<P> Another important process utilized throughout many cellular processes is ubiquitination - which is outlined in the image below . This is utilized in many cells in order to locate and identify viruses, as well as, restrict the viral infection throughout . NNSVs however have developed a pathway to synthesize proteins which target the ubiquitin pathway along many of the signaling cascades descriptive of the IFN response . More specifically, the NNSVs are capable of reprogramming the host cell's ubiquitination pathway in such a way that leads to the degradation of host cell mechanism that would otherwise silence a viral infection . </P> <P> Like all viruses, negative - sense RNA viruses (NSVs) contain a protein capsid that encapsulates the genomic material . The nucleocapsid of NSVs is assembled with a single nucleocapsid protein, and the viral RNA . Each NSV nucleocapsid is packaged inside a lipid envelope, but the appearance of the nucleocapsid differs from virus to virus . For example, in rhabdoviruses, the nucleocapsid assumes a bullet shape, while in paramyxoviruses, the nucleocapsid is filamentous or herringbone - like . However, when the nucleocapsids are released from the virion, they all appear like a coil . </P> <P> So far, the atomic structures of nucleocapsid - like - particles (NLP) have been elucidated for three NSV families: Rhabdoviridae, Paramyxoviridae, and Bunyaviridae . One important element of NSVs is that the capsid protein (N) is first synthesized as a monomeric protein (N0). N0 is a capsid protein that assembles a capsid to accommodate any RNA sequence . N0 is kept monomeric in different ways depending on which family of NSVs a virus falls into . For instance, rhabdoviruses keep the N0 monomeric by forming a complex with the phosphoprotein (P). It has been found that both the N - and C terminal regions of P bind to the capsid protein . Essentially, the P binding occupies the site required for N0 oligomerization . Other viruses, such as bunyaviruses, simply sequester the N terminus by N itself . Nonetheless, it is essential for N to be monomeric in order for the NSV to be competent in encapsidating viral RNA . </P> <P> In terms of the structure of the nucleocapsid, the N protein will eventually oligomerize to encapsidate the single - stranded RNA . In some NSVs the N subunits are oriented in a parallel orientation, and the ssRNA is sequestered in the center . In most NSVs, the nucleocapsid appears to be a random coil, and the symmetry is linear . Because the N subunits are oriented in a parallel fashion, the cross-molecular interactions among the subunits stabilize the nucleocapsid and are critical for capsid formation . The linear interactions along the encapsidated single - stranded RNA are actually a unique feature to NSVs . X-ray crystal structures of N proteins and EM micrographs of RNP complexe s from a number of Bunyaviridae (a Family of segmented NSVs that includes the Bunyamwera virus and the Schmallenberg virus) show that in these viruses the nucleocapsid adopts a helical arrangement where the N proteins form a head - to - tail chain by linking to each other via a flexible N - terminal arm . The resulting chain forms tight coils with four N proteins per turn that holds the circular ssRNA of these viruses on the inside of the coils and which extend to form large circular filaments . </P>

The minus strand of dna serves as the template for rna production