Our results suggest that satsiR-12 targeting the 3′ UTR of CMV RNAs triggered RDR6-dependent antiviral silencing. Competition experiments with wild-type CMV RNAs and anti-satsiR-12 mutant RNA1 in the JQ-EZ-05 research buy presence of 2b and satRNA demonstrate the inhibitory effect of the 2b protein on the satsiR-12-related degradation of CMV RNAs, revealing a substantial suppressor function of the 2b protein in native CMV infection. Our data provide evidence for the important biological functions

of satsiRNAs in homeostatic interactions among the host, virus, and satRNA in the final outcome of viral infection.”
“The Arabidopsis thaliana somatic embryogenesis receptor-like kinase (SERK) family consists of five leucine-rich repeat receptor-like kinases (LRR-RLKs) with diverse functions such as brassinosteroid insensitive 1 (BRI1)-mediated brassinosteroid perception, development and innate immunity. The autophosphorylation activity of the kinase domains of the five SERK proteins was compared and the phosphorylated residues were identified by LC-MS/MS. Differences in autophosphorylation that ranged from high

activity of SERK1, intermediate activities for SERK2 and SERK3 to low activity for SERK5 were noted. In the SERK1 kinase the C-terminally located residue Ser-562 controls full autophosphorylation activity. Activation loop phosphorylation, Selleck IPI145 including that of residue Thr-462 previously shown to be required for SERK1 kinase activity, was not affected. In vivo SERK1. phosphorylation was induced by brassinosteroids. Immunoprecipitation of CFP-tagged SERK1 from plant extracts followed by MS/MS identified Ser-303, Thr-337, Thr-459, Thr-462, Thr-463, Thr-468, and Ser-612 or Thr-613

or Tyr-614 as in vivo phosphorylation sites of SERK1. Transphosphorylation of SERK1 OICR-9429 mw by the kinase domain of the main brassinosteroid receptor BRI1. occurred only on Ser-299 and Thr-462. This suggests both intra- and intermolecular control of SERK1 kinase activity Conversely, BRI1 was transphosphorylated by the kinase domain of SERK1 on Ser-887. BRI1 kinase activity was not required for interaction with the SERK1 receptor in a pull down assay.”
“This review critically examines an emerging tool to measure viral clearance from biomanufacturing streams, monitor assembly of viruses and virus-like particles, rapidly identify viruses from biological milieu, assay virus neutralization, and prepare bionanoconjugates for bacterial detection. Electrospray differential mobility analysis (ES-DMA) is a tool of choice to simultaneously determine viral size and concentration because it provides full multimodal size distributions with subnanometer precision from individual capsid proteins to intact viral particles. The review contrasts ES-DMA to similar tools and highlights expected growth areas including at-line process sensing as a process analytical technology (PAT), bioseparating as a distinct unit operation, monitoring viral reactions, and interrogating virus host protein interactions.