Bacterial Inclusion Bodies: Discovering Their Better Half

被引:122
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
    Acebron, Sergio P.
    Martin, Ianire
    del Castillo, Urko
    Moro, Fernando
    Muga, Arturo
    [J]. FEBS LETTERS, 2009, 583 (18) : 2991 - 2996
  • [2] Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease
    Amen, Triana
    Kaganovich, Daniel
    [J]. CELLULAR AND MOLECULAR LIFE SCIENCES, 2015, 72 (03) : 401 - 415
  • [3] Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    Ami, D
    Natalello, A
    Gatti-Lafranconi, P
    Lotti, M
    Doglia, SM
    [J]. FEBS LETTERS, 2005, 579 (16): : 3433 - 3436
  • [4] Recombinant protein folding and misfolding in Escherichia coli
    Baneyx, F
    Mujacic, M
    [J]. NATURE BIOTECHNOLOGY, 2004, 22 (11) : 1399 - 1408
  • [5] Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones
    Ben-Zvi, A
    De los Rios, P
    Dietler, G
    Goloubinoff, P
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (36) : 37298 - 37303
  • [6] EXPRESSION AND SECRETION OF HETEROLOGOUS PROTEASES BY CORYNEBACTERIUM-GLUTAMICUM
    BILLMANJACOBE, H
    WANG, LF
    KORTT, A
    STEWART, D
    RADFORD, A
    [J]. 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
    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
    [J]. ACTA BIOMATERIALIA, 2016, 43 : 230 - 239
  • [8] Supramolecular organization of protein-releasing functional amyloids solved in bacterial inclusion bodies
    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
    [J]. ACTA BIOMATERIALIA, 2013, 9 (04) : 6134 - 6142
  • [9] Amyloid-like properties of bacterial inclusion bodies
    Carrió, M
    González-Montalbán, N
    Vera, A
    Villaverde, A
    Ventura, S
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (05) : 1025 - 1037
  • [10] Construction and deconstruction of bacterial inclusion bodies
    Carrió, MM
    Villaverde, A
    [J]. JOURNAL OF BIOTECHNOLOGY, 2002, 96 (01) : 3 - 12