Background In a rapidly evolving viral landscape, understanding virus–host protein interactions (VHPIs) is essential to elucidate viral infection mechanisms and support the development of effective therapeutic strategies. Accurate computational Prediction of VHPIs remains challenging because of the complexity and high dimensionality of protein sequence and functional representations. Methods We propose a Knowledge Distillation framework for pairwise VHPI prediction that integrates three teacher networks with a hybrid student architecture. Protein characteristics were represented using Conjoint Triad (CT), Dipeptide Composition (DC), Dipeptide Deviation from Expected Mean (DDE), Pseudo-Amino Acid Composition (PseAAC), amino acid encoding, and Gene Ontology (GO) features. We used tuned Monte Carlo ISUD for feature selection and compared it with five alternative approaches: PCA, MCFS, NMF, FA, and Optuna. We used an autoencoder to compress the one-hot encoded GO features. We evaluated on 25 randomly balanced datasets and one additional balanced dataset generated using NearMiss. Five-fold cross-validation was performed at the interaction-pair level using an 80:20 training-to-test ratio in each fold. The final configuration consisted of CT features, NearMiss-based data balancing, tuned MC-ISUD feature selection, and the Knowledge Distillation teacher–student framework. Results The proposed framework achieved 92.91% accuracy and 96.16% AUC-ROC on the evaluated virus–host protein interaction datasets. Comparative experiments demonstrated that the proposed approach outperformed the existing methods considered in this study. These results are specific to the evaluated datasets and pairwise cross-validation design and should not be interpreted as evidence of generalization to completely unseen viral or host proteins. Conclusions The findings indicate that combining CT-based representation, NearMiss-based data balancing, tuned ISUD feature selection, and Knowledge Distillation provides a computational framework for pairwise VHPI prediction. The predictions should be regarded as computational hypotheses requiring independent experimental validation.
Background Hyaluronidase enzyme is frequently used by plastic surgeons in aesthetic procedures to break down hyaluronic acid. The potential benefits of hyaluronidase in the clinical management of conditions associated with diseases and aging in the skin connective tissue are a subject of ongoing research. In this study, we investigated the changes associated with the hyaluronidase enzyme injected subcutaneously into the dorsal region of rats in the skin connective tissue. Methods This is an experimental and qualitative study. A total of 24 Wistar albino rats were divided into three groups of eight each: Control (Group 1), Sham (Group 2), and Experimental (Group 3). In the study, no procedure was performed on Group 1, normal saline was injected into Group 2, and hyaluronidase enzyme was injected subcutaneously into Group 3. At the end of the 14th day, sections were taken from the skin connective tissue of the injection site, and histochemical examination and biochemical analyses were performed on these sections. This research received no external funding. Results In Group 1, the collagen fibers, vessels, and layers of the epidermis and dermis appeared normal. In Group 2, the normal organization of collagen fibers was disrupted in some areas, and the connective tissue was edematous. In Group 3, a decrease in collagen fiber density in some areas, structural abnormalities in collagen and elastic fibers, and edema were detected. TGF-β1 and MMP-1 measurement results were compared between groups, and no statistically significant difference was found (p > 0.05). Conclusion The results of this study indicate that the hyaluronidase enzyme is associated with a decrease in collagen fiber quantity, structural abnormalities in fibers, edema, and the development of impaired elastic fiber structures in skin connective tissue.
Triosephosphate isomerase 1 (TPI1) is a key glycolytic enzyme that catalyzes the reversible interconversion of dihydroxyacetone phosphate and glyceraldehyde-3-phosphate. Emerging evidence suggests that TPI1 also participates in cancer-associated non-canonical functions involving altered subcellular localization, protein–protein interactions, signaling regulation, and therapeutic responses. This narrative review summarizes the biochemical properties of TPI1 and critically evaluates its expression patterns, prognostic associations, molecular mechanisms, and therapeutic implications across malignancies. TPI1 is frequently upregulated in several cancer types, although its biological and clinical significance varies substantially among tumors. Experimental studies have identified potential moonlighting functions involving nuclear localization in lung adenocarcinoma and protein-interaction-dependent signaling in breast cancer, glioblastoma, and bladder cancer. In hepatocellular carcinoma, apparently conflicting findings may reflect differences in experimental models, cellular contexts, and intracellular versus extracellular-vesicle-associated TPI1. Emerging evidence also implicates TPI1 in tumor immune regulation and therapeutic resistance, although many findings remain based on computational associations or preclinical models. Current research is limited by insufficient prospective clinical validation and the absence of established, broadly applicable pharmacological strategies targeting TPI1. Collectively, TPI1 represents a context-dependent candidate biomarker and potential therapeutic target in cancer, warranting further mechanistic investigation and clinical validation. Registration Not applicable; this article is a narrative review.
Background BRCA1 is a critical tumor suppressor that maintains genomic integrity through its C-terminal BRCT tandem domain, which mediates phosphoprotein interactions involved in DNA damage response signaling. Missense variants within the BRCT domain may disrupt protein stability and phosphopeptide recognition; however, their functional interpretation is often complicated by conflicting computational predictions and limited experimental evidence. We characterized two Middle Eastern BRCA1 BRCT variants, M1652I and F1662S, identified in Bahraini and Lebanese cohorts, respectively and compared their structural and functional properties with the pathogenic R1699W variant. Methods The structural stability and binding thermodynamics of wild-type and mutant BRCA1 BRCT domains were evaluated using circular dichroism, thermal denaturation assays and isothermal titration calorimetry (ITC) with phosphorylated BACH1 and CtIP peptides. Results M1652I and F1662S retained secondary structure and thermal stability comparable to wild-type BRCA1, whereas R1699W exhibited partial destabilization and a reduced melting temperature (ΔTm = -5.3°C). ITC demonstrated that M1652I and F1662S preserved near wild-type binding affinities for phosphorylated BACH1 and CtIP peptides, while R1699W showed no detectable phosphopeptide binding under the conditions tested. Conclusions M1652I and F1662S preserve BRCT structural integrity and phosphopeptide recognition, supporting a likely benign functional effect on BRCA1 BRCT-mediated interactions. These findings highlight the value of experimental biophysical characterization for interpreting BRCA1 variants identified in underrepresented populations. A major limitation is the reliance on in vitro biophysical assays; therefore, additional cellular and in vivo functional studies are required to confirm the biological consequences of these variants.
