Mechanisms and Research Methods of Protein Modification in Virus Entry

Protein interactions are of paramount importance for the performance of biological functions within organisms. Post-translational modifications, including glycosylation and phosphorylation, regulate protein-protein interactions through non-covalent mechanisms. Glycosylation typically facilitates binding by altering surface properties, whereas phosphorylation can either enhance or disrupt interactions depending on context, collectively amplifying the biological impact of proteins. The entry of viruses and certain intracellular parasites into host cells is facilitated by these modifications, which permit the binding of ligands to receptors and the traversal of the cell membrane barrier. As research in this domain progresses, innovative methodologies are being developed, including protein microarrays and proximity-labeling techniques. These developments are being increasingly employed in disease prevention, therapeutics, and fundamental medical research. In light of the recent surge in emerging infectious diseases, the study of protein interactions has assumed heightened relevance. This review explores protein modifications, including glycosylation, phosphorylation, and ubiquitination, and focuses on their roles in viral entry. It highlights advanced methods for analyzing protein-protein interactions (PPIs), notably proximity labeling and protein microarrays, and concludes with novel insights into therapeutic development, aiming to inspire innovation in this evolving field.