Biology subjects

Drouin, N.

Publications and source records attributed to Drouin, N..

3 recordsLinked to original sources

bioRxiv2025

Immunoglobulin sub-class levels define inter-donor plasma variability: a longitudinal dual-lab study

Advancements in mass spectrometry have transformed plasma proteomics, allowing for high-throughput analysis of large cohorts. This study utilized the TIMES cohort, consisting of 51 healthy participants monitored monthly over 12 months, to evaluate intra- and inter-individual variability in the plasma proteome. Approximately 600 samples were analyzed in two independent laboratories, revealing strong correlations despite methodological differences. The study focused on the stability of the plasma proteome within donors over a year, with larger differences observed between donors. A support vector machine model achieved a 98% median classification accuracy, confirming stable, donor-specific proteomic profiles. Immunoglobulins, often overlooked in plasma proteomics, were found to contribute significantly to donor-specific signatures, showing pronounced inter-individual variability but remarkable intra-donor stability. In contrast, C-reactive protein and other inflammation markers exhibited significant temporal fluctuations and donor-specific baseline levels. This inter-laboratory study highlights the importance of longitudinal sampling for biomarker discovery, the robustness of MS-based proteomic workflows, and provides new insights into immunoglobulin dynamics and variability in human plasma. Synopsis O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=65 SRC="FIGDIR/small/686385v1_ufig1.gif" ALT="Figure 1"> View larger version (19K): org.highwire.dtl.DTLVardef@1e7b501org.highwire.dtl.DTLVardef@11c85d7org.highwire.dtl.DTLVardef@1971a1dorg.highwire.dtl.DTLVardef@1338061_HPS_FORMAT_FIGEXP M_FIG C_FIG O_LILongitudinal analysis of individual plasma proteomes over a one-year period revealed low intra-individual variability albeit high inter-individual differences. C_LIO_LICross-site laboratory comparisons confirmed strong concordance in analytical performance and measurement consistency. C_LIO_LIConversion of relative protein intensities to absolute concentrations revealed immunoglobulin levels on par with established clinical reference ranges. C_LIO_LIDonors were distinguishable based on their unique plasma proteome. C_LIO_LIThe immunoglobulin sub-classes are key discriminators defining inter- and intra-donor variability C_LI

molecular biology↗

bioRxiv2023

How to prevent chick culling in the poultry industry? Discovery of a new biomarker for in ovo gender screening

Chicken eggs are one of the most consumed foods worldwide. However, the practice of chicken culling in the poultry industry involves unnecessary animal suffering and finding a way to put an end to this has become a societal priority. One approach that has been propagated as acceptable is based on the selection of female eggs early in the incubation process and the devitalization of the male eggs. It is with this objective in mind that we searched for a biomarker for early gender screening in eggs. Applying an untargeted mass spectrometry approach, we profiled allantoic fluid of different day-old eggs and identified the feature 3-[(2-aminoethyl)sulfanyl]butanoic acid (ASBA) as a strong biomarker for in-ovo gender prediction for day-9 old embryos. After validation using LC-APCI-MRM with an internal standard, we found ASBA can predict the female gender with a sensitivity and specificity well above 95% in our experiments. HighlightsO_LIDiscovery of a biomarker of chicken embryo gender in allantoic fluid from eggs C_LIO_LIDay 9 after laying was determined as optimum for sex prediction and animal welfare C_LIO_LI3-[(2-aminoethyl)sulfanyl]butanoic acid was identified using mass spectrometry C_LIO_LIThe biomarker was validated on large cohorts of different chicken species C_LI Graphical abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=77 SRC="FIGDIR/small/551526v1_ufig1.gif" ALT="Figure 1"> View larger version (21K): org.highwire.dtl.DTLVardef@c1330borg.highwire.dtl.DTLVardef@1fe2f28org.highwire.dtl.DTLVardef@c9f245org.highwire.dtl.DTLVardef@40a5f5_HPS_FORMAT_FIGEXP M_FIG C_FIG

developmental biology↗

bioRxiv2023

Evaluation of Expanded 2-Aminobenzothiazole Library for Inhibition of Pseudomonas aeruginosa Virulence Phenotypes

Bacterial resistance to antibiotics is a rapidly increasing threat to human health. New strategies to combat resistant organisms are desperately needed. One potential avenue is targeting two-component systems, which are the main bacterial signal transduction pathways used to regulate development, metabolism, virulence, and antibiotic resistance. These systems consist of a homodimeric membrane-bound sensor histidine kinase, and a cognate effector, the response regulator. The high sequence conservation in the catalytic and adenosine triphosphate-binding (CA) domain of histidine kinases and their essential role in bacterial signal transduction could enable broad-spectrum antibacterial activity. Through this signal transduction, histidine kinases regulate multiple virulence mechanisms including toxin production, immune evasion, and antibiotic resistance. Targeting virulence, as opposed to development of bactericidal compounds, could reduce evolutionary pressure for acquired resistance. Additionally, compounds targeting the CA domain have the potential to impair multiple two-component systems that regulate virulence in one or more pathogens. We conducted structure-activity relationship studies of 2-aminobenzothiazole-based inhibitors designed to target the CA domain of histidine kinases. We found these compounds have anti-virulence activities in Pseudomonas aeruginosa, reducing motility phenotypes and toxin production associated with the pathogenic functions of this bacterium.

microbiology↗