We are fascinated by the functioning of ribonucleoprotein complexes, macromolecular assembbies made of RNA and RNA-binding proteins that exist inside the cell and are the site of fundamental proceses such as protein syntheis, mRNA quality control and degradation, signaling and, as we and others recently discovered, antiviral defense mechanisms. The best known ribonucleoprotein complex is the ribosome, the machinery responsible for protein syntheis. Many viruses also form their own RNA-protein comlexes that, similarly to microscopic photocopy machines, multiply the viral genomes and orchestrate the assembly of new progeny. Viruses also modify cellular ribonucleoprotein complexes, including ribosomes, stress-granules and P-bodies, to take control of protein synthesis and other fundamental cellular functions. How does this happen? We want to identify key cellular and viral regulators of these proceses and find ways to interfere with the virus replication program.