Javier M. Rodríguez

TL;DR: Electron microscopy studies revealed that polyprotein pp62 is necessary for the correct assembly and maturation of the core of the viral particle, and its repression leads to the appearance of a significant fraction of empty particles, to an increase in the number of immature-like particles, and to the accumulation of defective particles.

TL;DR: The finding that, in the absence of protein pB438L, the viral particles formed have a tubular structure in which the icosahedral symmetry is lost supports a role for this protein in the construction or stabilization of the ic Rosahedral vertices of the virus particle.

TL;DR: Cryo-EM three-dimensional reconstruction of uncleaved virions showed spikes with a structure compatible with the atomic model of the cleaved spike, and indistinguishable from that of digested particles, suggesting that the spike precursor protein must be proteolytically processed not to achieve a rigid conformation, but to allow the conformational changes that drive virus entry.

TL;DR: High-resolution two-dimensional gel electrophoresis with mass spectrometry with the aim of identifying proteins represented in the 2-D gel database of Drosophila melanogaster mitochondria identified 66 mitochondrial spots in the database and confirmed their identity by MALDI-TOF/TOF analysis.

TL;DR: The results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions in Rosellinia necatrix quadrivirus 1, indicating that Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface.