Biomedical subjects

Sittiruk Roytrakul

Publications and source records attributed to Sittiruk Roytrakul.

3 recordsLinked to original sources

PubMed2026

How elephant host proteins fight-or fail-against EEHV: Insights from a multi-contrast proteomic enrichment study.

Elephant endotheliotropic herpesvirus hemorrhagic disease (EEHV-HD) is a rapidly fatal syndrome of juvenile Asian elephants, but the host-response programs distinguishing progression from survival and the underlying pathophysiology remain poorly defined. The serum proteome of 62 Asian elephants (Elephas maximus) was profiled using a multi-contrast design stratified by age, clinical status, and infection history; protein abundance was analyzed by empirical Bayes linear modeling and Gene Ontology enrichment with semantic similarity reduction. Clinically affected elephants showed enrichment of inflammatory and stress-associated processes-including cytokine signaling and chromatin remodeling-with suppression of type I interferon signaling and homeostatic functions, whereas asymptomatic exposed elephants showed enrichment of metabolic pathways, including fatty acid and pyruvate metabolism, vesicle-mediated transport, and protein quality control. Disease-versus-exposure comparisons distinguished a progression program (inflammatory escalation with loss of proteostasis and cell adhesion) from a resilience program (preserved metabolic and cellular homeostasis); juvenile susceptibility was further associated with impaired lipid and calcium regulation and disrupted intracellular transport. Collectively, these patterns support a pathology-centered model in which fatal EEHV-HD reflects endothelial injury coupled with maladaptive inflammation and metabolic failure. Protein-level interpretation identified candidate drivers of inflammatory amplification, endothelial barrier disruption, coagulation imbalance, and resilience-including JAK1, IL1RL2, IFI44, KCNJ15, MSN, HECW2, ITPR3, MFN2, AKT1, BMPER, and DROSHA-providing a mechanistic bridge between serum proteomic changes and the vascular lesions, thrombocytopenia, DIC-like coagulopathy, edema, and hemorrhage of EEHV-HD. These findings nominate candidate proteomic signatures for future diagnostic and risk-stratification studies; longitudinal individual-level validation is required before clinical application. Because diagnostic screening identified all PCR-positive sick cases as EEHV1A and pooled group-level serum profiles were analyzed, these signatures should be interpreted as exploratory host-response programs specifically reflecting acute EEHV1A disease requiring individual-level validation.

Animals↗

PubMed2026

Time-resolved proteomic adaptation of multidrug-resistant Acinetobacter baumannii to antimicrobial stress induced by partially purified fraction from Caesalpinia pulcherrima flower using DEqMS.

UNLABELLED: The global prevalence of multidrug-resistant (MDR) bacteria represents an urgent public health challenge, emphasizing the critical need for novel antimicrobial agents. MDR Acinetobacter baumannii, a nosocomial pathogen of critical global concern owing to its capacity to acquire and disseminate antimicrobial resistance, was employed as a bacterial model to investigate the antimicrobial potential of natural products derived from Caesalpinia pulcherrima (L.) Sw. (Fabaceae). This medicinal plant represents a promising reservoir of novel bioactive compounds; however, its molecular effects on the A. baumannii proteome had not previously been characterized. The partially purified ethyl acetate fraction of C. pulcherrima flowers (CPF4) exhibited potent bactericidal activity against susceptible A. baumannii (minimum inhibitory concentration and minimum bactericidal concentration = 31.25 µg/mL), and time-resolved label-free quantitative LC-MS/MS proteomics was subsequently performed on MDR A. baumannii cultures treated with CPF4 at 24 h, 48 h, and 72 h post-treatment alongside untreated controls in biological triplicate, with differential protein expression assessed using differential expression of quantified mass spectrometry data. No significantly differentially expressed proteins were detected at 24 h or 48 h relative to the control, indicating that the proteomic effects of CPF4 manifest predominantly at the late treatment stage. In contrast, a robust late-phase response was identified at 72 h, comprising the coordinated induction of proteins associated with DNA damage repair, transcriptional regulation, and cell surface glycosylation remodeling. The sensor histidine kinase PmrB was significantly upregulated at 72 h vs 48 h (adjusted P = 0.029), implicating the PmrA/PmrB two-component system in late-phase colistin tolerance acquisition under sustained CPF4 exposure. IMPORTANCE: These findings provide mechanistic insight into the adaptive survival strategies employed by multidrug-resistant Acinetobacter baumannii in response to plant-derived antimicrobial challenge and support the further development of Caesalpinia pulcherrima-derived natural products as candidate antimicrobial agents.

Acinetobacter baumannii↗

PubMed2026

Comparative proteomics reveals distinct functions and localization of invasive Entamoeba histolytica and non-invasive Entamoeba moshkovskii proteins.

BACKGROUND: Entamoeba histolytica is a pathogenic protozoan accountable for amoebiasis, while Entamoeba moshkovskii is considered non-invasive. Despite morphological similarity, the molecular mechanisms underlying their different pathogenicity remain largely undefined. METHODS: Trophozoite proteins from axenic cultures of E. histolytica and E. moshkovskii were separated and identified using GeLC-MS/MS, and classified using Gene Ontology. Selected and differentially expressed proteins were validated by peptide-specific antibody production, ELISA, and immunofluorescence to determine cellular localization. RESULTS AND DISCUSSION: A total of 1,077 and 1,201 proteins were identified from E. histolytica and E. moshkovskii, respectively. The 801 of Entamoeba common proteins included kinases, GTPase-activating proteins, and heat shock proteins, reflecting conserved cellular processes. E. histolytica-unique proteins involved in nitrogen compound metabolism, vesicle-mediated transport, and catalytic activities, whereas E. moshkovskii proteins were related to lipid metabolism and environmental resilience. Subcellular localization revealed species-specific distribution of MmpL and AIG1-family proteins, suggesting potential roles in pathogenicity and host-immune response. A large proportion of hypothetical proteins was identified, highlighting gaps and opportunities for future study. CONCLUSIONS: Our study highlights conserved and divergent functions and cellular locations of Entamoeba species-specific proteins as insights for distinct pathogenicity and adaptation. MmpL and AIG1 proteins were proposed as potential targets for further diagnostic and therapeutic development.

Proteomics↗