Journal
JOURNAL OF VIROLOGY
Volume 81, Issue 17, Pages 9451-9460Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00499-07
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Funding
- NIAID NIH HHS [R56 AI047140, R01 AI047140, U54 AI065359, AI47140, T32 AI007354, AI-065359, AI-050840, R01 AI050840, T32 AI-07354] Funding Source: Medline
- NINDS NIH HHS [T32 NS041219, T32 NS041219-06] Funding Source: Medline
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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 coinimunoprecipitation 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.
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