RT Journal Article
T1 Regulation of Ebola virus VP40 matrix protein by SUMO
A1 Baz-Martínez, Maite
A1 El Motiam, Ahmed
A1 Ruibal, Paula
A1 Condezo Castro, Gabriela Nérida
A1 Cruz Herrera, Carlos F. de la
A1 Lang, Valerie
A1 Collado Rodríguez, Manuel
A1 San Martín, Carmen
A1 Rodríguez, Manuel S.
A1 Muñoz Fontela, Cesar
A1 Rivas, Carmen
K1 Ebola virus
K1 Post-translational modifications
AB The matrix protein of Ebola virus (EBOV) VP40 regulates viral budding, nucleocapsid recruitment, virus structure and stability, viral genome replication and transcription, and has an intrinsic ability to form virus-like particles. The elucidation of the regulation of VP40 functions is essential to identify mechanisms to inhibit viral replication and spread. Post-translational modifications of proteins with ubiquitin-like family members are common mechanisms for the regulation of host and virus multifunctional proteins. Thus far, no SUMOylation of VP40 has been described. Here we demonstrate that VP40 is modified by SUMO and that SUMO is included into the viral like particles (VLPs). We demonstrate that lysine residue 326 in VP40 is involved in SUMOylation, and by analyzing a mutant in this residue we show that SUMO conjugation regulates the stability of VP40 and the incorporation of SUMO into the VLPs. Our study indicates for the first time, to the best of our knowledge, that EBOV hijacks the cellular SUMOylation system in order to modify its own proteins. Modulation of the VP40-SUMO interaction may represent a novel target for the therapy of Ebola virus infection
PB Nature Publishing Group
YR 2016
FD 2016-11-16
LK http://hdl.handle.net/10347/15973
UL http://hdl.handle.net/10347/15973
LA eng
NO Baz-Martínez M, El Motiam A, Ruibal P, Condezo G, de la Cruz-Herrera C, Lang V et al. Regulation of Ebola virus VP40 matrix protein by SUMO. Scientific Reports. 2016;6(1)
NO We thank Sergio Gomez-Medina for excellent technical assistance. Funding at the laboratory of CR is provided by BFU-2014-58530. Work at the laboratory of CSM is supported by BFU2013-41249-P. This work was partially funded by the Lebniz Association (Prämie ERC Starting Grant 2013 to CM-F). The Heinrich-Pette-Institute is financed by the German Federal Ministry of Health and the Freie und Hansestadt Hamburg. AEM is supported by the Spanish Ministry of Economy and Competitiveness (FPI Fellowship). CFC-H is supported by CONACYT. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript
DS Minerva
RD 3 may 2026