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Folding and Oligomerization of the gp2b/gp3/gp4 Spike Proteins of Equine Arteritis Virus in Vitro
Department of Immunology and Molecular Biology, Veterinary Faculty, Free University, Philippstraße 13, Berlin 10115, Germany
* Author to whom correspondence should be addressed.
Received: 5 January 2012; in revised form: 13 March 2012 / Accepted: 18 March 2012 / Published: 22 March 2012
Abstract: 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.
Keywords: equine arteritis virus; glycoproteins; gp2b; gp3; gp4; protein folding, oligomerization
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Kabatek, A.; Veit, M. Folding and Oligomerization of the gp2b/gp3/gp4 Spike Proteins of Equine Arteritis Virus in Vitro. Viruses 2012, 4, 414-423.
Kabatek A, Veit M. Folding and Oligomerization of the gp2b/gp3/gp4 Spike Proteins of Equine Arteritis Virus in Vitro. Viruses. 2012; 4(3):414-423.
Kabatek, Aleksander; Veit, Michael. 2012. "Folding and Oligomerization of the gp2b/gp3/gp4 Spike Proteins of Equine Arteritis Virus in Vitro." Viruses 4, no. 3: 414-423.