Viral and host proteins that modulate filovirus budding

Abstract

The filoviruses, Ebola and Marburg, utilize a multifaceted mechanism for assembly and budding of infectious virions from mammalian cells. Growing evidence not only demonstrates the importance of multiple viral proteins for efficient assembly and budding, but also the exploitation of various host proteins/pathways by the virus during this late stage of filovirus replication, including endocytic compartments, vacuolar protein sorting pathways, ubiquitination machinery, lipid rafts and cytoskeletal components. Continued elucidation of these complex and orchestrated virus-host interactions will provide a fundamental understanding of the molecular mechanisms of filovirus assembly/budding and ultimately lead to the development of novel viral- and/or host-oriented therapeutics to inhibit filovirus egress and spread. This article will focus on the most recent studies on host interactions and modulation of filovirus budding and summarize the key findings from these investigations.

Figure 1. Bimolecular complementation assay

Human 293T cells were transfected with (A) N-terminal yellow fluorescent protein (NYFP)-tumor susceptibility gene (Tsg)101 alone, (B) C-terminal YFP (CYFP)-Ebola virus (EBOV) VP40 alone, (C) CYFP-Marburg virus VP40 alone, (D) NYFP-Tsg101 plus CYFP-EBOV VP40-ΔPT/PY, (E) NYFP-Tsg101 plus CYFP-EBOV VP40 or (F) NYFP-Tsg101 plus CYFP-Marburg virus VP40. Cells were examined at 24 h post-transfection for YFP fluorescence activity by confocal microscopy using a Zeiss LSM-510 Meta system.