dc.contributor.author
Kabatek, Aleksander
dc.contributor.author
Veit, Michael
dc.date.accessioned
2018-06-08T02:58:03Z
dc.date.available
2014-03-25T11:58:36.281Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/14216
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-18412
dc.description.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.
de
dc.rights.uri
http://creativecommons.org/licenses/by/3.0/
dc.subject
equine arteritis virus
dc.subject
protein folding
dc.subject
oligomerization
dc.subject.ddc
600 Technik, Medizin, angewandte Wissenschaften::630 Landwirtschaft
dc.title
Folding and oligomerization of the gp2b/gp3/gp4 spike proteins of equine
arteritis virus in vitro
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Viruses 4 (2012), 3 , S. 414–423
dcterms.bibliographicCitation.doi
10.3390/v4030414
dcterms.bibliographicCitation.url
http://dx.doi.org/10.3390/v4030414
refubium.affiliation
Veterinärmedizin
de
refubium.affiliation.other
Institut für Virologie
refubium.mycore.fudocsId
FUDOCS_document_000000019966
refubium.note.author
Der Artikel wurde in einer Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000003316
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
1999-4915
