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N-linked glycosylation of Gn (but not Gc) is important for Crimean Congo hemorrhagic fever virus glycoprotein localization and transport.

Abstract：

:The mature Gn glycoprotein of Crimean Congo hemorrhagic fever (CCHF) virus contains two predicted glycosylation sites (557N and 755N). Of these, N-glycans are added only at 557N, as evidenced by abrogation of Gn-glycosylation by mutation of 557N but not 755N site. Mutational block of Gn-glycosylation at 557N did not significantly affect Gn proteolytic processing but did result in mislocalization and retention of Gn and other proteins synthesized from the virus M segment ORF (GP160, GP85, GP38 and Gc) in the endoplasmic reticulum. In contrast to Gn, similar mutational analysis demonstrated that, while N-glycosylation occurs at the two predicted sites in Gc, abrogation of their glycosylation did not alter localization of any of the CCHF virus glycoproteins. Studies of Gn expressed in the absence of Gc demonstrate that, while Gn processing and localization are independent of Gc, all the CCHF virus glycoproteins appear dependent on N-glycosylation of Gn for correct folding, localization and transport.

journal_name

Virology

journal_title

Virology

authors

Erickson BR,Deyde V,Sanchez AJ,Vincent MJ,Nichol ST

doi

10.1016/j.virol.2006.11.023

subject

Has Abstract

pub_date

2007-05-10 00:00:00

pages

348-55

issue

2

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(06)00866-X

journal_volume

361

pub_type

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