Differences in signal peptide processing between GP3 glycoproteins of Arteriviridae.

Abstract:

:We reported previously that carbohydrate attachment to an overlapping glycosylation site adjacent to the signal peptide of GP3 from equine arteritis virus (EAV) prevents cleavage. Here we investigated whether this unusual processing scheme is a feature of GP3s of other Arteriviridae, which all contain a glycosylation site at a similar position. Expression of GP3 from type-1 and type-2 porcine reproductive and respiratory syndrome virus (PRRSV) and from lactate dehydrogenase-elevating virus (LDV) revealed that the first glycosylation site is used, but has no effect on signal peptide cleavage. Comparison of the SDS-PAGE mobility of deglycosylated GP3 from PRRSV and LDV with mutants having or not having a signal peptide showed that GP3´s signal peptide is cleaved. Swapping the signal peptides between GP3 of EAV and PRRSV revealed that the information for co-translational processing is not encoded in the signal peptide, but in the remaining part of GP3.

journal_name

Virology

journal_title

Virology

authors

Zhang M,Veit M

doi

10.1016/j.virol.2017.11.026

subject

Has Abstract

pub_date

2018-04-01 00:00:00

pages

69-76

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(17)30405-1

journal_volume

517

pub_type

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