Publication Database

Differences in signal peptide processing between GP3 glycoproteins of Arteriviridae (2018)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Zhang, Minze (WE 5)

Veit, Michael (WE 5)

Quelle

Virology

Bandzählung: 517

Seiten: 69 – 76

ISSN: 0042-6822

Sprache

Englisch

Verweise

DOI: 10.1016/j.virol.2017.11.026

Pubmed: 29229370

Kontakt

Institut für Virologie

Robert-von-Ostertag-Str. 7-13
14163 Berlin
+49 30 838 51833
virologie@vetmed.fu-berlin.de

Abstract / Zusammenfassung

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.