Bacterial inclusion bodies are industrially exploitable amyloids

Publikation: Beitrag in Fachzeitschrift › Übersichtsarbeit › Forschung › Peer-Review

Autoren

  • Ario De Marco
  • Neus Ferrer-Miralles
  • Elena Garcia-Fruitós
  • Anna Mitraki
  • Spela Peternel
  • Ursula Rinas
  • Mauricio A. Trujillo-Roldán
  • Norma A. Valdez-Cruz
  • Esther Vázquez
  • Antonio Villaverde

Organisationseinheiten

Externe Organisationen

  • University of Nova Gorica
  • Universidad Autónoma de Barcelona (UAB)
  • Centros de Investigacion Biomedica en Red - CIBER
  • IRTA - Institute of Agrifood Research and Technology
  • University of Crete
  • Lupinica
  • Helmholtz-Zentrum für Infektionsforschung GmbH (HZI)
  • Universidad Nacional Autónoma de México (UNAM)
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)53-72
Seitenumfang20
FachzeitschriftFEMS Microbiology Reviews
Jahrgang43
Ausgabenummer1
Frühes Online-Datum24 Okt. 2018
PublikationsstatusVeröffentlicht - Jan. 2019

Abstract

Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids. Based on an amyloidal skeleton combined with varying amounts of native or native-like protein forms, bacterial inclusion bodies exhibit an unusual arrangement that confers mechanical stability, biological activity and conditional protein release, being thus exploitable as versatile biomaterials. The applicability of inclusion bodies in biotechnology as enriched sources of protein and reusable catalysts, and in biomedicine as biocompatible topographies, nanopills or mimetics of endocrine secretory granules has been largely validated. Beyond these uses, the dissection of how recombinant bacteria manage the aggregation of functional protein species into structures of highly variable complexity offers insights about unsuspected connections between protein quality (conformational status compatible with functionality) and cell physiology.

ASJC Scopus Sachgebiete

Ziele für nachhaltige Entwicklung

Zitieren

Bacterial inclusion bodies are industrially exploitable amyloids. / De Marco, Ario; Ferrer-Miralles, Neus; Garcia-Fruitós, Elena et al.
in: FEMS Microbiology Reviews, Jahrgang 43, Nr. 1, 01.2019, S. 53-72.

Publikation: Beitrag in Fachzeitschrift › Übersichtsarbeit › Forschung › Peer-Review

De Marco, A, Ferrer-Miralles, N, Garcia-Fruitós, E, Mitraki, A, Peternel, S, Rinas, U, Trujillo-Roldán, MA, Valdez-Cruz, NA, Vázquez, E & Villaverde, A 2019, 'Bacterial inclusion bodies are industrially exploitable amyloids', FEMS Microbiology Reviews, Jg. 43, Nr. 1, S. 53-72. https://doi.org/10.1093/femsre/fuy038
De Marco, A., Ferrer-Miralles, N., Garcia-Fruitós, E., Mitraki, A., Peternel, S., Rinas, U., Trujillo-Roldán, M. A., Valdez-Cruz, N. A., Vázquez, E., & Villaverde, A. (2019). Bacterial inclusion bodies are industrially exploitable amyloids. FEMS Microbiology Reviews, 43(1), 53-72. https://doi.org/10.1093/femsre/fuy038
De Marco A, Ferrer-Miralles N, Garcia-Fruitós E, Mitraki A, Peternel S, Rinas U et al. Bacterial inclusion bodies are industrially exploitable amyloids. FEMS Microbiology Reviews. 2019 Jan;43(1):53-72. Epub 2018 Okt 24. doi: 10.1093/femsre/fuy038
De Marco, Ario ; Ferrer-Miralles, Neus ; Garcia-Fruitós, Elena et al. / Bacterial inclusion bodies are industrially exploitable amyloids. in: FEMS Microbiology Reviews. 2019 ; Jahrgang 43, Nr. 1. S. 53-72.
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@article{5b846b77bb1a4f1eaedc5e4819e84ff0,
title = "Bacterial inclusion bodies are industrially exploitable amyloids",
abstract = "Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids. Based on an amyloidal skeleton combined with varying amounts of native or native-like protein forms, bacterial inclusion bodies exhibit an unusual arrangement that confers mechanical stability, biological activity and conditional protein release, being thus exploitable as versatile biomaterials. The applicability of inclusion bodies in biotechnology as enriched sources of protein and reusable catalysts, and in biomedicine as biocompatible topographies, nanopills or mimetics of endocrine secretory granules has been largely validated. Beyond these uses, the dissection of how recombinant bacteria manage the aggregation of functional protein species into structures of highly variable complexity offers insights about unsuspected connections between protein quality (conformational status compatible with functionality) and cell physiology.",
keywords = "Biomaterials, Functional amyloids, Inclusion bodies, Protein production, Protein release, Recombinant bacteria",
author = "{De Marco}, Ario and Neus Ferrer-Miralles and Elena Garcia-Fruit{\'o}s and Anna Mitraki and Spela Peternel and Ursula Rinas and Trujillo-Rold{\'a}n, {Mauricio A.} and Valdez-Cruz, {Norma A.} and Esther V{\'a}zquez and Antonio Villaverde",
note = "FUNDING The authors appreciate the financial support for research on therapeutic recombinant proteins to NFM (grant RTA2015-00064-C02-02, Instituto Nacional de Investigaci{\'o}n y Tecnolog{\'i}a Agraria y Alimentaria (INIA), Ministerio de Econom{\'i}a y Empresa (MINECO), Spain) to EGF (grant RTA2015-00064-C02-01, INIA, MINECO, Spain, CERCA Programme—Generalitat de Catalunya—and European Social Fund), to EV (grant PI15/00272, ISCIII, Spain, co-founding FEDER), to AdM (Slovenia-Belgium ARRS-FWO program, ARRS/N4-0046-5100-1/2015-59) and to AV (grant BIO2016-76063-R, Agencia Estatal de Investigaci{\'o}n and Fondo Europeo de Desarrollo Regional, AEI/FEDER, UE; grant 2017SGR-229, AGAUR, Spain). Besides, EGF received a post-doctoral fellowship from INIA (DOC-INIA, MINECO). MATR and NAVC thank the Institutional Program of the {\textquoteleft}Instituto de Investigaciones Biom{\'e}dicas-UNAM{\textquoteright}: {\textquoteleft}La producci{\'o}n de biomol{\'e}culas de inter{\'e}s biom{\'e}dico en bacterias y hongos.{\textquoteright} Funding {\textquoteleft}Consejo Nacional de Ciencia y Tecnolog{\'i}a{\textquoteright} CONACYT (220795, 247473 and 178528), and {\textquoteleft}Programa de Apoyo a Proyectos de Investigaci{\'o}n e Innovaci{\'o}n Tecnol{\'o}gica, Universidad Nacional Aut{\'o}noma de M{\'e}xico{\textquoteright} PAPIIT-UNAM (IN-209113 and IN-208415). We are also indebted to The Networking Research Center on Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), an initiative funded by the VI National R&D&I Plan 2008–2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Carlos III with assistance from the European Regional Development Fund. This manuscript was written in collaboration with the ICTS {\textquoteleft}NANBIOSIS,{\textquoteright} more specifically with the Unit 1: Protein Production Platform of CIBER-BBN/ IBB, at the UAB sePBioEs scientific-technical service (http://www.nanbiosis.es/portfolio/u1-protein-production-platform-ppp/). The authors do not appreciate any conflict of interest.",
year = "2019",
month = jan,
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language = "English",
volume = "43",
pages = "53--72",
journal = "FEMS Microbiology Reviews",
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Download

TY - JOUR

T1 - Bacterial inclusion bodies are industrially exploitable amyloids

AU - De Marco, Ario

AU - Ferrer-Miralles, Neus

AU - Garcia-Fruitós, Elena

AU - Mitraki, Anna

AU - Peternel, Spela

AU - Rinas, Ursula

AU - Trujillo-Roldán, Mauricio A.

AU - Valdez-Cruz, Norma A.

AU - Vázquez, Esther

AU - Villaverde, Antonio

N1 - FUNDING The authors appreciate the financial support for research on therapeutic recombinant proteins to NFM (grant RTA2015-00064-C02-02, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Ministerio de Economía y Empresa (MINECO), Spain) to EGF (grant RTA2015-00064-C02-01, INIA, MINECO, Spain, CERCA Programme—Generalitat de Catalunya—and European Social Fund), to EV (grant PI15/00272, ISCIII, Spain, co-founding FEDER), to AdM (Slovenia-Belgium ARRS-FWO program, ARRS/N4-0046-5100-1/2015-59) and to AV (grant BIO2016-76063-R, Agencia Estatal de Investigación and Fondo Europeo de Desarrollo Regional, AEI/FEDER, UE; grant 2017SGR-229, AGAUR, Spain). Besides, EGF received a post-doctoral fellowship from INIA (DOC-INIA, MINECO). MATR and NAVC thank the Institutional Program of the ‘Instituto de Investigaciones Biomédicas-UNAM’: ‘La producción de biomoléculas de interés biomédico en bacterias y hongos.’ Funding ‘Consejo Nacional de Ciencia y Tecnología’ CONACYT (220795, 247473 and 178528), and ‘Programa de Apoyo a Proyectos de Investigación e Innovación Tecnológica, Universidad Nacional Autónoma de México’ PAPIIT-UNAM (IN-209113 and IN-208415). We are also indebted to The Networking Research Center on Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), an initiative funded by the VI National R&D&I Plan 2008–2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Carlos III with assistance from the European Regional Development Fund. This manuscript was written in collaboration with the ICTS ‘NANBIOSIS,’ more specifically with the Unit 1: Protein Production Platform of CIBER-BBN/ IBB, at the UAB sePBioEs scientific-technical service (http://www.nanbiosis.es/portfolio/u1-protein-production-platform-ppp/). The authors do not appreciate any conflict of interest.

PY - 2019/1

Y1 - 2019/1

N2 - Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids. Based on an amyloidal skeleton combined with varying amounts of native or native-like protein forms, bacterial inclusion bodies exhibit an unusual arrangement that confers mechanical stability, biological activity and conditional protein release, being thus exploitable as versatile biomaterials. The applicability of inclusion bodies in biotechnology as enriched sources of protein and reusable catalysts, and in biomedicine as biocompatible topographies, nanopills or mimetics of endocrine secretory granules has been largely validated. Beyond these uses, the dissection of how recombinant bacteria manage the aggregation of functional protein species into structures of highly variable complexity offers insights about unsuspected connections between protein quality (conformational status compatible with functionality) and cell physiology.

AB - Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids. Based on an amyloidal skeleton combined with varying amounts of native or native-like protein forms, bacterial inclusion bodies exhibit an unusual arrangement that confers mechanical stability, biological activity and conditional protein release, being thus exploitable as versatile biomaterials. The applicability of inclusion bodies in biotechnology as enriched sources of protein and reusable catalysts, and in biomedicine as biocompatible topographies, nanopills or mimetics of endocrine secretory granules has been largely validated. Beyond these uses, the dissection of how recombinant bacteria manage the aggregation of functional protein species into structures of highly variable complexity offers insights about unsuspected connections between protein quality (conformational status compatible with functionality) and cell physiology.

KW - Biomaterials

KW - Functional amyloids

KW - Inclusion bodies

KW - Protein production

KW - Protein release

KW - Recombinant bacteria

UR - http://www.scopus.com/inward/record.url?scp=85058914795&partnerID=8YFLogxK

U2 - 10.1093/femsre/fuy038

DO - 10.1093/femsre/fuy038

M3 - Review article

C2 - 30357330

AN - SCOPUS:85058914795

VL - 43

SP - 53

EP - 72

JO - FEMS Microbiology Reviews

JF - FEMS Microbiology Reviews

SN - 0168-6445

IS - 1

ER -