Rift Valley Fever Virus (RVFV) is a significant pathogen known for causing severe febrile illness and hemorrhagic fever in humans and substantial economic losses in livestock. The virus is a member of the Phlebovirus genus in the Bunyaviridae family, with a segmented RNA genome that encodes essential proteins for viral replication and transcription. Among these, the L protein is a critical component of the viral RNA polymerase complex, responsible for synthesizing viral RNA. Despite its pivotal role, the detailed tertiary structure of the L protein remains poorly characterized. The primary objective of this study is to elucidate the tertiary structure of the RVFV L protein using a combination of structural biology techniques. By understanding the spatial arrangement of this protein, we aim to uncover its functional mechanisms and identify potential targets for therapeutic intervention. A multi-faceted approach was employed, integrating bioinformatics, molecular modeling, X-ray crystallography and cryo-Electron Microscopy (cryo-EM). Computational tools were used to predict structural features, while experimental methods provided highresolution structural data. Structural models were validated through comparisons with homologous proteins and functional assays to ascertain their biological relevance.
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Molecular Biology: Open Access received 607 citations as per Google Scholar report
