RPL7 is a structural component of the large ribosomal subunit (60S) that plays essential roles in protein synthesis and ribosome biogenesis 123. The protein binds to G-rich structures in 28S rRNA and mRNAs, exerting regulatory functions in the translation apparatus by inhibiting cell-free translation 1. Beyond canonical ribosomal functions, RPL7 participates in cellular processes involving RNA binding and rRNA processing 4. In viral contexts, RPL7 interacts with HTLV-1 Gag through zinc finger domains and is packaged into virions, where it functions as a co-chaperone facilitating tRNA annealing to the primer binding site during reverse transcription 5. This interaction represents a novel mechanism by which retroviruses exploit host ribosomal proteins. Clinically, RPL7 demonstrates relevance to multiple pathologies. It was identified as a biomarker overexpressed in thin endometrium, associated with abnormal immune regulation and female infertility 6. Additionally, RPL7 appears dysregulated in systemic autoimmune diseases, where it may serve as part of a diagnostic signature discriminating autoimmunity from infection 7. The protein is also recognized as an autoantigen in systemic lupus erythematosus, triggering T cell and B cell responses 8. Early exposure to bacterial ribosomal protein homologs associates with colorectal cancer progression 9, suggesting potential links between microbial antigens and malignant transformation.