Abstract:
:Maturation of the arenavirus GP precursor (GPC) involves proteolytic processing by cellular signal peptidase and the proprotein convertase subtilisin kexin isozyme 1 (SKI-1)/site 1 protease (S1P), yielding a tripartite complex comprised of a stable signal peptide (SSP), the receptor-binding GP1, and the fusion-active transmembrane GP2. Here we investigated the roles of SKI-1/S1P processing and SSP in the biosynthesis of the recombinant GP ectodomains of lymphocytic choriomeningitis virus (LCMV) and Lassa virus (LASV). When expressed in mammalian cells, the LCMV and LASV GP ectodomains underwent processing by SKI-1/S1P, followed by dissociation of GP1 from GP2. The GP2 ectodomain spontaneously formed trimers as revealed by chemical cross-linking. The endogenous SSP, known to be crucial for maturation and transport of full-length arenavirus GPC was dispensable for processing and secretion of the soluble GP ectodomain, suggesting a specific role of SSP in the stable prefusion conformation and transport of full-length GPC.
journal_name
Virologyjournal_title
Virologyauthors
Burri DJ,Pasquato A,da Palma JR,Igonet S,Oldstone MB,Kunz Sdoi
10.1016/j.virol.2012.10.038subject
Has Abstractpub_date
2013-02-05 00:00:00pages
127-33issue
1eissn
0042-6822issn
1096-0341pii
S0042-6822(12)00546-6journal_volume
436pub_type
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