Szalmás, AnitaDagane, Abdinoor2026-06-112026-06-112026-06-05https://hdl.handle.net/2437/409420This thesis investigates how a naturally occurring A45S amino acid substitution in the HPV11 E7 oncoprotein affects its biological function and potential role in disease progression. The study found that the HPV11 A2 (S45) variant more effectively degrades pRb family proteins, leading to enhanced activation of E2F-regulated genes compared to the prototype HPV11 A1 variant. Increased expression of DNA repair genes, including BRCA1, BRCA2, RAD51, and ATM, was observed in keratinocytes expressing the S45 variant, suggesting stronger modulation of host cellular pathways. Additionally, cells expressing HPV11 S45 E7 exhibited reduced cytotoxicity and improved viability, indicating a greater capacity to support viral persistence. Overall, the findings suggest that the A45S polymorphism gives HPV11 E7 high-risk-like molecular properties that may contribute to the aggressiveness and persistence of HPV11-associated diseases such as recurrent respiratory papillomatosis.33enHuman Papillomavirus, E7, E2F, RetinoblastomaMedicine::Medical microbiologyBiology::Molecular BiologyHozzáférhető a 2022 decemberi felsőoktatási törvénymódosítás értelmében.