, OR 97006 USA
[3] Idun Pharmaceut, La Jolla, CA 92037 USA
关键词
Pichia pastoris; Pichia methanolica; methylotrophic yeast; heterologous protein production; foreign gene expression; yeast protein expression; fermentation;
D O I
10.1385/MB:16:1:23
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The methylotrophic yeast Pichia pastoris is now one of the standard tools used in molecular biology for the generation of recombinant protein. P. pastoris has demonstrated its most powerful success as a large-scale (fermentation) recombinant protein production tool. What began more than 20 years ago as a program to convert abundant methanol to a protein source for animal feed has been developed into what is today two production system. To date well over 200 heterologous proteins have been expressed in P. pastoris. Significant advances in the development of new strains and vectors, improved techniques, and the commercial availability of these tools coupled with a better understanding of the biology of Pichia species have led to this microbe's value and power in commercial and research labs alike.
引用
收藏
页码:23 / 52
页数:30
相关论文
共 310 条
  • [1] Functional expression of bovine opsin in the methylotrophic yeast Pichia pastoris
    Abdulaev, NG
    Popp, MP
    Smith, WC
    Ridge, KD
    [J]. PROTEIN EXPRESSION AND PURIFICATION, 1997, 10 (01) : 61 - 69
  • [2] Production of human tissue factor using the Pichia pastoris expression system
    Austin, AJ
    Jones, CE
    Van Heeke, G
    [J]. PROTEIN EXPRESSION AND PURIFICATION, 1998, 13 (01) : 136 - 142
  • [3] Intracellular production of a major cytomegalovirus antigenic protein in the methylotrophic yeast Pichia pastoris
    Battista, MC
    Bergamini, G
    Campanini, F
    Landini, MP
    Ripalti, A
    [J]. GENE, 1996, 176 (1-2) : 197 - 201
  • [4] Expression of human monocyte chemoattractant protein-1 in the yeast Pichia pastoris
    Beall, CJ
    Breckenridge, SM
    Chakravarty, L
    Kolattukudy, PE
    [J]. PROTEIN EXPRESSION AND PURIFICATION, 1998, 12 (02) : 145 - 150
  • [5] Beaudet L, 1998, METHOD ENZYMOL, V292, P397
  • [6] Mutations in the nucleotide-binding sites of P-glycoprotein that affect substrate specificity modulate substrate-induced adenosine triphosphatase activity
    Beaudet, L
    Urbatsch, IL
    Gros, P
    [J]. BIOCHEMISTRY, 1998, 37 (25) : 9073 - 9082
  • [7] Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans
    Beauvais, A
    Monod, M
    Wyniger, J
    Debeaupuis, JP
    Grouzmann, E
    Brakch, N
    Svab, J
    Hovanessian, AG
    Latge, JP
    [J]. INFECTION AND IMMUNITY, 1997, 65 (08) : 3042 - 3047
  • [8] Biochemical and antigenic characterization of a new dipeptidyl-peptidase isolated from Aspergillus fumigatus
    Beauvais, A
    Monod, M
    Debeaupuis, JP
    Diaquin, M
    Kobayashi, H
    Latge, JP
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (10) : 6238 - 6244
  • [9] X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32
    Bewley, MC
    Tam, BM
    Grewal, J
    He, SM
    Shewry, S
    Murphy, MEP
    Mason, AB
    Woodworth, RC
    Baker, EN
    MacGillivray, RTA
    [J]. BIOCHEMISTRY, 1999, 38 (08) : 2535 - 2541
  • [10] The conformation of purified Toxoplasma gondii SAG1 antigen, secreted from engineered Pichia pastoris, is adequate for serorecognition and cell proliferation
    Biemans, R
    Grégoire, D
    Haumont, M
    Bosseloir, A
    Garcia, L
    Jacquet, A
    Dubeaux, C
    Bollen, A
    [J]. JOURNAL OF BIOTECHNOLOGY, 1998, 66 (2-3) : 137 - 146