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Benasolo, C. A.

Publications and source records attributed to Benasolo, C. A..

2 recordsLinked to original sources

StructGuy: Data leakage free prediction of functional effects of genetic variants.

The extent to which variations in protein-coding genes affect protein function has drawn the biological machine learning communitys attention to computationally model variant effect prediction tools. Multiplexed assays of variant effects (MAVE) experiments serve as a rich data source, but cannot deliver enough data for training truly large neural-net models. Therefore, zero-shot methods, for example protein language models, have increasingly gained popularity. For these methods, MAVE results serve primarily for evaluation purposes, as exemplified by the ProteinGym benchmark. In this study, we argue that the rapidly increasing amounts of MAVE data can be used to train efficient supervised methods, presenting our new tool StructGuy, based on gradient boosting trees methodology. In contrast to other supervised methods in the field, StructGuy, thanks to its dedicated training dataset and data leakage-free training process, can predict variant effects for proteins not seen during training. To evaluate this generalization ability, we constructed a dedicated benchmark and compared StructGuy with zero-shot methods from the ProteinGym leaderboard achieving a competitive performance. Further, we demonstrate that thanks to its architecture and careful feature engineering, we are able to provide fully interpretable predictions and direct explanations of the influence of mutations on protein three-dimensional structure, which favourably differs StructGuy from zero-shot tools.

bioinformatics↗

Uncoupling sodium channel dimers rescues phenotype of pain-linked Nav1.7 mutation

The voltage-gated sodium channel Nav1.7 is essential for an adequate perception of painful stimuli. Its mutations cause various pain syndromes in human patients. The hNav1.7/A1632E mutation induces symptoms of erythromelalgia and paroxysmal extreme pain disorder (PEPD), and its main gating change is a strongly enhanced persistent current.\n\nUsing molecular simulations, we demonstrate that the disease causing persistent current of hNav1.7/A1632E is due to impaired binding of the IFM motif, thus affecting proper function of the recently proposed allosteric fast inactivation mechanism. By using native polyacrylamide gel electrophoresis (PAGE) gels, we show that hNav1.7 dimerizes. The disease-linked persistent current depends on the channels functional dimerization status: Using difopein, a 14-3-3 inhibitor known to uncouple dimerization of hNav1.5, we detect a significant decrease in hNav1.7/A1632E induced persistent currents.\n\nOur work identifies that functional uncoupling of hNav1.7/A1632E dimers rescues the pain-causing molecular phenotype by interferes with an allosteric fast inactivation mechanism, which we link for the first time to channel dimerization. Our work supports the concept of sodium channel dimerization and reveals its relevance to human pain syndromes.

neuroscience↗