Abstract
Rhabdoviruses, as single-stranded, negative-sense RNA viruses within the order Mononegavirales, are characterised by bullet-shaped or bacteroid particles that contain a helical ribonucleoprotein complex (RNP). Here, we review the components of the RNP and its higher-order structural assembly.
Highlights
Rhabdoviruses are negative-sense, single-strandedRNA viruses with a genome of about 10.8–16.1 kb
The small genome encodes the minimal set of five proteins that are all present in the virus particle. They consist of the nucleoprotein (N), the matrix protein (M), the surface glycoprotein (G), the phosphoprotein or polymerase cofactor (P) and the RNA-dependent RNA polymerase (L)
Lagos bat virus (LBV), aa 1–57 in vesicular stomatitis virus (VSV)) is mostly unresolved in the crystal structure, except residues 30–37 (LBV) and translation interfering with export of pocket mRNAs from the nucleus and the
Summary
Rhabdoviruses (family Rhabdoviridae, order Mononegavirales) are negative-sense, single-stranded. The small genome encodes the minimal set of five proteins that are all present in the virus particle. They consist of the nucleoprotein (N), the matrix protein (M), the surface glycoprotein (G), the phosphoprotein or polymerase cofactor (P) and the RNA-dependent RNA polymerase (L). The G-protein is the only surface glycoprotein, and the essential factor for virus attachment and entry, including fusion. The RNP’s main building blocks are the N- and M-proteins Both are structurally highly conserved between the genera. The locations of the M- and N-proteins are indicated by blue circles and purple particles at the same scale. The location of the G-protein is indicated by red triangles, and the size of purple rectangles, respectively. By employing 3dmod [7]
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