Pan, JunhuaDong, LipingLin, LiOchoa, Wendy F.Sinkovits, Robert S.Havens, Wendy M.Nibert, Max L.Baker, Timothy S.Ghabrial, Said A.Tao, Yizhi Jane2019-10-142009Pan, J., L. Dong, L. Lin, W. F. Ochoa, R. S. Sinkovits, W. M. Havens, M. L. Nibert, T. S. Baker, S. A. Ghabrial, and Y. J. Tao. 2009. “Atomic Structure Reveals the Unique Capsid Organization of a DsRNA Virus.” Proceedings of the National Academy of Sciences 106 (11): 4225–30. doi:10.1073/pnas.0812071106.0027-84240744-28311091-6490http://nrs.harvard.edu/urn-3:HUL.InstRepos:41543005For most dsRNA viruses, the genome-enclosing capsid comprises 120 copies of a single capsid protein (CP) organized into 60 icosahedrally equivalent dimers, generally identified as 2 nonsymmetrically interacting CP molecules with extensive lateral contacts. The crystal structure of a partitivirus, Penicillium stoloniferum virus F (PsV-F), reveals a different organization, in which the CP dimer is related by almost-perfect local 2-fold symmetry, forms prominent surface arches, and includes extensive structure swapping between the 2 subunits. An electron cryomicroscopy map of PsV-F shows that the disordered N terminus of each CP molecule interacts with the dsRNA genome and probably participates in its packaging or transcription. Intact PsV-F particles mediate semiconservative transcription, and transcripts are likely to exit through negatively charged channels at the icosahedral 5-fold axes. Other findings suggest that the PsV-F capsid is assembled from dimers of CP dimers, with an arrangement similar to flavivirus E glycoproteins.en-USJournal Article2019-10-1410.1073/pnas.0812071106