Arenavirus envelope glycoproteins mimic autoprocessing sites of the cellular proprotein convertase subtilisin kexin isozyme-1/site-1 protease.


Autoria(s): Pasquato A.; Burri D.J.; Traba E.G.; Hanna-El-Daher L.; Seidah N.G.; Kunz S.
Data(s)

2011

Resumo

A crucial step in the arenavirus life cycle is the proteolytic processing of the viral envelope glycoprotein precursor (GPC) by the cellular proprotein convertase (PC) subtilisin kexin isozyme-1 (SKI-1)/site-1 protease (S1P). Here we conducted a systematic and quantitative analysis of SKI-1/S1P processing of peptides derived from the recognition sites of GPCs of different Old World and New World arenaviruses. We found that SKI-1/S1P showed a strong preference for arenaviral sequences resembling its autoprocessing sites, which are recurrent motifs in arenaviral GPCs. The African arenaviruses Lassa, Mobala, and Mopeia resemble the SKI-1/S1P autoprocessing C-site, whereas sequences derived from Clade B New World viruses Junin and Tacaribe have similarities to the autoprocessing B-site. In contrast, analogous peptides derived from cellular SKI-1/S1P substrates were remarkably poor substrates. The data suggest that arenavirus GPCs evolved to mimic SKI-1/S1P autoprocessing sites, likely ensuring efficient cleavage and perhaps avoiding competition with SKI-1/S1P's cellular substrates.

Identificador

http://serval.unil.ch/?id=serval:BIB_B25D9F29A681

isbn:1096-0341 (Electronic)

pmid:21612810

doi:10.1016/j.virol.2011.04.021

isiid:000293820300003

Idioma(s)

en

Fonte

Virology, vol. 417, no. 1, pp. 18-26

Tipo

info:eu-repo/semantics/article

article