SrasV1, Ncbi, Merge, bibRecord, 002534

Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.

Identifieur interne : 002534 ( Ncbi/Merge ); précédent : 002533; suivant : 002535

Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.

Auteurs : Krupakar Parthasarathy [Singapour] ; Huang Lu ; Wahyu Surya ; Ardcharaporn Vararattanavech ; Konstantin Pervushin ; Jaume Torres

Source :

Protein expression and purification [ 1096-0279 ] ; 2012.

RBID : pubmed:22819936

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Circular Dichroism, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Escherichia coli (genetics), Lipid Bilayers (chemistry), Molecular Sequence Data, Mutation, Protein Multimerization, Protein Structure, Secondary, Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (isolation & purification), SARS Virus (chemistry), SARS Virus (genetics), Severe Acute Respiratory Syndrome (virology), Ultracentrifugation, Up-Regulation, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (isolation & purification).
MESH :
- chemical , chemistry : Lipid Bilayers, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemistry : SARS Virus.
- genetics : Escherichia coli, Recombinant Fusion Proteins, SARS Virus, Viral Envelope Proteins.
- chemical , isolation & purification : Recombinant Fusion Proteins, Viral Envelope Proteins.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Circular Dichroism, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Mutation, Protein Multimerization, Protein Structure, Secondary, Ultracentrifugation, Up-Regulation.

Abstract

Coronavirus envelope (E) proteins are short (~100 residues) polypeptides that contain at least one transmembrane (TM) domain and a cluster of 2-3 juxtamembrane cysteines. These proteins are involved in viral morphogenesis and tropism, and their absence leads in some cases to aberrant virions, or to viral attenuation. In common to other viroporins, coronavirus envelope proteins increase membrane permeability to ions. Although an NMR-based model for the TM domain of the E protein in the severe acute respiratory syndrome virus (SARS-CoV E) has been reported, structural data and biophysical studies of full length E proteins are not available because efficient expression and purification methods for these proteins are lacking. Herein we have used a novel fusion protein consisting of a modified β-barrel to purify both wild type and cysteine-less mutants of two representatives of coronavirus E proteins: the shortest (76 residues), from SARS-CoV E, and one of the longest (109 residues), from the infectious bronchitis virus (IBV E). The fusion construct was subsequently cleaved with cyanogen bromide and all polypeptides were obtained with high purity. This is an approach that can be used in other difficult hydrophobic peptides.

DOI: 10.1016/j.pep.2012.07.005
PubMed: 22819936

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001335
to stream PubMed, to step Curation: 001335
to stream PubMed, to step Checkpoint: 001354

Links to Exploration step

pubmed:22819936

Le document en format XML

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<front><div type="abstract" xml:lang="en">Coronavirus envelope (E) proteins are short (~100 residues) polypeptides that contain at least one transmembrane (TM) domain and a cluster of 2-3 juxtamembrane cysteines. These proteins are involved in viral morphogenesis and tropism, and their absence leads in some cases to aberrant virions, or to viral attenuation. In common to other viroporins, coronavirus envelope proteins increase membrane permeability to ions. Although an NMR-based model for the TM domain of the E protein in the severe acute respiratory syndrome virus (SARS-CoV E) has been reported, structural data and biophysical studies of full length E proteins are not available because efficient expression and purification methods for these proteins are lacking. Herein we have used a novel fusion protein consisting of a modified β-barrel to purify both wild type and cysteine-less mutants of two representatives of coronavirus E proteins: the shortest (76 residues), from SARS-CoV E, and one of the longest (109 residues), from the infectious bronchitis virus (IBV E). The fusion construct was subsequently cleaved with cyanogen bromide and all polypeptides were obtained with high purity. This is an approach that can be used in other difficult hydrophobic peptides.</div>
</front>
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<Abstract><AbstractText>Coronavirus envelope (E) proteins are short (~100 residues) polypeptides that contain at least one transmembrane (TM) domain and a cluster of 2-3 juxtamembrane cysteines. These proteins are involved in viral morphogenesis and tropism, and their absence leads in some cases to aberrant virions, or to viral attenuation. In common to other viroporins, coronavirus envelope proteins increase membrane permeability to ions. Although an NMR-based model for the TM domain of the E protein in the severe acute respiratory syndrome virus (SARS-CoV E) has been reported, structural data and biophysical studies of full length E proteins are not available because efficient expression and purification methods for these proteins are lacking. Herein we have used a novel fusion protein consisting of a modified β-barrel to purify both wild type and cysteine-less mutants of two representatives of coronavirus E proteins: the shortest (76 residues), from SARS-CoV E, and one of the longest (109 residues), from the infectious bronchitis virus (IBV E). The fusion construct was subsequently cleaved with cyanogen bromide and all polypeptides were obtained with high purity. This is an approach that can be used in other difficult hydrophobic peptides.</AbstractText>
<CopyrightInformation>Copyright © 2012 Elsevier Inc. All rights reserved.</CopyrightInformation>
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Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.

Expression and purification of coronavirus envelope proteins using a modified β-barrel construct.

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