Our group has been investigating the molecular mechanisms involving proteins and nucleic acids in two virus models representative of DNA and RNA viruses and both of strong public health impact, and also selected for being minimal biological pathogenic entities. The human papillomavirus (HPV, 8 kbp DNA genome) was the first virus to be associated with cancer and partakes in uterine and oropharyngeal cancers. We have been addressing the biochemical mechanisms involved in oncogenesis (E6 and E7), transcription regulation (E2) and capsid assembly (L1). The respiratory syncytial virus (RSV, 15 kb RNA genome) is responsible for bronchiolitis in infants, immunocompromised and elderly patients. We have been investigating how the key replication proteins (N, P, M2-1, and L) interact and assemble in replication complexes, and the protein responsible for it s anti-interferon activity (NS1). During the last five years both systems led us to investigate their properties to form biomolecular condensates, recently discovered dynamic membraneless structures based on a chemical principle of liquid-liquid phase separation (LLPS), a field that revolutionized our understanding of cellular biochemistry, function and pathology, present in all kingdoms of life. We have dissected the main players and the accessory roles of the viral proteins involved in the assembly of RSV condensates, while other groups showed that viral replication and assembly factories are indeed liquid membraneless condensates. We also investigated the condensation mechanism of the nucleoprotein of SARS CoV2 with RNA. On the HPV front we established a condensation mechanism between the master regulator E2 and the transcriptional regulator p53 related to a replication inhibition mechanism. In doing so, we also determined a strong tendency of p53 itself to form condensates and entering an amyloid pathway, similar to neuropathies, that is being the focus of study as a likely cause of the gain-of-function activity of p53 in triggering cancer, given that it is the most mutated protein in cancer, in 50% of all tumors. We are focusing on p53 amyloids as neoantigens and aim at producing selective antibody tools for the clinic. Current understanding of assembly and modulation of condensates is at the center of fundamental understanding behind physiology and pathology, and provides novel platforms for drug discovery only beginning to emerge.