Study On The Structure And Function Of The M?nglà Virus VP30 C-terminal Domain

There are many deadly viruses in the filamentous virus family that can cause severe hemorrhagic fever in humans and other primates,such as Ebola virus(EBOV)and Marburg virus(MARV).M?nglà virus(MLAV)is one of the newly discovered members of the filamentous viruses family and is considered to be a potential human pathogen.Among members of the Filaviridae family,VP30 is essential for virus assembly,transcription and replication processes.On the one hand,VP30 can be closely combined with VP35 and nucleoprotein(NP)during virus assembly.On the other hand,VP30 can affect the process of viral transcription and replication through dynamic phosphorylation and dephosphorylation.Therefore,research on the three-dimensional structure of MLAV VP30 protein is of great significance for further understanding of the assembly of filamentous virus and the process of transcription and replication.In addition,the analysis of the three-dimensional structure of the MLAV VP30 protein can also play an important foundation for subsequent drug development based on the structure of the filamentous virus VP30.In this study,the MLAV VP30 C-terminal domain(VP30 CTD)was selected for its three-dimensional structural and functional analysis:(1)The MLAV VP30 CTD recombinant protein that could be used for high-quality crystal preparation was constructed,and it was clearly defined that it existed in the form of dimer in the solution state.(2)The three-dimensional structure of MLAV VP30 CTD monomer is firstly analyzed,and then its overall structure,surface potential and hydrophobicity are systematically analyzed and compared.(3)The important role of H7 helix in the formation of MLAV VP30 CTD dimer is clarified.