Viruses 2012, 4(3), 414-423; doi:10.3390/v4030414
Communication

Folding and Oligomerization of the gp2b/gp3/gp4 Spike Proteins of Equine Arteritis Virus in Vitro

Received: 5 January 2012; in revised form: 13 March 2012 / Accepted: 18 March 2012 / Published: 22 March 2012
(This article belongs to the Special Issue Animal Arteriviruses and Coronaviruses)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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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MDPI and ACS Style

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.

AMA Style

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.

Chicago/Turabian Style

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.

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