5nd1

Publication Abstract from PubMed

Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 A resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-A-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar alpha-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface.

Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses.,Mata CP, Luque D, Gomez-Blanco J, Rodriguez JM, Gonzalez JM, Suzuki N, Ghabrial SA, Carrascosa JL, Trus BL, Caston JR PLoS Pathog. 2017 Dec 8;13(12):e1006755. doi: 10.1371/journal.ppat.1006755., eCollection 2017 Dec. PMID:29220409^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.