Cellular proteins undergo a diverse array of modifications following their synthesis. These post-translational modifications (PTMs) dramatically impact protein function, localization, and interactions, thereby regulating nearly all cellular processes. Examples of these modifications include phosphorylation, ubiquitination, glycosylation, and acetylation, each introducing distinct chemical changes that alter a protein’s properties. Viruses, being obligate intracellular parasites, manipulate these host cell processes to facilitate their own replication and spread.
This manipulation is critical for viral survival. By hijacking cellular PTM machinery, viruses can enhance their own protein production, evade immune detection, and promote viral assembly and release. Understanding these viral strategies provides insight into fundamental aspects of viral pathogenesis. Historically, research into these interactions has led to the development of antiviral therapies targeting specific PTM pathways, demonstrating the practical significance of this area of study.
