Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-10-03DOI: 10.1016/j.jprot.2025.105543
Ana Escobar , Marcos H. Salazar , Magdalena Hernández-Ortiz , Herlinda Clement , Sergio Encarnación-Guevara , John Cleghorn , Hildaura Acosta , Gerardo Corzo
{"title":"Integration of proteomic and transcriptomic data of the venom and venom gland from Tityus jaimei","authors":"Ana Escobar , Marcos H. Salazar , Magdalena Hernández-Ortiz , Herlinda Clement , Sergio Encarnación-Guevara , John Cleghorn , Hildaura Acosta , Gerardo Corzo","doi":"10.1016/j.jprot.2025.105543","DOIUrl":"10.1016/j.jprot.2025.105543","url":null,"abstract":"<div><div>This work presents a comprehensive transcriptomic and proteomic analysis of the venom gland and venom of <em>Tityus jaimei</em>, a recently described scorpion species of medical relevance in Panama and Costa Rica. High-throughput RNA sequencing (RNA-seq) and tandem mass spectrometry (MS/MS) enabled the identification of a diverse repertoire of venom proteins. Notably, this is the first report of proteins belonging to the nucleotide pyrophosphatase/phosphodiesterase and knottins families in the venom proteome of a scorpion from the genus <em>Tityus</em>. In addition, several known venom protein families were identified, including hyaluronidases, voltage-gated sodium and potassium channel toxins, lipolysis-activating peptides (LVPs), cysteine-rich secretory proteins (CRISPs), metalloproteinases, peptidylglycine alpha-hydroxylating monooxygenases (PHMs), serine proteases, alpha-amylases, single insulin-like growth factor-binding domain proteins, non-disulfide-bridged peptides (NDBPs), chitinases, cyclotide trypsin inhibitors, and calcin-like peptides. The identification of 16 distinct families in the venom of <em>Tityus jaimei</em> offers novel insights into its composition and the diversity of Tityus venoms in Central America. Finally, the use of IA to protein domain search for protein annotation.</div></div><div><h3>Significance T jaimei</h3><div>Here a comprehensive transcriptomic and proteomic analysis of the venom gland and venom of <em>Tityus jaimei</em>, a recently described scorpion species of medical relevance in Panama and Costa Rica, is presented. Nucleotide pyrophosphatase/phosphodiesterase and knottins families in the venom proteome of a scorpion from the genus <em>Tityus</em> are for the first time reported. Sixteen distinct protein families in the venom of <em>Tityus jaimei</em> were found, and they offer novel insights into its composition and the diversity of Tityus venoms in Central America.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105543"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145232912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-09-22DOI: 10.1016/j.jprot.2025.105537
Lijie Tang , Hailiang Yang , Zhijiang Wu , Liping Bao , Yang Zhou , Huabing Wang
{"title":"Comparative proteomic analysis of residual proteins in waterlogged ancient leather","authors":"Lijie Tang , Hailiang Yang , Zhijiang Wu , Liping Bao , Yang Zhou , Huabing Wang","doi":"10.1016/j.jprot.2025.105537","DOIUrl":"10.1016/j.jprot.2025.105537","url":null,"abstract":"<div><div>Leather artifacts hold significant historical and cultural value in human civilization. During long-term preservation, ancient relics, especially waterlogged leather artifacts, are susceptible to protein degradation. Therefore, analyses of the structure and protein composition of these ancient relics are crucial for their effective conservation. However, comprehensive research in this field is scarce and urgently needed. In this study, systematic investigations of the structures of fresh vegetable-tanned leather, dried leather artifacts, and waterlogged leather artifacts were performed from multiple perspectives. Compared with fresh vegetable-tanned leather and dry leather artifacts, the deterioration of waterlogged leather artifacts resulted in a darkened color, increased brittleness, and reduced fiber structure. Infrared analyses revealed that the characteristic peaks of the amide II and III bands were nearly absent in waterlogged leather artifacts. The species of the leather artifacts were analyzed using enzyme-linked immunosorbent assay (ELISA). Furthermore, comparative proteomic analysis revealed a markedly reduced repertoire of protein species in waterlogged leather artifacts compared with fresh vegetable-tanned leather. In particular, the number of peptides derived from type I collagen and other structural proteins was substantially diminished. This loss of collagen- and structure-related peptides, together with extensive fiber disintegration, underlies the pronounced morphological deterioration observed in waterlogged leather. By integrating species identification through ELISA with proteomic profiling, we establish a strategy that enables rapid, sensitive, and specific characterization of leather proteins.</div></div><div><h3>Significance</h3><div>This study integrated stereomicroscopy, scanning electron microscopy (SEM), and fourier transform infrared spectroscopy (FTIR) to systematically characterize morphological and microstructural differences between fresh vegetable-tanned leather and archaeological waterlogged leather artifacts. To further unravel residual proteins, comparative proteomic profiling was implemented to identify compositional shifts in collagenous proteins resulting from prolonged waterlogged burial conditions. A multidisciplinary approach was used to assess the characteristics of waterlogged leather artifacts.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105537"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145137764","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-10-27DOI: 10.1016/j.jprot.2025.105547
Zhigang Xiong , Chaoxi Li , Qiangqiang Han , Yanting Su , Liming Cheng , Hao-Long Zeng
{"title":"Comparative quantitative proteomics of tumoral and peritumoral tissues for distinguishing human glioblastoma from low-grade astrocytoma","authors":"Zhigang Xiong , Chaoxi Li , Qiangqiang Han , Yanting Su , Liming Cheng , Hao-Long Zeng","doi":"10.1016/j.jprot.2025.105547","DOIUrl":"10.1016/j.jprot.2025.105547","url":null,"abstract":"<div><div>Glioblastoma multiforme (GBM) and low-grade astrocytoma (LGA) are diffuse gliomas with distinct biological features and prognoses. However, the molecular mechanisms driving their differences are not fully understood. In this study, we performed a multi-dataset analysis integrating in-house quantitative proteomics data with high-quality external datasets to identify GBM-specific proteomic alterations between tumoral and peritumoral tissues relative to LGA. Our analysis revealed more pronounced proteomic differences between intra- and peritumoral tissues in GBM than in LGA. Proteins specifically dysregulated in GBM were predominantly linked to upregulated RNA splicing and spliceosome signaling. Through multi-dataset integration, we identified 73 GBM-specific upregulated proteins enriched in processes such as transcriptional regulation, hypoxia and necrosis, cytoskeleton organization, extracellular matrix remodeling, and immune response. Conversely, the 129 GBM-specific downregulated proteins were mainly involved in tumor suppression, G-protein signaling, calcium signaling, and neuronal gap junctions. Using these signature proteins, we developed a risk model based on CDK2, HDAC1, IGFBP2, SLC6A1, and TNR, which significantly predicted overall survival in glioma patients. This study delineates the proteomic landscape of GBM in comparison to LGA and offers a valuable resource for future mechanistic and clinical investigations.</div></div><div><h3>Significance</h3><div>Diffuse gliomas are a heterogeneous brain tumor that include both low-grade and high-grade variants, each characterized by distinct morphological and biological features. Glioblastoma multiforme (GBM) is the most common primary high-grade and malignant brain tumor, with a median survival of less than 15 months despite aggressive treatment, including surgery, radiotherapy, and chemotherapy. In contrast, low-grade astrocytoma (LGA) exhibits indolent growth and a less aggressive clinical course, resulting in significantly longer patient survival compared to GBM. The molecular mechanisms underlying the biological differences between LGA and GBM are incompletely understood, and there is an urgent need for new molecular biomarkers to enhance diagnosis and therapeutic options. In this study, we conducted a comprehensive multi-dataset analysis by integrating our in-house quantitative proteomics data with several high-quality external datasets. We analyzed tumor and peritumoral tissue samples from human GBM and LGA, and further identified the GBM-specifically regulated proteomic signatures and signaling pathways, which is crucial for understanding the molecular mechanisms driving the aggressive behavior of GBM and could serve as a foundation for developing novel diagnostic biomarkers and therapeutic targets. Future research should focus on validating these GBM-specific proteins in larger cohorts and exploring their functional roles in GBM progression. Additionally, integrating multi-omic","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105547"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145401380","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-09-29DOI: 10.1016/j.jprot.2025.105541
Maria Pinheiro Spínola , Dina Rešetar Maslov , Ivana Rubić , Mónica Mendes da Costa , Vladimir Mrljak , Madalena Lordelo , André Martinho de Almeida , José António Mestre Prates
{"title":"Extruded Limnospira platensis with enzyme supplementation shifts the broiler muscle proteome toward enhanced energy metabolism pathways","authors":"Maria Pinheiro Spínola , Dina Rešetar Maslov , Ivana Rubić , Mónica Mendes da Costa , Vladimir Mrljak , Madalena Lordelo , André Martinho de Almeida , José António Mestre Prates","doi":"10.1016/j.jprot.2025.105541","DOIUrl":"10.1016/j.jprot.2025.105541","url":null,"abstract":"<div><div><em>Limnospira platensis</em> (Spirulina) is known for its nutritional and bioactive profile, but its high-level dietary inclusion effects in broilers, particularly post-extrusion and enzyme pre-treatment, remain underexplored. We investigated how 15 % <em>L. platensis</em> raw (MA), extruded (MAE) or extruded with pancreatin (0.20 %) and lysozyme (0.01 %) (MAEM) affects the <em>pectoralis major</em> proteome of Ross 308 broilers. Birds were fed until day 35, then muscle proteins were prepared by filter-aided sample preparation, TMT 6-plex labelling and analysed by LC-MS/MS. Statistical analysis identified 26 differentially abundant proteins (<em>p</em> < 0.05, ≥ 2 peptides). MAEM samples clustered separately, showing increased abundance of NDUFA10 (Complex I; + 1.30-fold), COX5B (Complex IV; + 1.25-fold) and glycogen phosphorylase (+ 1.40-fold). Enrichment analysis revealed up-regulation of ATP synthesis, oxidative phosphorylation and glycogen catabolism in L. <em>platensis</em> groups, whereas control diets featured proteins linked to fatty-acid β-oxidation and myofibrillar assembly. These results indicate that extrusion combined with enzyme treatment enhances nutrient bioavailability and shifts the broiler muscle proteome toward energy-metabolism pathways without compromising performance. Data are available via ProteomeXchange (<span><span>PXD064230</span><svg><path></path></svg></span>).</div></div><div><h3>Significance</h3><div>The incorporation of Spirulina (<em>Limnospira platensis</em>) as a sustainable alternative to conventional feed ingredients is gaining attention in poultry nutrition. However, its specific effects on broiler's muscle proteome, as well as the impact of higher Spirulina inclusion levels on animal performance, remain largely unexplored. Herein, we investigated how extruded L. <em>platensis</em>, with and without enzyme supplementation, influences muscle protein expression. Results revealed a metabolic shift toward enhanced mitochondrial ATP production and glycogen metabolism when L. <em>platensis</em> was incorporated into the diets, suggesting improved energy efficiency and nutrient utilisation. These findings provide valuable insight into the biological mechanisms underlying muscle development in broilers fed microalgae-based diets. More broadly, they highlight the potential of combining pre-treated microalga ingredients as a strategy to optimise animal performance and health in the framework of poultry production.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105541"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145206672","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-09-16DOI: 10.1016/j.jprot.2025.105536
Michael Santos Silva , Leila S. Coelho-Rato , Navid Delshad , Tatiana Tarkhova , Joakim Edman , Preethy Paul , Annika Meinander , John E. Eriksson
{"title":"Anisomelic acid promotes proteasomal degradation of HPV16 E6 via E3 ligase recruitment: A mass spectrometry-based interactome study","authors":"Michael Santos Silva , Leila S. Coelho-Rato , Navid Delshad , Tatiana Tarkhova , Joakim Edman , Preethy Paul , Annika Meinander , John E. Eriksson","doi":"10.1016/j.jprot.2025.105536","DOIUrl":"10.1016/j.jprot.2025.105536","url":null,"abstract":"<div><div>Human papillomavirus (HPV) is a major driver of cervical and other epithelial cancers, with the viral oncoprotein E6 playing a central role in tumorigenesis by promoting degradation of the tumor suppressor p53. While prophylactic vaccines prevent infection, there remains a critical need for therapeutic strategies that eliminate established HPV-positive cells. Here, we identify anisomelic acid (AA), a natural diterpenoid, as a novel pharmacological principle that selectively induces the degradation of HPV16 E6. Using cellular thermal shift assay, we demonstrate that AA directly interacts with E6, likely triggering a conformational change that promotes its ubiquitination. Proteomic analysis of the E6 interactome in AA-treated cells revealed consistent enrichment of E3 ubiquitin ligases, including E6AP, UBR4, CDC20, and TRIP12, as well as proteasomal subunits. To our knowledge, this represents the first comprehensive proteomics framework of the HPV16 E6 interactome under small-molecule treatment conditions. These findings support a model in which AA facilitates proteasome-mediated elimination of E6, and the dataset itself provides a timely and valuable resource for HPV biology and therapeutic development.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105536"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145086449","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-10-08DOI: 10.1016/j.jprot.2025.105539
Julio A. González-Noriega , Martín Valenzuela-Melendres , Adrián Hernández-Mendoza , Humberto Astiazarán-García , Thalia Islava-Lagarda , Orlando Tortoledo-Ortiz , Ana L. De La Garza-Hernández , Samaria L. Gutierrez-Pacheco , Andrés Alvarez-Armenta , Emmanuel Ríos-Castro , José A. Huerta-Ocampo , E. Aída Peña-Ramos
{"title":"Antiobesogenic effect of hydrolysates and peptide fractions of porcine collagen after in vitro gastrointestinal digestion","authors":"Julio A. González-Noriega , Martín Valenzuela-Melendres , Adrián Hernández-Mendoza , Humberto Astiazarán-García , Thalia Islava-Lagarda , Orlando Tortoledo-Ortiz , Ana L. De La Garza-Hernández , Samaria L. Gutierrez-Pacheco , Andrés Alvarez-Armenta , Emmanuel Ríos-Castro , José A. Huerta-Ocampo , E. Aída Peña-Ramos","doi":"10.1016/j.jprot.2025.105539","DOIUrl":"10.1016/j.jprot.2025.105539","url":null,"abstract":"<div><div>The present study evaluated the angiotensin-converting enzyme inhibitory activity (ACEi) of a porcine skin collagen hydrolysate (PSCH) and its peptide fractions before and after a simulation of gastrointestinal digestion and their ability to reduce lipid accumulation in adipocytes (LAA). Before digestion, peptide fractions <1 kDa (PF4) had the highest (<em>p</em> < 0.05) ACEia (85.45 %), followed by PSCH (53.54 %). Post-digestion, PF4 (IC<sub>50</sub>: 124.49 μg/mL) decreased its activity; thus, DPF4 (digested PF4) had an ACE IC<sub>50</sub> of 204.56 μg/mL, while fraction <1 kDa from digested hydrolysate (FDH) showed the lowest activity (IC<sub>50</sub>: 313.81 μg/mL). Peptides were identified by LC-MS/MS and homology database search and aligned to peptides widely recognized as ACE inhibitors. Nine peptides were identified as potential ACE inhibitors through docking with the active site cavity of this enzyme (mainly GAXGPXGPQ and GPPGPA), and interaction with Zn (II). Subsequently, adding 600 μg/mL of FDH in preadipocytes reduced 71 % LAA, while DPF4 was less effective (45.5 % reduction). The addition of digested peptide fractions into differentiated adipocytes had a similar (<em>p</em> > 0.05) reduction of LAA of 22–39 %. Therefore, regardless of their differences as ACE inhibitors, digested FDH and DPF4 have a similar potential as anti-obesogenic adjuvants.</div></div><div><h3>Significance</h3><div>In this study, we evaluated the angiotensin-converting enzyme inhibitory activity of a porcine skin collagen hydrolysate and its peptide fractions before and after a simulation of gastrointestinal digestion and their ability to reduce lipid accumulation in adipocytes. Peptides were identified by LC-MS/MS and homology database search and aligned to peptides widely recognized as ACE inhibitors. Nine peptides were identified as potential ACE inhibitors through docking with the active site cavity of this enzyme (mainly GAXGPXGPQ and GPPGPA), and interaction with Zn (II). Subsequently, adding digested peptide fractions into differentiated adipocytes resulted in a reduction of lipid accumulation in adipocytes.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105539"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145258205","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Molecular signature of early obesity-associated insulin resistance: Adipocyte-derived extracellular vesicle proteins reveal stage-specific candidates for metabolic dysfunction","authors":"Jaime Delgadillo-Velázquez , Esaú Bojórquez-Velázquez , Eliel Ruiz-May , Elizabeth Carvajal-Millan , Magdalena Aguirre-García , Efraín Alday-Noriega , José Ángel Huerta-Ocampo , Humberto Astiazaran-Garcia","doi":"10.1016/j.jprot.2025.105540","DOIUrl":"10.1016/j.jprot.2025.105540","url":null,"abstract":"<div><div>Visceral obesity is closely related to insulin resistance (IR), a key process in developing metabolic diseases. Adipocyte-derived extracellular vesicles (AdEVs) have emerged as mediators of intercellular communication, carrying signals reflecting adipose tissue's functional state. This study aimed to perform a comparative proteomic analysis of AdEVs to propose a molecular fingerprint of specific biomarker candidates for IR in early-onset obesity. AdEVs were isolated from epididymal adipocytes of 16-week-old male Wistar rats on a high-fat diet (HFD) and controls and analyzed by mass spectrometry coupled to a multi-software protein identification bioinformatics strategy. For relative quantification using the label-free method, more than 1200 proteins were identified, with 431 being overrepresented and unique to HFD, associated explicitly with energy metabolism, cellular stress, and insulin signaling. Based on biological plausibility, and/or the best log2FC and <em>p</em>-value scores, six proteins were proposed as part of the IR molecular fingerprint: Atp5f1b, Anxa6, Myo1c, GLUT4, Anxa5, and Aoc3. Phosphoproteomic analysis revealed key modifications in phosphorylated proteins such as CaATPase (S663), PLIN (S130), and PPM1H (S260,265). The results suggest that AdEVs reflect early mitochondrial alterations related to IR, which could be employed as potential non-invasive biomarker candidates for metabolic dysfunction and follow-up in early overweight or obesity.</div><div>Significance</div><div>In this study, we demonstrate that adipocyte-derived extracellular vesicles (AdEVs) encapsulate a stage-resolved molecular signature that reflects key pathophysiological events underlying the early development of insulin resistance in obesity. These vesicles carry proteins linked to lipotoxicity, mitochondrial and endoplasmic reticulum stress, and impaired vesicular trafficking, offering mechanistic insight into how local adipocyte dysfunction may trigger systemic metabolic impairment. This EV-based proteomic fingerprint advances our understanding of insulin resistance pathogenesis and identifies potential biomarker candidates for early metabolic risk stratification.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105540"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145206649","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-09-11DOI: 10.1016/j.jprot.2025.105526
Agyeya Pratap , Kadambot H.M. Siddique , Nicolas L. Taylor
{"title":"Potential protein biomarkers for heat tolerance in wheat at seedling and ear peep stages","authors":"Agyeya Pratap , Kadambot H.M. Siddique , Nicolas L. Taylor","doi":"10.1016/j.jprot.2025.105526","DOIUrl":"10.1016/j.jprot.2025.105526","url":null,"abstract":"<div><div>Heat stress is a major threat to global wheat (<em>Triticum aestivum</em> L.) production, adversely affecting crop yields and grain quality. Understanding wheat's heat tolerance mechanisms is crucial for developing resilient cultivars. This study used targeted proteomics to validate heat-induced changes to protein abundances in seedling and flag leaves of heat-tolerant (Vixen-T) and heat-sensitive (HD2329-S) wheat genotypes. Proteomics samples were collected on days 1, 3 and 5 of heat exposure (32/16 °C day/night for 3 hours per day over 5 days) and day 12 post-recovery. Flag leaf gas exchange was studied under heat treatment during ear peep and significant genotype × heat treatment interactions were observed for all traits. Significant protein abundance changes occurred under heat stress for 15 and 14 proteins at the seedling and ear peep stages, respectively. Two key proteins—DM2 domain-containing protein (<em>r =</em> 0.99) and Rubisco activase (<em>r =</em> 0.96)—showed consistent responses across both developmental stages. Redox homeostasis and protein chaperone pathways emerged as major contributors to wheat heat tolerance. These findings highlight critical protein biomarkers that can support breeding efforts to develop heat-tolerant wheat varieties, offering valuable strategies for sustaining wheat productivity under climate change.</div></div><div><h3>Significance</h3><div>This study identifies and validates novel protein biomarkers associated with heat tolerance in wheat. These proteins were discovered in our previous study in the flag leaves of four genotypes with contrasting heat responses (tolerant: RAJ3765, HD2932; susceptible: HD2329, HD2733) under short-term heat stress at the ear peep stage. These biomarkers were further validated in two genotypes (tolerant: Vixen; susceptible: HD2329) under short-term heat stress at both seedling and ear peep stages. The validated protein isoforms span key biological processes, including photosynthesis, redox regulation, chromatin remodelling, protein folding, and carbohydrate and secondary metabolism. This panel of protein biomarkers offers a novel molecular framework for breeding heat-tolerant wheat, providing a strategic avenue, utilising targeted proteomics, to sustain yield under rising temperatures.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105526"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145058669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-10-18DOI: 10.1016/j.jprot.2025.105548
Phetolo Motsa , Beric Muller , Lesetja R. Motadi , Benedict C. Offor , Lizelle A. Piater
{"title":"Proteomic exploration of the recently Re-classified forest cobra Naja species and the potential cytotoxic activity in cancer cell lines","authors":"Phetolo Motsa , Beric Muller , Lesetja R. Motadi , Benedict C. Offor , Lizelle A. Piater","doi":"10.1016/j.jprot.2025.105548","DOIUrl":"10.1016/j.jprot.2025.105548","url":null,"abstract":"<div><div>The forest cobra (<em>Naja melanoleuca</em>) species represents one of the most widespread medically important elapid snakes across Africa. The immense tissue-damaging effect of cobra venoms is attributed to the cytotoxins (CTX), which predominate in virtually all cobra venoms. In this study a bottom-up venomic approach was followed for deciphering the composition of the <em>N. melanoleuca</em>, <em>N. subfulva</em>, and <em>N. savannula</em> venom proteomes. The results revealed complex venoms that constituted predominantly of proteins belonging to the three-finger toxins (3FTxs) followed by phospholipase A<sub>2</sub> (PLA<sub>2</sub>s) and snake venom metalloproteinases (SVMPs). The cytotoxicity and selectivity of the crude venoms and fractions were evaluated against cancer and normal cell lines. The crude <em>N. melanoleuca</em> venom sample demonstrated weak/low cytotoxic activity across the different cell lines as corroborated by SI values of less than 2, thus highlighting its limited application against these cancer cells, while the <em>N. subfulva</em> venom demonstrated its highest cytotoxic activity against the HeLa cancer cell line with a moderate selectivity index of 2.04. It is crucial to emphasize that these findings are still in the preliminary stages, primarily based on in vitro studies, and there remains a significant gap to bridge before any therapeutic applications can be considered.</div></div><div><h3>Significance</h3><div><em>Biological significance:</em> African forest cobra venom is a rich source of bioactive compounds such as cytotoxins, which cause tissue necrosis and descending paralysis. However, the venom has also been identified as a potential source of therapeutic agents, including anticancer agents. In this study, we evaluate the anticancer effects of the <em>N. melanoleuca</em>, <em>N. subfulva</em>, and <em>N. savannula</em> venoms and their fractions against the selected cell lines. The 3FTxs and PLA<sub>2</sub>s, which are the most abundant protein families in the venoms, are predominantly responsible for the cytotoxic effects. In conclusion, this research study highlights the important role of forest cobra venoms as potential resources that researchers can further exploit to investigate the molecules responsible for the anticancer effect and investigate their mechanisms of action.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105548"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145337249","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Journal of proteomicsPub Date : 2026-01-06Epub Date: 2025-10-23DOI: 10.1016/j.jprot.2025.105551
Robert Winkler , Aldo Moreno-Ulloa
{"title":"Advancing post-genomics research in Mexico: Opportunities and strategies for the next decade","authors":"Robert Winkler , Aldo Moreno-Ulloa","doi":"10.1016/j.jprot.2025.105551","DOIUrl":"10.1016/j.jprot.2025.105551","url":null,"abstract":"<div><div>The Mexican Proteomics Society (SMP) is the oldest proteomics organization in Latin America (LATAM), dedicated to advancing research in proteomics, metabolomics, and mass spectrometry (MS). As a non-profit, SMP organizes symposia and academic events, promoting collaboration and education. Since its founding in 2005, SMP has held biennial meetings and workshops in proteomics and metabolomics, invited international experts and fostered a multidisciplinary community. In this perspective manuscript, we provide a brief overview of the SMP, highlighting positive and negative aspects related to the economy, funding, infrastructure, technology and innovation, agriculture, health, and other fields. We also offer an overview of the MS equipment—critical infrastructure for omics research development—available within research centers and universities nationwide. Moreover, we present statistics on the contributions of Mexican-affiliated researchers to published research articles across various omics disciplines comparing Mexico's output to that of other LATAM countries. We believe that with this perspective the community will capture the role of the SMP in the development of omics research in Mexico, what is the country's contribution in the field, what are the country needs and how the new SMP board will contribute to advancing the field.</div></div><div><h3>Significance</h3><div>Omics-based societies play a crucial role in education, scientific development, and fostering multi-institutional collaborations. Although there are various societies worldwide focused on mass spectrometry-based omics, such as proteomics and metabolomics, their presence and impact on academia can be difficult to track. Therefore, in this manuscript, we provide a brief overview of the Mexican Proteomics Society (SMP), highlighting its contributions to omics research, the opportunities envisioned by the 2025-elected SMP leadership to advance omics science nationwide, and insights into the strategic directions for the coming decade.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105551"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145364006","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}