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A luciferase-based budding assay for Ebola virus.

Authors
  • McCarthy, Sarah E
  • Licata, Jillian M
  • Harty, Ronald N
Type
Published Article
Journal
Journal of Virological Methods
Publisher
Elsevier
Publication Date
Oct 01, 2006
Volume
137
Issue
1
Pages
115–119
Identifiers
PMID: 16837071
Source
Medline
License
Unknown

Abstract

The VP40 matrix protein of Ebola virus (EBOV) is capable of budding from mammalian cells as a virus-like particle (VLP) and is the major protein involved in virus egress. A functional budding assay has been developed based upon this characteristic of VP40 to assess the contributions of VP40 sequences as well as host proteins to the budding process. This well-defined assay has been modified for potential use in a high-throughput format in which the detection and quantification of firefly luciferase protein in VLPs represents a direct measure of VP40 budding efficiency. Luciferase was found to be incorporated into budding VP40 VLPs. Furthermore, co-expression of EBOV glycoprotein (GP) enhances release of VLPs containing VP40 and luciferase. In contrast, when luciferase is co-expressed with a budding deficient mutant of VP40, luciferase levels in the VLP fraction decrease significantly. This assay represents a promising high-throughput approach to identify inhibitors of EBOV budding.

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