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Brucellosis is a zoonotic infectious disease caused by the Brucella spp., and the enhancement of diagnostic techniques is imperative for effective disease control. Currently, the diagnosis of brucellosis predominantly relies on serological tests, bacterial culture, and molecular biology methods. Among these approaches, serological diagnosis is the most widely utilized due to its relative simplicity. However, existing diagnostic antigens encounter challenges, such as cross-reactivity. Consequently, the development of novel antigens with high specificity and sensitivity is essential to improve the accuracy and efficiency of serological diagnosis for brucellosis. In this study, five antigenic proteins-Erythritol kinase, Nucleoside diphosphate kinase (NDK), Adenosylhomocysteinase, the 31 kDa immunogenic protein, and Lyso-ornithine lipid O-acyltransferase-were selected, and B-cell linear epitopes were predicted using bioinformatics tools. Four prediction tools, namely ABCpred, SVMTriP, BCPred, and Bepipred Linear Epitope Prediction 2.0, were employed to screen for overlapping candidate epitopes. Fusion proteins were constructed through prokaryotic expression to serve as antigens for serological diagnosis. The sensitivity and specificity of the fusion protein were evaluated using indirect ELISA to detect human IgG antibodies in serum samples. The results indicated that the fusion protein achieved sensitivity and specificity values of 0.8095 and 0.9949, respectively. Although these values were lower in comparison to traditional antigens such as lipopolysaccharide (LPS) and the Rose Bengal antigen, the fusion protein exhibited improved cross-reactivity. This study successfully developed a multiepitope fusion protein for the diagnosis of brucellosis, thereby providing a foundation for the creation of highly specific and sensitive diagnostic antigens.
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http://dx.doi.org/10.1038/s41598-025-04244-5 | DOI Listing |
J Mater Chem B
September 2025
Malopolska Centre of Biotechnology, Jagiellonian University, Krakow 30-387, Poland.
Degradation during production and delivery is a significant bottleneck in developing biomolecular therapies. Protein cages, formed by engineered variants of lumazine synthase, present an effective strategy for the microbial production and isolation of labile biomolecular therapies. Genetic fusion of the target polypeptide to a cage component protomer ensures its efficient encapsulation within the cage during production in host bacterial cells, thereby protecting it from degradation.
View Article and Find Full Text PDFChembiochem
September 2025
Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Kuprevich str. 5/2, 220084, Minsk, Belarus.
The terminal deoxynucleotidyl transferase is a unique polymerase that incorporates nucleotides at the 3'-terminus of single-stranded DNA primers in a template-independent manner. This biological function propels the development of numerous biomedical and bioengineering applications. However, the extensive use of TdT is constrained by its low expression levels in E.
View Article and Find Full Text PDFJ Med Chem
September 2025
Guangzhou National Laboratory, Guangzhou 510005, P. R. China.
Respiratory syncytial virus (RSV) is a major pathogen causing acute respiratory infections, and the RSV fusion glycoprotein (F) has been identified as a key target for developing small-molecule inhibitors. Based on our prior identification of lonafarnib as an F protein inhibitor, medicinal chemistry efforts led to the development of , which exhibits significantly enhanced potency against both laboratory and clinical RSV isolates in cellular assays. Time-of-addition and SPR assays indicate that inhibits viral entry by targeting the RSV F protein, but has farnesyltransferase-independent antiviral efficacy.
View Article and Find Full Text PDFAdv Healthc Mater
September 2025
Epigenetics Research Laboratory, Institute of Nano Science and Technology, Knowledge City, Sector 81, Mohali, Punjab, 140306, India.
Acute Myeloid Leukemia (AML) is a heterogeneous hematological malignancy with an altered bone marrow microenvironment sheltering leukemic stem cells (LSCs). LSCs are characterized as self-renewing and highly proliferative cancer stem cells and accumulate abnormal genetic and epigenetic factors contributing to their uncontrolled proliferation. Chromosomal translocation t(9;11)(p22;q23) forms fusion oncoprotein, MLL-AF9, and regulates the transcription factor, C-Myb, which is highly expressed in AML.
View Article and Find Full Text PDFNat Biotechnol
September 2025
Key Laboratory of RNA Innovation, Science and Engineering, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, China.
Targeted protein degraders hold potential as therapeutic agents to target conventionally 'undruggable' proteins. Here, we develop a high-throughput screen, DEath FUSion Escaper (DEFUSE), to identify small-molecule protein degraders. By conjugating the protein of interest to a fast-acting triggerable death protein, this approach translates target protein degradation into a cell survival phenotype to illustrate the presence of degraders.
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