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
PY - 2019/1/1
Y1 - 2019/1/1
N2 - © FEMS 2018. All rights reserved. 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 - © FEMS 2018. All rights reserved. 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
KW - Biotechnology/trends
KW - Bacterial Proteins/metabolism
KW - Bacteria/chemistry
KW - Inclusion Bodies/chemistry
KW - Organisms, Genetically Modified
UR - http://www.mendeley.com/research/bacterial-inclusion-bodies-industrially-exploitable-amyloids
U2 - 10.1093/femsre/fuy038
DO - 10.1093/femsre/fuy038
M3 - Review article
C2 - 30357330
SN - 0168-6445
VL - 43
SP - 53
EP - 72
JO - FEMS Microbiology Reviews
JF - FEMS Microbiology Reviews
IS - 1
ER -