Bacterial Inclusion Bodies: Discovering Their Better Half

被引:129
作者
Rinas, Ursula [1 ,2 ]
Garcia-Fruitos, Elena [3 ]
Corchero, Jose Luis [4 ,5 ,6 ]
Vazquez, Esther [4 ,5 ,6 ]
Seras-Franzoso, Joaquin [4 ,7 ]
Villaverde, Antonio [4 ,5 ,6 ]
机构
[1] Leibniz Univ Hannover, Tech Chem & Life Sci, Hannover, Germany
[2] Helmholtz Ctr Infect Res, Braunschweig, Germany
[3] IRTA, Dept Ruminant Prod, Barcelona 08140, Spain
[4] CIBER BBN, Bellaterra 08193, Spain
[5] Univ Autonoma Barcelona, Inst Biotecnol & Biomed, Bellaterra 08193, Cerdanyola Del, Spain
[6] Univ Autonoma Barcelona, Dept Genet & Microbiol, Bellaterra 08193, Cerdanyola Del, Spain
[7] Hosp Valle De Hebron, Mol Biol & Biochem Res Ctr Nanomed Cibbim Nanomed, Passeig Vall dHebron 119-129, Barcelona 08035, Spain
关键词
AMYLOID AGGREGATION KINETICS; ESCHERICHIA-COLI; PROTEIN AGGREGATION; RECOMBINANT PROTEINS; FUNCTIONAL AMYLOIDS; SECRETORY GRANULES; CELL-PROLIFERATION; EXPRESSION SYSTEM; BIOLOGICAL ROLE; BODY FORMATION;
D O I
10.1016/j.tibs.2017.01.005
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
Bacterial inclusion bodies (lBs) are functional, non-toxic amyloids occurring in recombinant bacteria showing analogies with secretory granules of the mammalian endocrine system. The scientific interest in these mesoscale protein aggregates has been historically masked by their status as a hurdle in recombinant protein production. However, progressive understanding of how the cell handles the quality of recombinant polypeptides and the main features of their intriguing molecular organization has stimulated the interest in inclusion bodies and spurred their use in diverse technological fields. The engineering and tailoring of !Bs as functional protein particles for materials science and biomedicine is a good example of how formerly undesired bacterial byproducts can be rediscovered as promising functional materials for a broad spectrum of applications.
引用
收藏
页码:726 / 737
页数:12
相关论文
共 99 条
[1]   DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface [J].
Acebron, Sergio P. ;
Martin, Ianire ;
del Castillo, Urko ;
Moro, Fernando ;
Muga, Arturo .
FEBS LETTERS, 2009, 583 (18) :2991-2996
[2]   Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease [J].
Amen, Triana ;
Kaganovich, Daniel .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2015, 72 (03) :401-415
[3]   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
[4]   Recombinant protein folding and misfolding in Escherichia coli [J].
Baneyx, F ;
Mujacic, M .
NATURE BIOTECHNOLOGY, 2004, 22 (11) :1399-1408
[5]   Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones [J].
Ben-Zvi, A ;
De los Rios, P ;
Dietler, G ;
Goloubinoff, P .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (36) :37298-37303
[6]   EXPRESSION AND SECRETION OF HETEROLOGOUS PROTEASES BY CORYNEBACTERIUM-GLUTAMICUM [J].
BILLMANJACOBE, H ;
WANG, LF ;
KORTT, A ;
STEWART, D ;
RADFORD, A .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1995, 61 (04) :1610-1613
[7]   Functional protein-based nanomaterial produced in microorganisms recognized as safe: A new platform for biotechnology [J].
Cano-Garrido, Olivia ;
Sanchez-Chardi, Alejandro ;
Pares, Silvia ;
Giro, Irene ;
Tatkiewicz, Witold I. ;
Ferrer-Miralles, Neus ;
Ratera, Imma ;
Natalello, Antonino ;
Cubarsi, Rafael ;
Veciana, Jaume ;
Bach, Alex ;
Villaverde, Antonio ;
Aris, Anna ;
Garcia-Fruitos, Elena .
ACTA BIOMATERIALIA, 2016, 43 :230-239
[8]   Supramolecular organization of protein-releasing functional amyloids solved in bacterial inclusion bodies [J].
Cano-Garrido, Olivia ;
Rodriguez-Carmona, Escarlata ;
Diez-Gil, Cesar ;
Vazquez, Esther ;
Elizondo, Elisa ;
Cubarsi, Rafael ;
Seras-Franzoso, Joaquin ;
Luis Corchero, Jose ;
Rinas, Ursula ;
Ratera, Imma ;
Ventosa, Nora ;
Veciana, Jaume ;
Villaverde, Antonio ;
Garcia-Fruitos, Elena .
ACTA BIOMATERIALIA, 2013, 9 (04) :6134-6142
[9]   Amyloid-like properties of bacterial inclusion bodies [J].
Carrió, M ;
González-Montalbán, N ;
Vera, A ;
Villaverde, A ;
Ventura, S .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (05) :1025-1037
[10]   Construction and deconstruction of bacterial inclusion bodies [J].
Carrió, MM ;
Villaverde, A .
JOURNAL OF BIOTECHNOLOGY, 2002, 96 (01) :3-12