Kalhor Mostafa, Saylan Cemil Can, Picciani Mario, Fischer Lutz, Schimweg Falk Boudewijn, Lapin Joel, Rappsilber Juri, Wilhelm Mathias
Computational Mass Spectrometry, TUM School of Life Sciences, Technical University of Munich, Freising, Germany.
Bioanalytics, Institute of Biotechnology, Technical University Berlin, Berlin, Germany.
Nat Commun. 2025 Jul 1;16(1):5429. doi: 10.1038/s41467-025-61203-4.
It has been shown that integrating peptide property predictions such as fragment intensity into the scoring process of peptide spectrum match can greatly increase the number of confidently identified peptides compared to using traditional scoring methods. Here, we introduce Prosit-XL, a robust and accurate fragment intensity predictor covering the cleavable (DSSO/DSBU) and non-cleavable cross-linkers (DSS/BS3), achieving high accuracy on various holdout sets with consistent performance on external datasets without fine-tuning. Due to the complex nature of false positives in XL-MS, an approach to data-driven rescoring was developed that benefits from Prosit-XL's predictions while limiting the overestimation of the false discovery rate (FDR). After validating this approach using two ground truth datasets consisting of synthetic peptides and proteins, we applied Prosit-XL on a proteome-scale dataset, demonstrating an up to ~3.4-fold improvement in PPI discovery compared to classic approaches. Finally, Prosit-XL was used to increase the coverage and depth of a spatially resolved interactome map of intact human cytomegalovirus virions, leading to the discovery of previously unobserved interactions between human and cytomegalovirus proteins.
研究表明,与使用传统评分方法相比,将诸如片段强度等肽属性预测整合到肽谱匹配的评分过程中,可以大大增加可靠鉴定的肽的数量。在此,我们介绍了Prosit-XL,这是一种强大且准确的片段强度预测器,涵盖可裂解(DSSO/DSBU)和不可裂解交联剂(DSS/BS3),在各种保留集上实现了高精度,在外部数据集上具有一致的性能,无需微调。由于交联质谱中假阳性的复杂性质,开发了一种数据驱动的重新评分方法,该方法受益于Prosit-XL的预测,同时限制了对错误发现率(FDR)的高估。在使用由合成肽和蛋白质组成的两个真实数据集验证了该方法后,我们将Prosit-XL应用于蛋白质组规模的数据集,结果表明与经典方法相比,蛋白质-蛋白质相互作用(PPI)发现最多提高了约3.4倍。最后,Prosit-XL被用于增加完整人类巨细胞病毒病毒粒子空间分辨相互作用组图谱的覆盖范围和深度,从而发现了人类和巨细胞病毒蛋白质之间以前未观察到的相互作用。