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

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), consist...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of virology Jg. 81; H. 17; S. 9451
Hauptverfasser: Capul, Althea A, Perez, Mar, Burke, Emily, Kunz, Stefan, Buchmeier, Michael J, de la Torre, Juan C
Format: Journal Article
Sprache:Englisch
Veröffentlicht: United States 01.09.2007
Schlagworte:
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
ISSN:0022-538X
Online-Zugang:Weitere Angaben
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung: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.
Bibliographie:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0022-538X
DOI:10.1128/JVI.00499-07