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Blom, T.

Publications and source records attributed to Blom, T..

5 recordsLinked to original sources

Protein Abundance Inference via Expectation Maximization in Fluorosequencing

1Fluorosequencing produces millions of single-peptide reads, yet a principled strategy for converting these data into quantitative protein abundances has been lacking. We introduce a probabilistic framework that adapts expectation maximization to the fluorosequencing measurement process, estimating relative protein abundances with peptide inference results delivered by previously developed peptide-classification tools. The algorithm iteratively updates protein abundances, maximising the likelihood of the observed reads by obtaining more accurate protein abundance estimations. We first assess performance on simulated five-protein mixtures that reflect realistic labelling and system errors. A simple Python implementation processes one million reads in under ten seconds on a standard work-station and lowers the mean absolute error in relative abundance by more than an order of magnitude compared with a uniform-abundance guess, demonstrating robustness in protein inference for small-scale settings. Scalability is then evaluated with simulations of the complete human proteome (20 642 proteins). Ten million reads are processed in less than four hours on a NVIDIA DGX system using one Tesla V100 GPU, confirming that the method remains tractable at proteome scale. Using error rates characteristic of current fluorosequencing, the algorithm produces marginal improvements in relative abundance accuracy. However, when error rates were artificially lowered, estimation error decreased significantly. This result suggests that improvements in fluorosequencing chemistry could directly translate into substantially more accurate quantitative proteomics with this computational framework. Together, these results establish EM-based inference as a scalable model-driven bridge between peptide-level classification and protein-level quantification in fluorosequencing, laying computational groundwork for high-throughput single-molecule proteomics. Furthermore, the proposed protein inference framework can also be used as a refinement step within other inference methods, enhancing their protein abundance estimates. 2 Author summaryProteins carry out many of the functions inside our cells, but measuring how many copies of each protein are present remains a difficult task. The protein sequencing technology called fluorosequencing observes individual protein fragments one by one, producing millions of short "snapshots" in a single experiment. While this flood of data holds great promise, it is not yet clear how to turn the snapshots into reliable counts of the original proteins. In this study we developed a mathematical procedure, based on a classic "guess-and-improve" strategy called expectation maximization, that bridges this gap. Our program takes the computers best guesses for each fragment and repeatedly refines protein abundances until they best explain all of the measurements. Using realistic computer-generated data, we show that the method is both fast and accurate: it finishes in seconds for small mixtures and in only a few hours for the entire human set of proteins, both with accessible hardware. Because our approach can work with any future improvements in fragment interpretation, it lays the essential groundwork for bringing single-molecule protein sequencing into routine biological and medical use.

bioinformatics↗

Robust and scalable single-molecule protein sequencing with fluorosequencing

The need to accurately survey proteins and their modifications with ever higher sensitivities, particularly in clinical settings with limited samples, is spurring development of new single molecule proteomics technologies. Fluorosequencing is one such highly parallelized single molecule peptide sequencing platform, based on determining the sequence positions of select amino acid types within peptides to enable their identification and quantification from a reference database. Here, we describe substantial improvements to fluorosequencing, including identifying fluorophores compatible with the sequencing chemistry, mitigating dye-dye interactions through the use of extended polyproline linkers, and developing an end-to-end workflow for sample preparation and sequencing. We demonstrate by fluorosequencing peptides in mixtures and identifying a target neoantigen from a database of decoy MHC peptides, highlighting the potential of the technology for high sensitivity clinical applications.

molecular biology↗

Estimating error rates for single molecule protein sequencing experiments

The practical application of new single molecule protein sequencing (SMPS) technologies requires accurate estimates of their associated sequencing error rates. Here, we describe the development and application of two distinct parameter estimation methods for analyzing SMPS reads produced by fluorosequencing. A Hidden Markov Model (HMM) based approach, extends whatprot, where we previously used HMMs for SMPS peptide-read matching. This extension offers a principled approach for estimating key parameters for fluorosequencing experiments, including missed amino acid cleavages, dye loss, and peptide detachment. Specifically, we adapted the Baum-Welch algorithm, a standard technique to estimate transition probabilities for an HMM using expectation maximization, but modified here to estimate a small number of parameter values directly rather than estimating every transition probability independently, which should help prevent overfitting. We demonstrate a high degree of accuracy on simulated data, but on experimental datasets, we observed that the model needed to be augmented with an additional error type, N-terminal blocking. This, in combination with data pre-processing, results in reasonable parameterizations of experimental datasets that agree with controlled experimental perturbations. A second independent implementation using a hybrid of DIRECT and Powells method to reduce the root mean squared error (RMSE) between simulations and the real dataset was also developed. We compare these methods on both simulated and real data, finding that our Baum-Welch based approach outperforms DIRECT and Powells method by most, but not all, criteria. Although some discrepancies between the results exist, we also find that both approaches provide similar error rate estimates from experimental single molecule fluorosequencing datasets.

bioinformatics↗

Position representations of moving objects align with real-time position in the early visual response

AO_SCPLOWBSTRACTC_SCPLOWWhen localising a moving object, the brain receives outdated sensory information about its position, due to the time required for neural transmission and processing. The brain may overcome these fundamental delays through predictively encoding the position of moving objects using information from their past trajectories. In the present study, we evaluated this proposition using multivariate analysis of high temporal resolution electroencephalographic data. We tracked neural position representations of moving objects at different stages of visual processing, relative to the real-time position of the object. During early stimulus-evoked activity, position representations of moving objects were activated substantially earlier than the equivalent activity evoked by unpredictable flashes, aligning the earliest representations of moving stimuli with their real-time positions. These findings indicate that the predictability of straight trajectories enables full compensation for the neural delays accumulated early in stimulus processing, but that delays still accumulate across later stages of cortical processing.

neuroscience↗

Stability and sensitivity of structural connectomes: effect of thresholding and filtering and demonstration in neurodegeneration

Structural connectomes derived using diffusion tractography are increasingly used to investigate white matter connectivity in neurological diseases. However inherent biases in diffusion tractography algorithms may lead to both false negatives and false positives in connectome construction. A range of graph thresholding approaches and more recently several streamline filtering algorithms have been developed to address these issues. However there is no consensus in the literature regarding the best available approach. Using a cohort of Huntingtons disease patients and healthy controls we compared the effect of several graph thresholding strategies: proportional, absolute, consensus and consistency thresholding, with and without streamline filtering, using Spherical Deconvolution Informed Filtering of tractograms (SIFT2) algorithm. We examined the effect of thresholding strategies on the stability of graph theory metrics and the sensitivity of these measures in neurodegeneration. We show that while a number of graph thresholding procedures result in stable metrics across thresholds, the detection of group differences is highly variable. We also showed that the application of streamline filtering using SIFT2 resultes in better detection of group differences and stronger clinical correlations. We therefore conclude that the application of SIFT2 streamline filtering without graph thresholding may be sufficient for structural connectome construction.

neuroscience↗