Efficient protein production inspired by how spiders make silk

Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the ver...

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Vydáno v:Nature communications Ročník 8; číslo 1; s. 15504 - 15
Hlavní autoři: Kronqvist, Nina, Sarr, Médoune, Lindqvist, Anton, Nordling, Kerstin, Otikovs, Martins, Venturi, Luca, Pioselli, Barbara, Purhonen, Pasi, Landreh, Michael, Biverstål, Henrik, Toleikis, Zigmantas, Sjöberg, Lisa, Robinson, Carol V., Pelizzi, Nicola, Jörnvall, Hans, Hebert, Hans, Jaudzems, Kristaps, Curstedt, Tore, Rising, Anna, Johansson, Jan
Médium: Journal Article
Jazyk:angličtina
Vydáno: London Nature Publishing Group UK 23.05.2017
Nature Publishing Group
Nature Portfolio
Témata:
101/28
140/131
631/1647/2230/2233
631/337/470/2284
631/61/338/469
82/16
82/29
82/58
82/80
82/83
Amino acids
Animal diseases
Animal models
Animals
Biochemistry
Cholecystokinin - chemistry
Chromatography
Circular Dichroism
Dimerization
Disease Models, Animal
E coli
Escherichia coli - metabolism
Female
Fibroins - biosynthesis
Humanities and Social Sciences
Hydrogen-Ion Concentration
Lung - pathology
Magnetic Resonance Spectroscopy
Medical Bioscience
Medicinsk biovetenskap
Micelles
Microscopy, Electron, Transmission
multidisciplinary
Mutagenesis, Site-Directed
Mutation
Peptides
Peptides - chemistry
Protein Domains
Proteins
Rabbits
Recombinant Proteins - biosynthesis
Respiration Disorders - drug therapy
Respiratory diseases
Science
Science (multidisciplinary)
Silk
Silk - biosynthesis
Spiders
Surface-Active Agents - chemistry
Surfactants
Sweden
ISSN:2041-1723, 2041-1723
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Abstract Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general. The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional tags.
AbstractList Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general.
Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT star) that is pH insensitive, stabilized and hypersoluble compared to wildtype NT. NT star-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT star enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT star also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general.
Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general. The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional tags.
The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional tags.
Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general.Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general.
Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general.
Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins. Spiders can produce silk proteins at huge concentrations by sequestering their aggregation-prone regions in micellar structures, where the very soluble N-terminal domain (NT) forms the shell. We hypothesize that fusion to NT could similarly solubilize non-spidroin proteins, and design a charge-reversed mutant (NT*) that is pH insensitive, stabilized and hypersoluble compared to wild-type NT. NT*-transmembrane protein fusions yield up to eight times more of soluble protein in Escherichia coli than fusions with several conventional tags. NT* enables transmembrane peptide purification to homogeneity without chromatography and manufacture of low-cost synthetic lung surfactant that works in an animal model of respiratory disease. NT* also allows efficient expression and purification of non-transmembrane proteins, which are otherwise refractory to recombinant production, and offers a new tool for reluctant proteins in general. The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal domain of a spider silk protein to express and purify several difficult to express proteins at levels considerably higher than with conventional tags.
ArticleNumber 15504
Author Toleikis, Zigmantas
Jörnvall, Hans
Jaudzems, Kristaps
Curstedt, Tore
Johansson, Jan
Rising, Anna
Pioselli, Barbara
Kronqvist, Nina
Pelizzi, Nicola
Purhonen, Pasi
Biverstål, Henrik
Sarr, Médoune
Venturi, Luca
Hebert, Hans
Lindqvist, Anton
Landreh, Michael
Sjöberg, Lisa
Robinson, Carol V.
Otikovs, Martins
Nordling, Kerstin
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  organization: Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
– sequence: 2
  givenname: Médoune
  surname: Sarr
  fullname: Sarr, Médoune
  organization: Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
– sequence: 3
  givenname: Anton
  surname: Lindqvist
  fullname: Lindqvist, Anton
  organization: Spiber Technologies AB
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  organization: Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
– sequence: 5
  givenname: Martins
  surname: Otikovs
  fullname: Otikovs, Martins
  organization: Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis
– sequence: 6
  givenname: Luca
  surname: Venturi
  fullname: Venturi, Luca
  organization: R&D Department, Chiesi Farmaceutici, Largo Belloli 11/A
– sequence: 7
  givenname: Barbara
  surname: Pioselli
  fullname: Pioselli, Barbara
  organization: R&D Department, Chiesi Farmaceutici, Largo Belloli 11/A
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  givenname: Pasi
  surname: Purhonen
  fullname: Purhonen, Pasi
  organization: Department of Biosciences and Nutrition, Karolinska Institutet, and School of Technology and Health, KTH Royal institute of Technology
– sequence: 9
  givenname: Michael
  surname: Landreh
  fullname: Landreh, Michael
  organization: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
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  surname: Biverstål
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  organization: Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet, Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis
– sequence: 11
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  surname: Toleikis
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  organization: Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis
– sequence: 12
  givenname: Lisa
  surname: Sjöberg
  fullname: Sjöberg, Lisa
  organization: Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet
– sequence: 13
  givenname: Carol V.
  surname: Robinson
  fullname: Robinson, Carol V.
  organization: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford
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  surname: Pelizzi
  fullname: Pelizzi, Nicola
  organization: R&D Department, Chiesi Farmaceutici, Largo Belloli 11/A
– sequence: 15
  givenname: Hans
  surname: Jörnvall
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  givenname: Hans
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  organization: Department of Biosciences and Nutrition, Karolinska Institutet, and School of Technology and Health, KTH Royal institute of Technology
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  surname: Jaudzems
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  organization: Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis
– sequence: 18
  givenname: Tore
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  fullname: Curstedt, Tore
  organization: Department of Molecular Medicine and Surgery, Karolinska Institutet at Karolinska University Hospital
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  givenname: Anna
  orcidid: 0000-0002-1872-1207
  surname: Rising
  fullname: Rising, Anna
  organization: Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet, Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences
– sequence: 20
  givenname: Jan
  surname: Johansson
  fullname: Johansson, Jan
  organization: Division for Neurogeriatrics, Department of NVS, Center for Alzheimer Research, Karolinska Institutet, Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, School of Natural Sciences and Health, Tallinn University
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Snippet Membrane proteins are targets of most available pharmaceuticals, but they are difficult to produce recombinantly, like many other aggregation-prone proteins....
The properties of many transmembrane or aggregation-prone proteins make them difficult to recombinantly express. Here the authors use a modified N-terminal...
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StartPage 15504
SubjectTerms 101/28
140/131
631/1647/2230/2233
631/337/470/2284
631/61/338/469
82/16
82/29
82/58
82/80
82/83
Amino acids
Animal diseases
Animal models
Animals
Biochemistry
Cholecystokinin - chemistry
Chromatography
Circular Dichroism
Dimerization
Disease Models, Animal
E coli
Escherichia coli - metabolism
Female
Fibroins - biosynthesis
Humanities and Social Sciences
Hydrogen-Ion Concentration
Lung - pathology
Magnetic Resonance Spectroscopy
Medical Bioscience
Medicinsk biovetenskap
Micelles
Microscopy, Electron, Transmission
multidisciplinary
Mutagenesis, Site-Directed
Mutation
Peptides
Peptides - chemistry
Protein Domains
Proteins
Rabbits
Recombinant Proteins - biosynthesis
Respiration Disorders - drug therapy
Respiratory diseases
Science
Science (multidisciplinary)
Silk
Silk - biosynthesis
Spiders
Surface-Active Agents - chemistry
Surfactants
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Title Efficient protein production inspired by how spiders make silk
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