Details
| Original language | English |
|---|---|
| Pages (from-to) | 53-72 |
| Number of pages | 20 |
| Journal | FEMS Microbiology Reviews |
| Volume | 43 |
| Issue number | 1 |
| Early online date | 24 Oct 2018 |
| Publication status | Published - 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.
Keywords
- Biomaterials, Functional amyloids, Inclusion bodies, Protein production, Protein release, Recombinant bacteria
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology
- Medicine(all)
- Infectious Diseases
Sustainable Development Goals
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In: FEMS Microbiology Reviews, Vol. 43, No. 1, 01.2019, p. 53-72.
Research output: Contribution to journal › Review article › Research › peer review
}
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 -