Construct design, biophysical, and biochemical characterization of the fusion core from mouse hepatitis virus (a coronavirus) spike protein.
Identifieur interne : 002B20 ( PubMed/Corpus ); précédent : 002B19; suivant : 002B21Construct design, biophysical, and biochemical characterization of the fusion core from mouse hepatitis virus (a coronavirus) spike protein.
Auteurs : Yanhui Xu ; David K. Cole ; Zhiyong Lou ; Yiwei Liu ; Lan Qin ; Xu Li ; Zhihong Bai ; Fang Yuan ; Zihe Rao ; George F. GaoSource :
- Protein expression and purification [ 1046-5928 ] ; 2004.
English descriptors
- KwdEn :
- Amino Acid Sequence, Chromatography, Gel, Circular Dichroism, Membrane Glycoproteins (chemistry), Molecular Sequence Data, Molecular Weight, Murine hepatitis virus (chemistry), Murine hepatitis virus (pathogenicity), Protein Structure, Secondary, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Fusion Proteins (chemistry), Viral Fusion Proteins (isolation & purification), Viral Fusion Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemistry : Murine hepatitis virus.
- chemical , isolation & purification : Viral Fusion Proteins.
- chemical , metabolism : Viral Fusion Proteins.
- pathogenicity : Murine hepatitis virus.
- Amino Acid Sequence, Chromatography, Gel, Circular Dichroism, Molecular Sequence Data, Molecular Weight, Protein Structure, Secondary, Spike Glycoprotein, Coronavirus.
Abstract
Membrane fusion between virus and host cells is the key step for enveloped virus entry and is mediated by the viral envelope fusion protein. In murine coronavirus, mouse hepatitis virus (MHV), the spike (S) protein mediates this process. Recently, the formation of anti-parallel 6-helix bundle of the MHV S protein heptad repeat (HR) regions (HR1 and HR2) has been confirmed, implying coronavirus has a class I fusion protein. This bundle is also called fusion core. To facilitate the solution of the crystal structure of this fusion core, we deployed an Escherichia coli in vitro expression system to express the HR1 and HR2 regions linked together by a flexible linker as a single chain (named 2-helix). This 2-helix polypeptide subsequently assembled into a typical 6-helix bundle. This bundle has been analyzed by a series of biophysical and biochemical techniques and confirmed that the design technique can be used for coronavirus as we successfully used for members of paramyxoviruses.
DOI: 10.1016/j.pep.2004.08.005
PubMed: 15477089
Links to Exploration step
pubmed:15477089Le document en format XML
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<term>Molecular Weight</term>
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<term>Murine hepatitis virus (pathogenicity)</term>
<term>Protein Structure, Secondary</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<front><div type="abstract" xml:lang="en">Membrane fusion between virus and host cells is the key step for enveloped virus entry and is mediated by the viral envelope fusion protein. In murine coronavirus, mouse hepatitis virus (MHV), the spike (S) protein mediates this process. Recently, the formation of anti-parallel 6-helix bundle of the MHV S protein heptad repeat (HR) regions (HR1 and HR2) has been confirmed, implying coronavirus has a class I fusion protein. This bundle is also called fusion core. To facilitate the solution of the crystal structure of this fusion core, we deployed an Escherichia coli in vitro expression system to express the HR1 and HR2 regions linked together by a flexible linker as a single chain (named 2-helix). This 2-helix polypeptide subsequently assembled into a typical 6-helix bundle. This bundle has been analyzed by a series of biophysical and biochemical techniques and confirmed that the design technique can be used for coronavirus as we successfully used for members of paramyxoviruses.</div>
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