Abstract:
:The disulphide-linked GP2/3/4 spike of equine arteritis virus (EAV) is essential for virus entry. We showed recently that in transfected cells carbohydrates attached adjacent to the signal peptide of GP3 inhibit cleavage. Here we confirm this unique phenomenon in recombinant viruses with disabled glycosylation sites. Surprisingly, the infectivity of EAV containing GP3 with cleaved signal peptide was not impaired and GP3 with cleaved signal peptide associates with GP2/4 in virus particles. In contrast, viruses containing GP3 with deleted hydrophobic C-terminus rapidly reverted back to wild type. The data support our model that the signal peptide is exposed to the lumen of the ER and the C-terminus peripherally attaches GP3 to membranes.
journal_name
Virus Resjournal_title
Virus researchauthors
Matczuk AK,Veit Mdoi
10.1016/j.virusres.2014.02.005subject
Has Abstractpub_date
2014-04-01 00:00:00pages
107-11eissn
0168-1702issn
1872-7492pii
S0168-1702(14)00058-6journal_volume
183pub_type
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