Alfalfa mosaic virus replicase proteins, P1 and P2, localize to the tonoplast in the presence of virus RNA.

To identify the virus components important for assembly of the Alfalfa mosaic virus replicase complex, we used live cell imaging of Arabidopsis thaliana protoplasts that expressed various virus cDNAs encoding native and GFP-fusion proteins of P1 and P2 replicase proteins and full-length virus RNAs. Expression of P1-GFP alone resulted in fluorescent vesicle-like bodies in the cytoplasm that colocalized with FM4-64, an endocytic marker, and RFP-AtVSR2, RabF2a/Rha1-mCherry, and RabF2b/Ara7-mCherry, all of which localize to multivesicular bodies (MVBs), which are also called prevacuolar compartments, that mediate traffic to the lytic vacuole. GFP-P2 was driven from the cytosol to MVBs when expressed with P1 indicating that P1 recruited GFP-P2.

Normal basilar artery structure and biaxial mechanical behaviour.

Much is known about cerebral vasospasm, a devastating sequela to ruptured intracranial aneurysms, yet underlying mechanisms remain unclear and clinical treatments have proven unsatisfactory. We have hypothesised that biochemical stimuli associated with the formation of extravascular blood clots dominate early maladaptive responses, leading to marked structural and functional changes in affected cerebral arteries. Before a precise picture of vasospasm can be obtained, however, we must understand better the structure and mechanical behaviour of normal cerebral arteries.