Studies on bacterial inclusion bodies

被引:33
作者
de Groot, Natalia S. [1 ,2 ]
Espargaro, Alba [1 ,2 ]
Morell, Montserrat [1 ,2 ]
Ventura, Salvador [1 ,2 ]
机构
[1] Univ Autonoma Barcelona, Dept Bioquim & Biol Mol, E-08193 Bellaterra, Spain
[2] Univ Autonoma Barcelona, Inst Biotecnol & Biomed, E-08193 Bellaterra, Spain
关键词
amyloid; chaperone; Escherichia coli; inclusion bodies; protein aggregation; protein folding; protein production; protein solubility;
D O I
10.2217/17460913.3.4.423
中图分类号
Q93 [微生物学];
学科分类号
071005 [微生物学]; 100705 [微生物与生化药学];
摘要
The field of protein misfolding and aggregation has become an extremely active area of research in recent years. Of particular interest is the deposition of polypeptides into inclusion bodies inside bacterial cells. One reason for this interest is that protein aggregation constitutes a major bottleneck in protein production and restricts the spectrum of protein-based drugs available for commercialization. Additionally, prokaryotic cells could provide a simple yet powerful system for studying the formation and prevention of toxic aggregates, such as those responsible for a number of degenerative diseases. Here, we review recent work that has challenged our understanding of the structure and physiology of inclusion bodies and provided us with a new view of intracellular protein deposition, which has important implications in microbiology, biomedicine and biotechnology.
引用
收藏
页码:423 / 435
页数:13
相关论文
共 106 条
[1]
2 NOVEL HEAT-SHOCK GENES ENCODING PROTEINS PRODUCED IN RESPONSE TO HETEROLOGOUS PROTEIN EXPRESSION IN ESCHERICHIA-COLI [J].
ALLEN, SP ;
POLAZZI, JO ;
GIERSE, JK ;
EASTON, AM .
JOURNAL OF BACTERIOLOGY, 1992, 174 (21) :6938-6947
[2]
Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy [J].
Ami, D ;
Natalello, A ;
Gatti-Lafranconi, P ;
Lotti, M ;
Doglia, SM .
FEBS LETTERS, 2005, 579 (16) :3433-3436
[3]
FT-IR study of heterologous protein expression in recombinant Escherichia coli strains [J].
Ami, D ;
Bonecchi, L ;
Calì, S ;
Orsini, G ;
Tonon, G ;
Doglia, SM .
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 2003, 1624 (1-3) :6-10
[4]
Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy [J].
Ami, Diletta ;
Natalello, Antonino ;
Taylor, Geoffrey ;
Tonon, Giancarlo ;
Doglia, Silvia Maria .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2006, 1764 (04) :793-799
[5]
Formation of active inclusion bodies in the periplasm of Escherichia coli [J].
Arie, Jean-Philippe ;
Miot, Marika ;
Sassoon, Nathalie ;
Betton, Jean-Michel .
MOLECULAR MICROBIOLOGY, 2006, 62 (02) :427-437
[6]
Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones [J].
Ben-Zvi, AP ;
Goloubinoff, P .
JOURNAL OF STRUCTURAL BIOLOGY, 2001, 135 (02) :84-93
[7]
BOWDEN GA, 1990, J BIOL CHEM, V265, P16760
[8]
STRUCTURE AND MORPHOLOGY OF PROTEIN INCLUSION-BODIES IN ESCHERICHIA-COLI [J].
BOWDEN, GA ;
PAREDES, AM ;
GEORGIOU, G .
BIO-TECHNOLOGY, 1991, 9 (08) :725-730
[9]
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases [J].
Bucciantini, M ;
Giannoni, E ;
Chiti, F ;
Baroni, F ;
Formigli, L ;
Zurdo, JS ;
Taddei, N ;
Ramponi, G ;
Dobson, CM ;
Stefani, M .
NATURE, 2002, 416 (6880) :507-511
[10]
Investigating the effects of mutations on protein aggregation in the cell [J].
Calloni, G ;
Zoffoli, S ;
Stefani, M ;
Dobson, CM ;
Chiti, F .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (11) :10607-10613