The replication of recombinant viruses harboring mutations in single Selleck SB203580 trafficking motifs was comparable to replication of wild-type virus. In contrast, viruses containing mutations in three or four of the trafficking signals showed pronounced deficits in replication with a reduction of

approximately 100-fold. Moreover, recombinant viruses expressing gpUL132 with three or four trafficking motifs mutated failed to incorporate the mutant protein into the virus particle. These results demonstrate a role of endocytosis of an HCMV envelope glycoprotein for incorporation into the virion and optimal virus replication.”
“Voltage-gated sodium channels are cell membrane glycoproteins responsible for action potential generation and propagation

in excitable cells. These large polypeptides which are comprised of 24 transmembrane segments organized into four domains require cellular factors to regulate channel maturation and sorting to different cellular compartments, anchoring the channels at plasma membrane, and modulating gating properties of these channels as effector molecules in the signal transduction pathway. Mutations of sodium channels or their cytosolic partners produce similar pathologies, providing a compelling evidence for the biological significance of channel complexes that form during channel biogenesis and following sorting to different cellular compartments and anchoring at plasma membrane. Genetic, biochemical and bioinformatic Carnitine palmitoyltransferase II approaches have been utilized to identify sodium channel partners. click here Here we review the important functional role of pan-sodium channel and isoform-specific partners in regulating sodium current density and gating properties. (C) 2010 Elsevier Ireland Ltd. All rights reserved.”
“The

morphogenesis and budding of virus particles represent an important stage in the life cycle of viruses. For Ebola virus, this process is driven by its major matrix protein, VP40. Like the matrix proteins of many other nonsegmented, negative-strand RNA viruses, VP40 has been demonstrated to oligomerize and to occur in at least two distinct oligomeric states: hexamers and octamers, which are composed of antiparallel dimers. While it has been shown that VP40 oligomers are essential for the viral life cycle, their function is completely unknown. Here we have identified two amino acids essential for oligomerization of VP40, the mutation of which blocked virus-like particle production. Consistent with this observation, oligomerization-deficient VP40 also showed impaired intracellular transport to budding sites and reduced binding to cellular membranes. However, other biological functions, such as the interaction of VP40 with the nucleoprotein, NP, remained undisturbed.