<p><strong>In closed communities such as the Amish in North America, rare genetic disorders occur more frequently. In children from this community, a condition has been described that affects the development of the nervous system and manifests, for example, as muscle weakness or epileptic seizures. The disorder is linked to a small change in a single protein, but for a long time it was unclear which cellular process this change disrupts. This question has now been answered by researchers from CEITEC Masaryk University, who show that the disease is caused by a disruption of a key mechanism required for the proper processing of genetic information in the cell.</strong></p><p>Every cell must first transcribe genetic information and then modify it before it can be used. From the original “working transcript,” unnecessary parts are removed and the remaining pieces are precisely joined together. This process, known as RNA splicing, consists of many consecutive steps and is tightly regulated. If the process does not proceed correctly or stops at any point, the cell cannot properly convert the copied genetic information into a usable form and therefore cannot function as it should.</p><p>Researchers from CEITEC Masaryk University have now described one of the key steps in this process – <strong>a specific signal inside the cell</strong>. This signal acts as a checkpoint: only once it is fulfilled, the entire mechanism is activated and the process can continue.</p><p><i>“We showed that during RNA splicing, a chemical modification of the protein SF3B1 is required at a precisely timed step. This modification allows another protein, SNIP1, to bind. If this signal is not transmitted correctly, the cell cannot proceed with the splicing process,”</i> explains first author<strong> </strong><a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/pavla-gajduskova-ph-d/u26136?page=publication"><strong>Pavla Gajdušková</strong></a>.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_4_79e003984a.jpeg" alt="CEITEC: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Pavla Gajdušková" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_4_79e003984a.jpeg 235w," sizes="100vw" width="1600" height="1067"></p><p>This is where the research connects to patients in the Amish community. In affected children, a <strong>small genetic change in the SNIP1 protein </strong>disrupts its ability to respond properly to the signal mediated by the modified SF3B1 protein, <strong>making RNA splicing less efficient than in healthy individuals</strong>. As a result, errors occur during RNA splicing that the cell cannot correct, impairing its function – especially in the nervous system.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_44a7e2ef17.jpg" alt="CEITEC/Blažek Lab: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Interaction between SF3B1 and SNIP1 proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_44a7e2ef17.jpg 156w," sizes="100vw" width="1600" height="1600"><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_2_85826d711e.jpg" alt="CEITEC/Blažek Lab: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: The effect of mutations in SNIP1 on cell proliferation." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_2_85826d711e.jpg 235w," sizes="100vw" width="1600" height="1067"></p><p>The researchers were thus able to clarify the cause of this rare neurodevelopmental disorder. <i>“Additionally, the cause of this disease also confirms the correctness of the checkpoint we described. It shows that even a small change in one of the proteins involved can disrupt the RNA splicing mechanism on which the cell depends,”</i> adds group leader <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/dalibor-blazek-ph-d/u25918"><strong>Dalibor Blažek</strong></a>.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_3_f95cfd68eb.jpeg" alt="CEITEC/Martin Indruch: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Dalibor Blažek." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_3_f95cfd68eb.jpeg 235w," sizes="100vw" width="1600" height="1067"></p><p>Although the study focuses on basic research, its implications are broader. It suggests that the same mechanism may also play a role in regulating cell division – a process that is often disrupted in cancer.</p><blockquote><p>The research was carried out by scientists from <strong>CEITEC Masaryk University </strong>in collaboration with researchers from Spain and Germany. The study was published in the journal <a target="_blank" rel="noopener noreferrer" href="https://www.nature.com/articles/s41467-026-71119-2">Nature Communications</a>.</p></blockquote>

A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism

<p><strong>This study investigates the pathogenesis of neurosyphilis through cerebrospinal fluid proteomics using LC–MS/MS and ELISA validation. Comparative analysis identified 234 differentially expressed proteins, with major alterations linked to lysosomal dysfunction, axon guidance, and neurodegeneration pathways.</strong></p><p>Key lysosomal proteins, including PSAP and DNASE2, together with the axonal protein EPHA4, were significantly downregulated in neurosyphilis patients. These proteins showed potential as biomarkers for neurodegeneration and may provide new insights into disease mechanisms, diagnostics, and therapeutic targets.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689"><strong>Cerebrospinal Fluid Proteome Reveals Dysregulation of Lysosomal and Axonal Proteins in Neurosyphilis</strong></a></h4><p>Huayang Tang*, Junjie Hu, Yifan Wu, Jinping Gao, Wenjun Wang, Xiaodong Zheng, Ran Zhang, Bo Liang, Fusheng Zhou, Ze Guo*</p><p>J. Proteome Res. 2026, 25, 2, 713–722</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.jproteome.5c00689">https://doi.org/10.1021/acs.jproteome.5c00689</a></p><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/"><strong>CC-BY 4.0</strong></a></h6></blockquote><p><strong>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.</strong></p><div><p>Neurosyphilis (NS) is a group of clinical syndromes characterized by neuroinflammation caused by <i>Treponema pallidum</i> (<i>T. pallidum</i>), which occurs in all stages of syphilis. <a href="javascript:void(0);">(1,2)</a> NS is classified based on clinical presentation as either asymptomatic (ANS) or symptomatic (SNS), and based on disease stage as either early (occurring 1–2 years after primary infection) or late. <a href="javascript:void(0);">(1)</a> <i>T. pallidum</i> can cause local nonspecific and central nervous system (CNS) inflammation, leading to possible degenerative changes. <a href="javascript:void(0);">(3)</a> The immune response of CNS in neurosyphilis is comparable to that observed in other neuroinflammatory diseases. Consequently, the presence of neurological symptoms may not reliably indicate active CNS inflammation in syphilis patients. <a href="javascript:void(0);">(3)</a> A cerebrospinal fluid (CSF) proteomic study identified three biomarkers (SEMA7A, SERPINA3, and ITIH4) that contribute to NS and have potential implications for diagnosis and therapeutic strategies. <a href="javascript:void(0);">(4)</a> Through integrated proteomics and single-cell transcriptomics analyses, Toll-like/NF-κB signaling was identified as the key pathway involved in CNS damage caused by <i>T. pallidum</i>. <a href="javascript:void(0);">(5)</a> Despite an increasing understanding of the biomarkers and possible neuroinflammatory damage mechanisms of neurosyphilis, the mechanisms of neurodegeneration caused by <i>T. pallidum</i> infection remain elusive. <a href="javascript:void(0);">(6)</a></p><p>Patients with neurosyphilis exhibit stage-specific profiles of soluble factors in their CSF, which are linked to both immune status and the extent of neuronal damage. <a href="javascript:void(0);">(7)</a> In this study, we analyzed differentially expressed proteins (DEPs) in the CSF proteomes from 28 individuals, including neurosyphilis (NS), suspected neurosyphilis (spNS) and non-neurosyphilis (nNS) individuals, by LC–MS/MS and analyzed a public data set of the neurosyphilis CSF proteome. Validation was then performed by ELISA in an independent group comprising 110 samples. The results revealed that neuroinflammation by <i>T. pallidum</i> infection results in dysregulation of the key proteins in lysosomal and axonal pathway, which suggesting a potential contribution to neurodegeneration in neurosyphilis.</p><h4><strong>Materials and Methods</strong></h4><h5><strong>LC–MS/MS</strong></h5><p>The tryptic peptides were dissolved in 0.1% formic acid (solvent A) and loaded onto a custom-made reversed-phase column (15 cm × 75 μm). Using an <strong>EASY-nLC 1000 UPLC system</strong>, a gradient was run at 400 nL/min as follows: 6% to 23% solvent B (0.1% formic acid in 98% acetonitrile) over 26 min, 23% to 35% in 8 min, up to 80% in 3 min, and held at 80% for 3 min. Peptides were ionized via an NSI source at 2.0 kV and analyzed online by a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/559"><strong>Q Exactive Plus mass spectrometer</strong></a><strong>.</strong> Full scans (<i>m</i>/<i>z</i> 350–1800) were acquired in the Orbitrap at 70,000 resolution. The top precursors were selected for MS/MS with an NCE of 28, and fragments were detected at 17,500 resolution. A data-dependent method cycled between one MS scan and 20 MS/MS scans with a 15.0 s dynamic exclusion. AGC was set at 5E4. MS/MS data were processed with MaxQuant (v.1.5.2.8) using Trypsin/P as the enzyme (up to 2 missed cleavages). Precursor mass tolerance was 20 ppm (first search) and 5 ppm (main search); fragment mass tolerance was 0.02 Da. Fixed modification: carbamidomethyl (C); variable modification: oxidation (M). The FDR threshold was &lt;1%, and the minimum peptide score was &gt;40.</p><h5><strong>ELISA</strong></h5><p>CSF levels of host proteins were quantified using commercial ELISA kits according to the manufacturers’ protocols. Proteins analyzed included PSAP (OKEH07124, Aviva, USA), CTSL (abx150963, Abbexa, UK), NPC2 (A-QEK07857, Biogradetech, USA), and DNASE2 (abx386953, Abbexa, UK). Briefly, 100 μL of CSF was added to precoated plates and incubated at 37 °C for 2 h. After washing, 100 μL of detection antibody was added to each well and incubated at 37 °C for another 2 h. Following a wash, 100 μL of streptavidin-HRP working solution was added and incubated at room temperature for 20 min in the dark. The reaction was stopped with 50 μL of stop solution, and the optical density was measured at 450 nm.</p><h4><strong>Results</strong></h4><h5><strong>Downregulation of Key Lysosomal Proteins in CSF from Patients With Neurosyphilis</strong></h5><p>By analyzing the DEPs in NS vs nNS, we observed a significant enrichment of downregulated proteins in the lysosome pathway (<i>P</i> = 0.007) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>A), with 9 lysosomal proteins showing significant downregulation (<i>P</i><sub>adj</sub> &lt; 0.05) in the NS group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S4</a>). To validate this finding, we examined the public CSF proteomics data set of neurosyphilis (PXD033034) and identified 18 proteins in the lysosomal pathway that were significantly downregulated in patients with NS (<i>P</i><sub>adj</sub> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S4</a>). PPI network analysis determined the top 10 hub genes within the lysosome pathway (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>B). A Venn diagram revealed 3 proteins (PSAP, CTSL, and NPC2) shared across our current data, the public data set (PXD033034) and the top 10 hub genes (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>C). The mass spectrometry results indicated that the levels of PSAP (<i>P</i><sub>adj</sub> = 0.043), CTSL (<i>P</i><sub>adj</sub> = 0.028) and NPC2 (<i>P</i><sub>adj</sub> = 0.013) were significantly lower in the NS group compared to the nNS group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D). The PXD033034 data set revealed consistent changes in the PSAP, CTSL, and NPC2 levels in the NS group (<i>P</i><sub>adj</sub> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S1 and Table S4</a>). In addition, associations between the lysosomal protein DNASE2 and NS were observed in both the present study (<i>P</i><sub>adj</sub> = 0.003) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D) and the PXD033034 data set (<i>P</i><sub>adj</sub> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S1 and Table S4</a>), with subgroup analysis revealing a significantly lower expression level of DNASE2 in the SNS group compared to the ANS group (<i>P</i> = 0.035) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D and <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S3</a>). Further validation by ELISA (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S5</a>) in an independent group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#tbl1">Table 1</a>) confirmed significantly downregulated CSF levels of PSAP (<i>P</i> &lt; 0.0001), CTSL (<i>P</i> &lt; 0.0001), NPC2 (<i>P</i> = 0.0024) and DNASE2 (<i>P</i> &lt; 0.0001) in patients with NS (n = 21) than in nNS individuals (n = 56) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>E) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S6</a>), as well as decreased in the SNS subgroup (<i>P</i> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S2 and Table S6</a>). Receiver operating characteristic (ROC) curve analysis supported PSAP (AUC = 0.91, 95% CI: 0.83–0.99) and DNASE2 (AUC = 0.95, 95% CI: 0.91–0.99) for distinguishing NS from nNS and as potential biomarkers for assessing neurodegeneration in NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>F). These results indicate that <i>T. pallidum</i> infection may lead to lysosomal dysfunction in CNS.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/J_Proteome_Res_2026_25_2_713_722_Figure_2_Downregulation_of_key_lysosomal_proteins_in_the_cerebrospinal_fluid_of_neurosyphilis_patients_bbccd95f44.jpg" alt="J. Proteome Res. 2026, 25, 2, 713–722: Figure 2. Downregulation of key lysosomal proteins in the cerebrospinal fluid of neurosyphilis patients. (a) KEGG pathway analysis demonstrated that downregulated proteins in patients with NS were significantly enriched in the lysosome pathway, as well as in axon guidance and neurodegeneration. (b) The top 10 hub genes involved in the lysosome pathway were identified using the STRING network data set and PPI analysis. (c) A Venn diagram revealed 3 proteins (PSAP, CTSL, and NPC2) shared across our current data, the public data set (PXD033034) and the top 10 hub genes. (d) The CSF levels of PSAP (Padj = 0.043), CTSL (Padj = 0.028), DNASE2 (Padj = 0.003) and NPC2 (Padj = 0.013) were significantly decreased in the NS group than in the nNS group. Subgroup analysis found a significantly lower expression level of DNASE2 in the SNS group than in the ANS group (P = 0.035). (e) PSAP, DNASE2, CTSL and NPC2 levels in CSF were tested by ELISA in the nNS (n = 56) and NS (n = 21) groups. Compared with those in the nNS group, significantly lower PSAP (P &lt; 0.0001), CTSL (P &lt; 0.0001), DNASE2 (P &lt; 0.0001) and NPC2 (P = 0.0024) levels were detected in the NS group. (f) ROC curve analysis for NS revealed that PSAP had an AUC = 0.91 (95% CI: 0.83–0.99), DNASE2 had an AUC = 0.95 (95% CI: 0.91–0.99), CTSL had an AUC = 0.85 (95% CI: 0.76–0.95), and NPC2 had an AUC = 0.72 (95% CI: 0.59–0.85). NS: neurosyphilis; nNS: non-neurosyphilis; ANS: asymptomatic neurosyphilis; SNS: symptomatic neurosyphilis. ROC: receiver operating characteristic; AUC: area under the curve. * P &lt; 0.05, ** P &lt; 0.01, ****P &lt; 0.0001." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_J_Proteome_Res_2026_25_2_713_722_Figure_2_Downregulation_of_key_lysosomal_proteins_in_the_cerebrospinal_fluid_of_neurosyphilis_patients_bbccd95f44.jpg 140w," sizes="100vw" width="2100" height="2339"></p><h5><strong>Downregulation of Key Axonal Proteins Correlated with Lysosomal Protein Reduction in Neurosyphilis CSF</strong></h5><p>Lysosomes play crucial roles in neuronal health by maintaining axonostasis. <a href="javascript:void(0);">(10)</a> The enrichment analysis indicated that the downregulated proteins in NS were implicated in the biological processes of axonostasis (such as axon development and axonogenesis) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig1">Figure 1</a>F) and the pathway of axon guidance (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>A). Our proteomic data revealed a total of 24 downregulated (<i>P</i><sub>adj</sub> &lt; 0.05) axonal proteins and 1 upregulated (<i>P</i><sub>adj</sub> &lt; 0.05) axonal protein in the CSF of patients with NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S9</a>). Furthermore, the PXD033034 data set revealed 55 downregulated (<i>P</i><sub>adj</sub> &lt; 0.05) and 4 upregulated (<i>P</i><sub>adj</sub> &lt; 0.05) axonal proteins in NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S9</a>). The top 10 hub genes involved in the biological processes of axon development and axonogenesis were identified by PPI network analysis (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>A). Considering the overlap of our current data, the PXD033034 data set and the top 10 hub genes (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>B), one key protein, EPHA4, was identified across 3 data sets, with significant downregulation in our current data (<i>P<sub>adj</sub></i> = 0.011) and in the PXD033034 data set (<i>P<sub>adj</sub></i> = 0.028) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>C). Correlation analysis further revealed a positive correlation between the levels of PSAP and EPHA4 (<i>r</i> = i 0.83, <i>P</i> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>D). Reduced levels of PSAP and EPHA4 in CSF have been implicated in neurodegenerative diseases, including Alzheimer’s disease (AD) and Parkinson’s disease (PD). <a href="javascript:void(0);">(11,12)</a> Our findings suggest that coordinated dysregulation of lysosomal and axonal proteins may contribute to neurodegeneration in NS.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/J_Proteome_Res_2026_25_2_713_722_Figure_4_Key_axonal_protein_downregulated_in_CSF_from_patients_with_neurosyphilis_66f5533e94.jpg" alt="J. Proteome Res. 2026, 25, 2, 713–722: Figure 4. Key axonal protein downregulated in CSF from patients with neurosyphilis. (a) The top 10 hub genes involved in axonostasis were identified by the STRING network data set and PPI analysis. (b) A Venn diagram revealed 1 protein (EPHA4) shared across DEPs related to axonostasis in our current data and in the public data set (PXD033034) and the top 10 hub genes. (c) EPHA4 was significantly downregulated both in our present study (Padj = 0.011) and in the PXD033034 data set (Padj = 0.028). (d) Correlation analysis demonstrated that the EPHA4 level was significantly positively correlated (P &lt; 0.05) with the levels of PSAP (r = 0.83), CTSL (r = 0.6), NPC2 (r = 0.69), DNASE2 (r = 0.61) and SEMA7A (r = 0.83). NS: neurosyphilis; nNS: non-neurosyphilis. * P &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_J_Proteome_Res_2026_25_2_713_722_Figure_4_Key_axonal_protein_downregulated_in_CSF_from_patients_with_neurosyphilis_66f5533e94.jpg 178w," sizes="100vw" width="1250" height="1096"></p><h4><strong>Conclusions</strong></h4><p>The present study reveals the associations of dysregulated proteins in lysosomal and axonal pathways with neurosyphilis, and potential evidence of shared pathophysiological mechanisms between neuroinflammation caused by <i>T. pallidum</i> infection and neurodegenerative diseases.</p><p>However, this study has certain limitations. First, the use of ELISA to validate a limited number of proteins has certain limitations, such as the inherent cross-reactivity of ELISA. In the future, we can optimize the validation experiments by adding techniques such as Western blotting for verification. Second, this study uses a cross-sectional sampling method for research, which limits our ability to infer disease progression and treatment responses. In the future, we will conduct follow-up on the subjects, continue collecting cerebrospinal fluid samples after treatment, and observe whether the protein dysregulation is reversible after treatment. For spNS patients, follow-up should also be conducted to determine if they have transformed into NS, which will be very valuable for validating the predictive utility of our biomarkers. Finally, although multiple discovery and validation cohort studies have been conducted, we currently lack direct mechanistic evidence. Future work will investigate whether exposing neural cell coculture models to outer-membrane antigens of <i>T. pallidum</i> reproduces the lysosome and axon alterations observed in CSF, clarifying their role in neural damage of neurosyphilis and potential biomarkers for diagnosis and treatment of neurodegeneration in neurosyphilis.</p></div>

Cerebrospinal Fluid Proteome Reveals Dysregulation of Lysosomal and Axonal Proteins in Neurosyphilis

<p><strong>In the week of May 11, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.</strong></p><blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars"><strong>👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</strong></a></h4><p><strong>👉 Search and filter in the largest global database</strong> with over <strong>5 500 GC, LC, MS and spectroscopy webinars</strong>.</p></blockquote><h5><strong>1. Thermo Fisher Scientific: Uncovering Microplastics: Identification, Quantification, and Exposure Assessment</strong></h5><ul><li>Tu, 12.5.2026 08:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6136">Registration</a></li></ul><p>In this webinar, we will explore complementary analytical solutions for comprehensive microplastics characterization.</p><h5><strong>2. Waters Corporation: Size variant analysis of antibodies and ADCs using SEC, SEC-MALS, SEC-MS, and 2D Protein A-SEC Methods</strong></h5><ul><li>Tu, 12.5.2026 17:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6169">Registration</a></li></ul><p>Size-exclusion chromatography (SEC) is essential for analyzing aggregates, monomers, and fragments in biotherapeutic proteins.</p><h5><strong>3. Waters Corporation: Beyond C18 and Phenyl: Expanding Selectivity with Biphenyl Columns Built for UV and pH Robustness</strong></h5><ul><li>We, 13.5.2026 16:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6183">Registration</a></li></ul><p>Discover how modern biphenyl stationary phases improve challenging LC separations with lower UV bleed, broad pH stability, and enhanced recovery of metal-sensitive analytes.</p><h5><strong>4. Milestone: Modern Sample Prep for Organic Contaminants: PAHs, PFAS, MOSH/MOAH in Food</strong></h5><ul><li>We, 13.5.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5822">Registration</a></li></ul><p>Learn how microwave-assisted extraction streamlines food analysis of PAHs, PFAS, and MOSH/MOAH, improving recoveries, reducing solvents, and meeting regulatory demands.</p><h5><strong>5. SelectScience: Achieve faster GLP-1 amino acid analysis with rapid UPLC technology</strong></h5><ul><li>We, 13.5.2026 17:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6173">Registration</a></li></ul><p>Accelerate GLP-1 amino acid analysis. Learn how UPLC, microwave hydrolysis and Waters AccQ-Tag solutions speed up drug development and ensure compliance.</p><h5><strong>6. Waters Corporation: Transform Your Daily Lab Operations with Automation - Biomolecules Workflows</strong></h5><ul><li>Th, 14.5.2026 11:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6174">Registration</a></li></ul><p>Discover how Andrew+ and OneLab automate complex biomolecule workflows. Learn how labs improve consistency, traceability, and efficiency in oligonucleotide and peptide analysis.</p>

Webinars LabRulezLCMS Week 20/2026

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Since its establishment in 2011, CEITEC has quickly developed into a cutting-edge infrastructure for research which performs highly alongside the best institutes in Europe. Among the main priorities of CEITEC are the promotion of a motivating and dynamic international scientific environment, the provision of state-of-the-art research infrastructure, and the policy of open communication and equal opportunities.

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KNAUER LH 8.1 - Modular analytical XYZ Autosampler

KNAUER Liquid Handler offers finally an alternative in the world of robotic autosamplers. In-house design and development for a new level of simplicity and speed.

<p><strong>KNAUER Liquid Handler offers finally an alternative in the world of robotic autosamplers. In-house design and development for a new level of simplicity and speed, namely by:</strong></p><h4><strong>Performance</strong></h4><ul><li>Highest repeatability of peak area in full loop or sandwich injection mode</li><li>Zero sample loss and high precision via Sandwich injection mode&nbsp;</li><li>Lowest carry over with active Fast wash station that cleans the injection syringe and needle on the in- and outside by delivering an adjustable cleaning solvent flow</li><li>User-friendly control via pre programmed injection parameters in Chromatography Software packages</li></ul><h4><strong>Versatility</strong></h4><ul><li>Modular design and wide selection of accessories</li><li>Flexible injection volumes by a variety of exchangeable injection syringes&nbsp;</li><li>Customizable lengths of the rail from standard &nbsp;557 or 887 mm up to 1200mm to increase the amount of modules</li></ul><h4><strong>High throughput</strong></h4><ul><li>Up to 390 x 1.5 mL vials or 6 well plates per Robotic Cooler</li><li>Maximum 1560 x 1.5 ml vials or 24 well plates per Liquid Handler</li><li>Short cycle times via fast and precise movements and the software option "overlapped injections" that allows for preparing the next injection while the previous is still running</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_Liquid_Handler_LH_8_1_AZURA_system1_7ad2b43571.jpg" alt="Knauer: Liquid Handler LH 8.1 with AZURA system" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_Liquid_Handler_LH_8_1_AZURA_system1_7ad2b43571.jpg 244w," sizes="100vw" width="1390" height="889"></p><h3><strong>Great variety of modules available</strong></h3><p><strong>KNAUER offers a range of active and passive modules for easy customisation of your LH 8.1.</strong></p><ul><li>Want to have more samples and need a cooling option? Use the Robotic Cooler!</li><li>Want a lower carry over? Install the Fast Wash Station with two different solvents for in- and outside syringe and needle cleaning!</li><li>Want to change the solvent in your syringe? Use a passive solvent option to draw liquid during the injection process!</li></ul><p>There are a variety of active and passive options available. Just mount the module on the sampler, configure it in your software and you are ready to go.</p><h4><strong>Injection Valve</strong></h4><p>The injection valve consists of a valve drive and a 6 Port 2-Position valve with a special injection port.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_Liquid_Handler_LH_8_1_standalone1_5f21514cca.jpg" alt="Knauer: Liquid Handler LH 8.1 - standalone" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_Liquid_Handler_LH_8_1_standalone1_5f21514cca.jpg 179w," sizes="100vw" width="1293" height="1127"></p><h4><strong>Tray Holder</strong></h4><p>The manual tray holder can store up to 130 standard HPLC vials and is recommended whenever no sample cooling is needed.</p><h4><strong>Robotic Cooler</strong></h4><p>The Robotic Cooler can store your samples at 4 - 40°C. You can insert up to 3 Sample Racks for 130 vials each, what means you can store up to 390 sample vials per Robotic Cooler.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_Liquid_Handler_LH_8_1_cooled_tray_2_c6fd0672e9.jpg" alt="Knauer: Liquid Handler LH 8.1 - cooled tray" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_Liquid_Handler_LH_8_1_cooled_tray_2_c6fd0672e9.jpg 239w," sizes="100vw" width="1595" height="1043"></p><h4><strong>Fast Wash Station</strong></h4><p>With the fast wash station, the injection syringe is cleaned on the in- and outside. It is always recommended, because it significantly reduces carry-over and offers a very user-friendly handling.&nbsp;</p><h4><strong>Manual Wash Station</strong></h4><p>Manual wash stations are an alternative to the fast wash station when carry-over is not the major concern. A manual wash station can be integrated in the manual tray holder with 5 x 10 ml vials or used as an additional module with 6 x 10 ml vials or 2 x 60 ml vials.</p><h4><strong>Sample Trays</strong></h4><p>Different sample trays can be used either in the manual rack holder or in the Robotic Cooler. Depending on your needs, they are made for analytical standard 1.5 ml vials or well plates.</p><h4><strong>Syringes</strong></h4><p>The most common syringes are implemented in the chromatography software packages. All optimized parameters are preconfigured to get quickly started.</p><h3><strong>Special features</strong></h3><h4><strong>Injection modes</strong></h4><h5><strong>Sandwich loop: Zero sample loss with excellent reproducibility</strong></h5><p><strong>Tired of choosing between sample loss and high performance? The new injection mode offers both.</strong></p><ul><li>KNAUER Liquid Handler LH 8.1 has a special injection mode. Next to standard injections like full loop and partial loop it has the opportunity to use the sandwich injection mode.</li><li>The sample is prepared inside a gastight syringe and then transferred into the HPLC System. In sandwich mode the sample is trapped between small gaps of air. This injection method only takes up the sample volume it needs and the air gaps prevent any peak broadening. Furthermore the pressure increase during the injection process will reduce the sample plug even more leading ot much narrower peak shapes and higher injection precision. &nbsp;</li><li>Ths injection method combines the zero sample loss of µl pickup and injection precision of partial loop injection.</li><li>Only the amount of sample that is injected is aspired by the syringe</li><li>Minimized sample widenening during injection process</li><li>Very high precision</li><li>No loss of sample</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_Liquid_Handler_LH_8_1_Sandwich_Injection_Mode_Big_fb713e65a0.jpg" alt="Knauer - Liquid Handler LH 8.1 - Sandwich Injection Mode" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_Liquid_Handler_LH_8_1_Sandwich_Injection_Mode_Big_fb713e65a0.jpg 179w," sizes="100vw" width="2832" height="2475"></p><h5><strong>Full loop</strong></h5><ul><li>Sample loop is completely filled with the sample</li><li>Maximum reproducibility is achieved</li><li>Injection volume equals the loop volume</li><li>The sample loop will be overfilled to ensure a complete and reproducible filling</li></ul><h5><strong>Partial loop</strong></h5><ul><li>Sample loop is partially filled with programmed amount of sample&nbsp;</li><li>Injection mode is recommended for preparative tasks</li><li>Maximum injection volume equals 50 % of the loop volume</li><li>No sample loss</li></ul><h3><strong>Large number of samples for high-throughput applications</strong></h3><p><strong>The Robotic Cooler offers space for up to 390 x 1.5 ml standard sample vials while maintaining a stable temperature.&nbsp;</strong></p><ul><li>The Robotic Cooler compartment offers 6 places for sample racks. Two per drawer with a variety of options. One place can be used by a 60 x 1.5 ml vial rack, or 384 well plates or 96 well plates. Furthermore a double rack can be used to offer 130 x 1.5 mL vial positions, taking the total sample capacity to 390 x 1.5 ml vials.</li><li>Depending on the rail length a multitude of Robotic Coolers can be installed and used seperatly. Up to 4 Robotic Coolers on the longest rail.</li><li>The Robotic Cooler is software controlled, which enables a higher response speed and only open the doors so the injection syringe can reach the sample, to protect other samples from temperature fluctuations.&nbsp;</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_Liquid_Handler_LH_8_1_cooled_tray_1_d2a6edf265.jpg" alt="Knauer: Liquid Handler LH 8.1 - high throughtput" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_Liquid_Handler_LH_8_1_cooled_tray_1_d2a6edf265.jpg 245w," sizes="100vw" width="1722" height="1040"></p><h3><strong>Speed up your injection</strong></h3><p><strong>The LH 8.1 is optimized to save time during injection and movement.</strong></p><ul><li>To safe time during the movement, the opening of the Robotic Cooler is software controlled and happens automatically.</li><li>To further speed up the injection, the sampler can apply the "overlapped injections" function, where the sample is already prepared inside the syringe.</li><li>Then the sample can be injected directly after the end of the previous run.&nbsp;</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_Liquid_Handler_LH_8_1_Method_overlapped_2_e94a888086.jpg" alt="Knauer: Liquid Handler LH 8.1 - Method_overlapped" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_Liquid_Handler_LH_8_1_Method_overlapped_2_e94a888086.jpg 245w," sizes="100vw" width="1121" height="310"></p><h3><strong>Easy control via HPLC software&nbsp;</strong></h3><ul><li><strong>The LH 8.1 </strong>can be used just as comfortable as any HPLC Autosampler.</li><li>All parameters for recommended syringes, like injection speed, delay and sandwich build-up are already implemented and extensively tested in our Chromatography Software packages, so that you are ready to go!</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Knauer_Liquid_Handler_LH_8_1_Method_overlapped_af91cd2ba5.jpg" alt="Knauer: Liquid Handler LH 8.1 - SW control" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Knauer_Liquid_Handler_LH_8_1_Method_overlapped_af91cd2ba5.jpg 188w," sizes="100vw" width="928" height="771"></p>

KNAUER AZURA Autosampler AS 6.1L

KNAUER AZURA AS 6.1L autosampler with up to 768 samples, ultra-low carryover, and fast injection cycles for HPLC/UHPLC workflows.

<p><strong>The KNAUER AZURA® AS 6.1L is a high-performance autosampler designed for automated sample injection in HPLC/UHPLC systems, offering high capacity, precision, and flexibility for both routine and high-throughput applications.</strong></p><p>The <strong>autosampler supports:</strong></p><ul><li>up to <strong>768 sample positions (microtiter plates)</strong></li><li>up to <strong>108 standard 1.5 mL vials</strong></li></ul><p>A highly effective <strong>internal and external needle wash system</strong> minimizes carryover to extremely low levels. The system is also fast, with a <strong>complete injection cycle taking less than one minute</strong>, including needle washing.</p><p>Three <strong>injection modes</strong> are supported:</p><ul><li><strong>full loop filling</strong> (highest precision)</li><li><strong>partial loop filling</strong> (variable volumes)</li><li><strong>µl pickup</strong> (loss-free injection of small volumes)</li></ul><p>The integrated <strong>ILD™ (Intermediate Loop Decompression) valve</strong> ensures accurate high-pressure injections without sample dilution and reduces pressure spikes, protecting the column.</p><h4><span><strong>Key Features</strong></span></h4><ul><li><strong>Autosampler for HPLC/UHPLC</strong> systems</li><li><strong>Up to 768 sample positions</strong></li><li><strong>Up to 108 vials </strong>(1.5 mL)</li><li>Ultra-low <strong>carryover (&lt; 0.0003%)</strong></li><li><strong>Fast injection</strong> cycle (<strong>&lt; 1 min</strong>)</li><li><strong>3 injection modes</strong> (full loop, partial loop, µl pickup)</li><li>ILD™ technology for high-pressure injection</li><li>PASA™ (pressure-assisted sample aspiration)</li><li>Optional <strong>sample cooling (4–40 °C)</strong></li><li>Missing vial/plate detection</li><li>Supports precolumn derivatization</li></ul><h3><span><strong>Technical Specifications</strong></span></h3><h4><span><strong>Sample Injection</strong></span></h4><ul><li><strong>Injection volume range:</strong> 0.1 µl – 10 mL</li><li><strong>Precision:</strong><ul><li><strong>Full loop:</strong> &lt; 0.3% RSD</li><li><strong>Partial loop:</strong> &lt; 0.5% RSD</li><li><strong>µl pickup:</strong> &lt; 1.0% RSD</li></ul></li><li><strong>Accuracy:</strong> 0.2 µl (250 µl syringe)</li></ul><h4><span><strong>Performance</strong></span></h4><ul><li><strong>Carryover:</strong><ul><li>&lt; 0.0015% (standard)</li><li>&lt; 0.0003% (extended wash)</li></ul></li><li><strong>Injections per vial:</strong> <strong>max. 9</strong></li><li><strong>Cycle time:</strong><ul><li>7 s (same vial)</li><li>14 s (different vials)</li><li>&lt; 60 s total</li></ul></li></ul><h4><span><strong>Capacity &amp; Compatibility</strong></span></h4><ul><li><strong>Microtiter plates:</strong> ANSI SLAS standard</li><li><strong>Max vial/plate height:</strong> <strong>47 mm</strong></li></ul><h4><span><strong>Additional Features</strong></span></h4><ul><li>Headspace pressure (bubble prevention)</li><li>Precolumn derivatization</li><li>Sample tray cooling (optional, 4–40 °C)</li><li>Vial detection sensor</li></ul><h4><span><strong>Materials</strong></span></h4><ul><li>ETFE, PTFE, stainless steel, glass, Vespel</li><li>Wide chemical compatibility</li></ul><h4><span><strong>Control &amp; Communication</strong></span></h4><ul><li>LAN / Ethernet</li><li>Analog inputs</li><li>TTL inputs (start, stop, freeze)</li><li>Relay output (alarm, marker)</li></ul><h4><span><strong>Operating Conditions</strong></span></h4><ul><li><strong>Temperature:</strong> 10–40 °C</li><li><strong>Humidity:</strong> 20–80%</li></ul>

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