Open AccessRubella Virus E2 Signal Peptide Is Required for Perinuclear Localization of Capsid Protein and Virus Assembly
Author(s) -
Lok Man J. Law,
Robert C. Duncan,
Ali Esmaili,
Hira L. Nakhasi,
Tom C. Hobman
Publication year - 2001
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.75.4.1978-1983.2001
Subject(s) - capsid , biology , signal peptidase , signal peptide , rubella virus , endoplasmic reticulum , golgi apparatus , virus , microbiology and biotechnology , virology , glycoprotein , peptide sequence , biochemistry , rubella , gene , measles , vaccination
The rubella virus (RV) structural proteins capsid, E2, and E1 are synthesized as a polyprotein precursor. The signal peptide that initiates translocation of E2 into the lumen of the endoplasmic reticulum remains attached to the carboxy terminus of the capsid protein after cleavage by signal peptidase. Among togaviruses, this feature is unique to RV. The E2 signal peptide has previously been shown to function as a membrane anchor for the capsid protein. In the present study, we demonstrate that this domain is required for RV glycoprotein-dependent localization of the capsid protein to the juxtanuclear region and subsequent virus assembly at the Golgi complex.