Search bioRxiv⌕ Search

bioRxiv · 10.64898/2026.10.20.760564

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

Abstract

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.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

da Silva de Araujo, C., Rodrigues, A. C. S., Rodrigues de Souza, G., Nogueira, F. C. S., Leda Valverde, A., JUNQUEIRA, M.. 2026-10-21. Sample Preparation and Homology-Driven Search Shape the First Holobiont Proteome of the Marine Sponge Viles ophiraphidites (formerly Topsentia ophiraphidites). https://doi.org/10.64898/2026.10.20.760564

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Standardisation Challenges in ELISA-Based Quantification of Equine Chorionic Gonadotropin (eCG/PMSG)

Equine chorionic gonadotropin (eCG/PMSG) is widely used for female-cycle synchronization and estrus induction in livestock and in biomedical research, where reliable quantitative assessment is increasingly important. However, its structural and glycosylation heterogeneity complicates antibody-based measurement and assay standardization. This Technical Note evaluated six commercially available quantitative PMSG ELISA kits representing three distinct analytical profile groups. Kit-provided calibration standards were characterized by Western blotting, Coomassie staining, and LC-MS/MS, while quantitative performance was assessed using serial dilutions of two commercial PMSG preparations. DRG, Creative Diagnostics, and Demeditec showed similar calibration-standard profiles and concentration-dependent responses, although measured concentrations were consistently below nominal values. Biomatik and MyBiosource displayed closely related analytical profiles but little meaningful concentration-dependent response, whereas Krishgen measurements remained within a narrow range despite changes in nominal PMSG input. The calibration standards differed substantially in protein composition, and no eCG-derived peptides were identified by LC-MS/MS under the conditions used. These findings demonstrate that quantitative results obtained with commercially available PMSG ELISAs are not necessarily comparable and may be strongly influenced by calibration-material composition, assay format, and matrix effects. The findings highlight the limitations of current quantitative PMSG assays and the need for a well-characterized, commutable reference material, together with assay-specific validation of dilution parallelism and analyte recovery, to improve the reliability and comparability of eCG/PMSG measurements.

biochemistry↗

Optimization of the NFκB-DNA ensemble leads to high affinity binding of partial consensus sites

Our ability to respond to a myriad of external stressors is dependent on the activity of specific transcription factors that precisely regulate gene expression. While some transcription factors have high specificity for their consensus DNA binding site, others such as NF{kappa}B (RelA/p50) readily bind to partial and nonconsensus sites. In fact, ChIP-Seq data shows that nearly half of the DNA-bound RelA occupies sequences that do not match the consensus. Here we explore how NF{kappa}B (RelA/p50) binds to alternative sequences that differ subtly from the consensus. The two subunits of the NF{kappa}B heterodimer, RelA and p50, form an extensive pocket where DNA binding is mediated by both base-specific contacts and nonspecific interactions with the DNA backbone. RelA and p50 each form sequence-specific contacts with DNA at different 4-nucleotide sequences separated by two nucleotides, together forming a 10-base pair consensus binding sequence. Partial consensus sequences, known as half-sites, match the consensus sequence at only one of these two 4-nucleotide interaction sites. Here, using hydrogen deuterium exchange mass spectrometry (HDX-MS) and molecular dynamics (MD) simulations to investigate protein structural dynamics, we observe that rearranging nucleotides at the RelA-interacting end of a consensus DNA sequence to form a half-site induces dynamic structural changes through both subunits of RelA/p50. MD simulations reveal a shift in the position of DNA within the RelA/p50 binding pocket that allows optimal interaction with the half-site sequence. Our results demonstrate how RelA/p50 fine-tunes its interactions to achieve high-affinity binding with multiple different target DNA sequences.

biochemistry↗

A High-Sensitivity and High-Throughput LC-MS Workflow for Low-Input and Single-Cell Proteomics

Single-cell proteomics (SCP) requires sample preparation that minimizes sample loss and highly sensitive LC-MS analysis because the amount of protein available from a single cell is extremely limited. Here, we developed an integrated workflow for low-input and single-cell proteomics based on single-cell proteomics by LMNG-assisted sample preparation (scpLASP), which enables microliter-scale sample preparation using standard laboratory consumables. Systematic optimization of peptide reconstitution conditions identified 0.01% n-dodecyl-{beta}-D-maltoside (DDM) combined with 0.01% lauryl maltose neopentyl glycol (LMNG) as the condition yielding the highest number of identified peptides among those tested for low-input samples. Optimization of the LC mobile-phase composition identified 0.5% acetic acid with 1% dimethyl sulfoxide (DMSO) as the optimal condition, increasing the mean number of identified protein groups from 6,767 with 0.1% formic acid to 7,409 for 250 pg HeLa digests analyzed using an Orbitrap Astral Zoom. Shortening the LC gradient from 11 to 5.5 min enabled higher analytical throughput while maintaining mean identification counts of 6,558 and 7,088 protein groups from 100 and 250 pg HeLa digests, respectively, with median protein-level coefficients of variation of 9.20% and 6.99%. When the optimized workflow was applied to HEK293-derived Expi293F single cells using the same 5.5-min LC gradient, an effective analytical throughput of 135 samples per day was achieved with an injection volume of 4.5 {micro}L, accounting for sample-loading time. This workflow identified a median of 5,655 protein groups per cell using an empirical spectral library generated from 20-cell samples. Overall, this study establishes a sensitive and high-throughput workflow for low-input and single-cell proteomics that combines low-loss microliter-scale sample preparation with optimized LC-MS analysis, achieving high proteome depth and analytical throughput without requiring specialized nanoliter-scale sample-preparation devices.

biochemistry↗