Ronald N. Harty

TL;DR: The data demonstrate that the VP40 protein of Ebola virus possesses a PY motif that is functionally similar to those described previously for Gag and M proteins of specific retroviruses and rhabdoviruses, respectively, and imply that VP40 likely plays an important role in filovirus budding.

TL;DR: Evidence of antiviral activity of ISG15 against Ebola virus is provided and a mechanism of action involving disruption of Nedd4 function and subsequent ubiquitination of VP40 is suggested.

TL;DR: Results indicate that both the PTAP and PPEY motifs contribute to efficient budding of VP40-containing VLPs, and provide important insights into the complex interplay between viral and host proteins during the late stages of Ebola virus budding.

TL;DR: It is demonstrated that VP24 alone does not affectVP40 VLP release, whereas NP and GP enhance release of VP40 VLPs, individually and to a greater degree in concert.

TL;DR: To demonstrate further that ubiquitin may be involved in the budding process of rhabdoviruses, proteasome inhibitors were used to decrease the level of free Ubiquitin in VSV- and RV-infected cells, suggesting that free ubiquitIn is important for efficient virus budding.