Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains.

Details

Serval ID
serval:BIB_932E308356CC
Type
Article: article from journal or magazin.
Collection
Publications
Title
Arenavirus Z-glycoprotein association requires Z myristoylation but not functional RING or late domains.
Journal
Journal of Virology
Author(s)
Capul A.A., Perez M., Burke E., Kunz S., Buchmeier M.J., de la Torre J.C.
ISSN
0022-538X (Print)
ISSN-L
0022-538X
Publication state
Published
Issued date
2007
Volume
81
Number
17
Pages
9451-9460
Language
english
Abstract
Generation of infectious arenavirus-like particles requires the virus RING finger Z protein and surface glycoprotein precursor (GPC) and the correct processing of GPC into GP1, GP2, and a stable signal peptide (SSP). Z is the driving force of arenavirus budding, whereas the GP complex (GPc), consisting of hetero-oligomers of SSP, GP1, and GP2, forms the viral envelope spikes that mediate receptor recognition and cell entry. Based on the roles played by Z and GP in the arenavirus life cycle, we hypothesized that Z and the GPc should interact in a manner required for virion formation. Here, using confocal microscopy and coimmunoprecipitation assays, we provide evidence for subcellular colocalization and biochemical interaction, respectively, of Z and the GPc. Our results from mutation-function analysis reveal that Z myristoylation, but not the Z late (L) or RING domain, is required for Z-GPc interaction. Moreover, Z interacted directly with SSP in the absence of other components of the GPc. We obtained similar results with Z and GPC from the prototypical arenavirus lymphocytic choriomeningitis virus and the hemorrhagic fever arenavirus Lassa fever virus.
Keywords
Animals, Arenavirus/physiology, Carrier Proteins/chemistry, Carrier Proteins/metabolism, Cell Line, Cytoplasm/chemistry, Glycoproteins/chemistry, Glycoproteins/metabolism, Immunoprecipitation, Microscopy, Confocal, Protein Binding, Protein Processing, Post-Translational, Viral Envelope Proteins/chemistry, Viral Envelope Proteins/metabolism, Viral Matrix Proteins/metabolism, Viral Proteins/chemistry, Viral Proteins/metabolism, Virus Assembly/physiology
Pubmed
Web of science
Open Access
Yes
Create date
17/04/2013 11:56
Last modification date
20/08/2019 14:56
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