Download MendeleyCrystal Structure of the Marburg Virus VP35 Oligomerization Domain.
Bruhn, J.F., Kirchdoerfer, R.N., Urata, S.M., Li, S., Tickle, I.J., Bricogne, G., Saphire, E.O.(2017) J Virol 91
- PubMed: 27847355
- DOI: https://doi.org/10.1128/JVI.01085-16
- Primary Citation of Related Structures:
5TOH, 5TOI - PubMed Abstract:
Marburg virus (MARV) is a highly pathogenic filovirus that is classified in a genus distinct from that of Ebola virus (EBOV) (genera Marburgvirus and Ebolavirus, respectively). Both viruses produce a multifunctional protein termed VP35, which acts as a polymerase cofactor, a viral protein chaperone, and an antagonist of the innate immune response. VP35 contains a central oligomerization domain with a predicted coiled-coil motif. This domain has been shown to be essential for RNA polymerase function. Here we present crystal structures of the MARV VP35 oligomerization domain. These structures and accompanying biophysical characterization suggest that MARV VP35 is a trimer. In contrast, EBOV VP35 is likely a tetramer in solution. Differences in the oligomeric state of this protein may explain mechanistic differences in replication and immune evasion observed for MARV and EBOV.
Organizational Affiliation:
Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.
