Key result
Folding and oligomerization of Equine arteritis virus glycoproteins gp2b, gp3, and gp4 in vitro are interdependent processes, with Gst-tagged proteins facilitating the solubility of His-tagged proteins.
Folding and oligomerization of EAV spike proteins gp2b, gp3, and gp4 in vitro are interdependent processes.
No clinical implications for EAV; leaves open interdependent glycoprotein folding in natural infection.
Equine arteritis virus (EAV) is a small, positive-stranded RNA virus. The glycoproteins gp2b, gp3 and gp4 form a heterotrimer in the viral envelope, which is required for cell entry of EAV. We describe expression of the ectodomains of the proteins in E. coli and their refolding from inclusion bodies. After extraction of inclusion bodies and dialysis, Gst-, but not His-tagged proteins, refold into a soluble conformation. However, when dialyzed together with Gst-gp3 or with Gst-gp4, His-gp2b and His-gp4 remain soluble and oligomers are obtained by affinity-chromatography. Thus, folding and oligomerization of gp2b, gp3 and gp4 in vitro are interdependent processes.
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Kabatek et al. (2012) studied this question. Expression and refolding of EAV glycoproteins gp2b, gp3, and gp4 was evaluated on Protein folding and oligomerization. Folding and oligomerization of Equine arteritis virus glycoproteins gp2b, gp3, and gp4 in vitro are interdependent processes, with Gst-tagged proteins facilitating the solubility of His-tagged proteins.
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