Most RNA viruses require a matrix protein for the packaging of the ribonucleoprotein SAR131675 complexes and release of viral particles, however viruses of the Bunyaviridae family do not encode a matrix protein. Based on our results, the Gn cytoplasmic tail appears to function in place of matrix and recruits RdRp, N and possibly, genomic RNA into virions. By Niraparib contrast, the cytosolic portion of Gc was dispensable for recruitment and packaging of RdRp, N and genome. Particles lacking N are inefficiently produced however, we were able to confirm that they contain genomic RNA. Although N is capable of non-specifically binding cellular RNA, efficient RVF-VLP release requires genomic RNA. These data suggest that genomic RNA is recognized specifically, possibly by Gn, since particles lacking the cytoplasmic portion of Gc are infectious and efficiently produced. Different regions of the Gn cytoplasmic tail are required for independent interactions with RdRp and N. The truncated Gn allele, GnK48, allowed us to define the sequences required for N and RdRp recruitment. The sequence on the Gn cytosolic tail required for interaction with N is located within the first 30 amino acids while that of the RdRp is in the last 40 amino acids. The Gn domain required for N interaction corresponds to a region that is highly hydrophobic. The hydrophobic character of this domain is conserved amongst phleboviruses. Binding of N and RdRp to Gn can occur independently. This observation may reflect the fact that there are few copies of RdRp and many copies of N within a virion. Thus, you would not expect that their binding to Gn would be mutually dependent. Studies performed with the Uukuniemi virus found that the Gn cytoplasmic tail is required for the packaging of N, but identified a different region as important for this interaction. The envelope glycoproteins and N of Uukuniemi virus are divergent from the rest of the phlebovirus genus, which may explain why our results contrast. Gn interaction with N is unlikely to be conserved across the five genera within family Bunyaviridae, as the envelope glycoproteins and N are not similar. The N of the hantaviruses independently localize to perinuclear membrane structures when expressed alone, suggesting a distinct mode of assembly. For tospoviruses, independent interactions between Gn and Gc with N were discovered, indicating a possible requirement for both glycoproteins during recruitment. We found no role for Gc in recruitment of N, genome and RdRp, however Gc is necessary for optimal Gn expression, efficient production of RVF-VLPs and possibly, infectivity. Studies performed on RVFV by Besselaar and Blackburn suggest a requirement for Gc in virus entry, as they were able to neutralize virus with antibodies recognizing Gc, either pre- or post- virus absorption.