Search bioRxiv⌕ Search

Biology subjects

Leda Valverde, A.

Publications and source records attributed to Leda Valverde, A..

2 recordsLinked to original sources

Asking the Data: Conversational Interrogation of LC-MS/MS Proteomics Data Sets with an LLM Agent

Proteomics workflows are designed to answer predefined questions, leaving analytical problems that emerge after first results difficult to investigate without additional bioinformatics work. We introduce data set interrogation, a conversational framework in which a researcher uses a large language model (LLM) agent to translate emerging questions into executable tests, check the answers against controls, and keep the code, inputs, and decisions in a dated record. Applied retrospectively to four LC-MS/MS data sets, the framework exposed problems that changed the interpretation of three in-house studies: a search database lacking one of two symbionts, a swapped pair of tandem mass tag (TMT) channels, statistics inflated by non-host proteins, and false deamidation assignments caused by selection of the 13C isotope peak as monoisotopic; the same question asked of every data set revealed failed or partial cysteine alkylation in all three. A public TMT data set was reanalyzed from raw files in 24 min, a feasibility measure without a human comparison; among spectra identified by both workflows, 99.2% received the same peptide assignment as in Proteome Discoverer, and protein fold changes correlated (r = 0.93). In seeded tests, a purpose built channel assignment check detected all 216 between strain channel swaps and none of 90 within-strain swaps. The framework couples natural language interaction with executable analyses, explicit controls, and traceable decisions, enabling researchers to investigate questions not anticipated by the original pipeline. These results establish feasibility in a limited retrospective setting with one researcher; broader evaluation across users, models, and data sets is required to determine general performance.

bioinformatics↗

Sample Preparation and Homology-Driven Search Shape the First Holobiont Proteome of the Marine Sponge Viles ophiraphidites (formerly Topsentia ophiraphidites)

Marine sponges are holobionts of host cells, extracellular matrix and dense microbial communities, and most lack reference proteomes. Viles ophiraphidites (formerly Topsentia ophiraphidites), a Brazilian demosponge, is represented in UniProtKB by a single protein. The study had two phases. In phase 1, four sample preparation workflows were compared on two specimens in 42 nLC-MS/MS runs: urea/thiourea in-solution digestion, acetone precipitation, S-Trap and GeLC-MS/MS. Every run was analysed with FragPipe and with a homology-driven pipeline that adds three layers to a rescored Sage search: the proteome of the closest sequenced relative (Halichondria panicea), MS-BLAST style alignment of de novo sequence tags, and error-tolerant interpretation of tag flanks. In phase 2, the selected workflow, S-Trap, was applied to four specimens in 12 runs. Both strategies ranked the workflows identically ({rho} = 0.98). S-Trap gave the deepest and most specimen independent proteome, with about 2,100 protein groups per specimen and an 8% difference between specimens, against 21-39% for the other workflows. The homology-driven layers raised assigned non-contaminant spectra by 21.3% in phase 1 and 26.8% in phase 2. They contributed 1,969 protein groups found only by homology and agreed with the database search on 99.5-99.9% of shared spectra. The proteome comprises 4,294 protein groups: 42% sponge and 58% bacterial or archaeal, the latter dominated by Poribacteria. It includes Nitrospira nitrite oxidoreductase detected in every run. The four phase-2 specimens had a similar composition (Bacteria 51-64% and Porifera 35-48% of peptides, Poribacteria alone 27-33%), whereas the two specimens stored long-term in ethanol at 4{degrees}C, which also differed in collection site and storage history, yielded four to five times less evidence than the frozen ones, even though reduction and alkylation had not been effective in the two frozen specimens. S-Trap combined with homology-driven search is a robust strategy for proteomics of non-model holobionts.

biochemistry↗