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Ducrey, I.

Publications and source records attributed to Ducrey, I..

2 recordsLinked to original sources

Huntingtin is a cell-autonomous regulator of neuropeptide trafficking and clock output

Huntingtons disease is a severe neurodegenerative condition arising from an abnormal CAG repeat expansion in the HTT gene, which leads to the production of a mutant Huntingtin protein carrying an extended polyglutamine stretch. Although the field has largely centred on the toxic effects gained by this mutant protein, growing evidence points to the loss of normal wild-type Huntingtin function as an additional contributor to disease progression. Despite this, the cell-intrinsic roles of wild-type Huntingtin in neuronal biology remain poorly defined, in part because disentangling its specific contributions from broader network-level effects has proven technically challenging. To address this knowledge gap, we took advantage of the Drosophila huntingtin homolog (htt) and selectively manipulated its expression in the small lateral ventral neurons (sLNvs), a discrete cluster of just eight circadian pacemaker neurons that govern behavioral rhythmicity and sleep. Through targeted genetic knock-down, we show that reducing htt levels in sLNvs weakens the robustness of free-running circadian rhythms and substantially increases sleep in female flies. These behavioral changes are not rooted in developmental abnormalities, as restricting htt knock-down to adult flies reproduces the sleep phenotype across both beam-crossing and video-based locomotion assays. At the cellular level, htt loss disrupts dense core vesicle trafficking along sLNv axons, altering the fraction of motile vesicles and their velocity, and abolishing the time-of-day-dependent fluctuations in vesicle dynamics observed in these neurons. Complementary electrophysiological recordings using whole-cell patch-clamp further reveal that htt knock-down lowers action potential firing rates without perturbing resting membrane potential. Together, these results identify huntingtin as a cell-autonomous regulator of neuropeptide trafficking, neuronal excitability and circadian output. Beyond advancing our understanding of wild-type huntingtin physiology, this work carries direct relevance for HD therapeutic strategies, particularly those involving huntingtin-lowering approaches, by highlighting functions that may be unintentionally compromised.

neuroscience↗

Conjugates of α-d-Galp-(1->3)-β-d-Galp for the serological diagnosis of Chagas disease.

BackgroundChagas disease (ChD), caused by the parasitic protozoan Trypanosoma cruzi, is a lifelong, neglected tropical disease with substantial medical and socioeconomic impact. Despite this situation, currently available diagnostic and therapeutic methods display serious limitations. A promising strategy to improve ChD serodiagnosis involves targeting parasite carbohydrate antigens, particularly the -galactosyl-rich mucins that coat the surface of bloodstream trypomastigotes (tGPI-mucins). Methods/Principle FindingsHere, we present a concise and efficient protocol for the chemical synthesis of a tGPI-mucin-derived glycotope, the disaccharide -O_SCPLOWDC_SCPLOW-Galp-(1[->]3)-{beta}-O_SCPLOWDC_SCPLOW-Galp, and its functional conjugation to different scaffolds using the squarate method. A neoglycoprotein made upon a bovine serum albumin (BSA) carrier decorated with [~]28 units of the disaccharide, termed BSA-Di, was interrogated with sera of chronic ChD patients and healthy individuals from Argentina using an in-house enzyme-linked immunosorbent assay (ELISA). BSA-Di exhibited excellent sensitivity and effectively discriminated between ChD-positive and negative sera with high accuracy (AUC = 0.905), though its specificity was partially affected by cross-reactivity of some non-ChD sera containing natural -Gal antibodies. Conjugation of -O_SCPLOWDC_SCPLOW-Galp-(1[->]3)-{beta}-O_SCPLOWDC_SCPLOW-Galp to T. cruzi antigenic peptides, instead of BSA, corroborated these findings and enabled the generation of bivalent ChD diagnostic reagents combining glycan- and peptide-based epitopes. Conclusions/SignificanceOverall, our results identify -O_SCPLOWDC_SCPLOW-Galp-(1[->]3)-{beta}-O_SCPLOWDC_SCPLOW-Galp as a robust and reliable biomarker of T. cruzi infection. The methodologies and tools described here, together with optimized derivatives, are expected to positively impact ChD serological applications. AUTHOR SUMMARYDespite the enormous burden imposed by Chagas disease, diagnostic and therapeutic methods still present serious deficiencies. Towards filling this gap, we herein developed a protocol for the chemical synthesis of -O_SCPLOWDC_SCPLOW-Galp-(1[->]3)-{beta}-O_SCPLOWDC_SCPLOW-Galp, a major glycotope present on the Trypanosoma cruzi surface coat. This disaccharide was conjugated with different molecular scaffolds and serologically evaluated using an in-house enzyme-linked immunosorbent assay (ELISA). Our results indicate that -O_SCPLOWDC_SCPLOW-Galp-(1[->]3)-{beta}-O_SCPLOWDC_SCPLOW-Galp provides an overall robust and reliable biomarker of T. cruzi infection, with excellent sensitivity and only minor concerns regarding its potential cross-reactivity with natural -Gal antibodies. These findings indicate that the tools developed here, as well as optimized versions derived from them, should have a positive impact on the diagnosis and clinical management of Chagas disease and on the identification and/or clinical validation of novel drug/vaccine candidates for the treatment of T. cruzi infections.

microbiology↗