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<p>The E6 oncoprotein from Human Papillomavirus type 16 (HPV16) interacts with PDZ-domain proteins such as DLG1, a key regulator of cell polarity and proliferation. In this study, we used an in silico approach to investigate the predicted interactions between the reference E6 protein and five variants using a domain-focused model of DLG1 in phosphorylated and non-phosphorylated states. Protein–protein docking analyses revealed variant-dependent differences in predicted binding affinity. Notably, the E-C188/G350 and AAa variants showed stronger predicted binding to the non-phosphorylated form of DLG1. In contrast, all variants exhibited reduced predicted affinity for the phosphorylated form, while the reference E6 displayed comparatively higher predicted binding. These observations suggest a preferential predicted interaction of E6 variants with the cytoplasmic, non-phosphorylated pool of DLG1, whereas the reference E6 may preferentially interact with phosphorylated DLG1. Overall, our findings provide predictive structural insights into the differential behavior of HPV16 E6 variants in their interaction with DLG1 and establish a framework for future experimental validation.</p>

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Molecular Dynamics and Docking Reveal Enhanced Binding of HPV16 E6 Asian American Variants To non-phosphorylated DLG1

  • 期刊论文

  • 发表日期：

    2026年1月17日

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  • Lilian Esmeralda Araujo-Arcos,
  • Sarita Montaño,
  • Ciresthel Bello-Rios,
  • Olga Lilia Garibay-Cerdenares,
  • Marco Antonio Leyva-Vázquez,
  • Berenice Illades-Aguiar

摘要

The E6 oncoprotein from Human Papillomavirus type 16 (HPV16) interacts with PDZ-domain proteins such as DLG1, a key regulator of cell polarity and proliferation. In this study, we used an in silico approach to investigate the predicted interactions between the reference E6 protein and five variants using a domain-focused model of DLG1 in phosphorylated and non-phosphorylated states. Protein–protein docking analyses revealed variant-dependent differences in predicted binding affinity. Notably, the E-C188/G350 and AAa variants showed stronger predicted binding to the non-phosphorylated form of DLG1. In contrast, all variants exhibited reduced predicted affinity for the phosphorylated form, while the reference E6 displayed comparatively higher predicted binding. These observations suggest a preferential predicted interaction of E6 variants with the cytoplasmic, non-phosphorylated pool of DLG1, whereas the reference E6 may preferentially interact with phosphorylated DLG1. Overall, our findings provide predictive structural insights into the differential behavior of HPV16 E6 variants in their interaction with DLG1 and establish a framework for future experimental validation.