Journal of Virology · 2007 · 110 citations · 39 references
Life SciencesInfectious DiseasesMolecular BiologyHost-pathogen InteractionsMolecular VirologyVirologyHost-virus InteractionsViral EntryViral InfectionsViral PathogenesisViral StructureVirus-host InteractionsMarburg Virus DiseaseProtein Matrix OrganizationProtein-matrix InteractionsViral Budding MechanismsViral Surface ProteinsVirus-host Protein InteractionsVirus-like Particles
Marburg virus (MARV) VP40 is a matrix protein that can be released from mammalian cells in the form of virus-like particles (VLPs) and contains the PPPY sequence, which is an L-domain motif. Here, we demonstrate that the PPPY motif is important for VP40-induced VLP budding and that VLP production is significantly enhanced by coexpression of NP and GP. We show that Tsg101 interacts with VP40 depending on the presence of the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and plays an important role in VLP budding. These findings provide new insights into the mechanism of MARV budding.
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Tsg101 and the Vacuolar Protein Sorting Pathway Are Essential for HIV-1 Budding
Jennifer Garrus, Uta K. von Schwedler, Owen Pornillos et al. · Cell · 2001 · 1.4K citations · Full text