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Huntington's disease (HD) is a hereditary neurodegenerative condition caused by a CAG repeat expansion mutation in the gene encoding the huntingtin (HTT) protein. The accumulation of HTT inclusion bodies is a pathological hallmark of HD and a common target for therapeutic strategies. However, the limited efficacy of treatments targeting the HTT protein highlights the need for a better understanding of the role of HTT inclusion bodies in HD pathogenesis. This study examined the heterogeneity of HTT inclusion body composition by co-labelling with three HTT epitope-specific antibodies to characterize HTT inclusion body 'immunophenotype'. We then characterized the size and sub-cellular location of HTT inclusions with distinct immunophenotypes. Using multiplex immunohistochemistry, we also examined the ubiquitination profile of each immunophenotype. Our findings demonstrate that HTT inclusions have a range of immunophenotypes, with some labelled by only one of the three antibodies and others exhibiting co-labelling by several antibodies, thus demonstrating the heterogeneity in inclusion composition and structure. We outline evidence that inclusion bodies exclusively labelled with the EM48 antibody are small, non-nuclear, and more abundant in HD cases with increased CAG repeat length, higher Vonsattel grade, and earlier age of onset. We also find that HTT inclusion bodies labelled by multiple antibodies are more likely to be ubiquitinated, predominantly by K63- rather than K48-linked ubiquitin, suggesting preferential degradation by autophagy. Lastly, we show that ubiquitinated HTT inclusion bodies are more highly immunoreactive for ubiquilin 2 than p62. Our findings highlight the need for multiple antibodies to capture the full spectrum of HTT pathology in HD and imply that future studies should consider the diversity of inclusion body composition and structure when correlating pathology formation to neurodegeneration, clinical symptoms, or disease severity.
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http://dx.doi.org/10.1038/s41598-025-00465-w | DOI Listing |
ACS Synth Biol
September 2025
The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, P. R. China.
Human Bone Morphogenetic Protein-2 (hBMP-2) serves as a critical regulator in bone and cartilage formation; however, its industrial application is hindered by its inherent tendency to form inclusion bodies in prokaryotic expression systems. To address this issue, we established a recombinant hBMP-2 (rhBMP-2) expression system using the pCold II plasmid and the SHuffle T7 strain. We explored several strategies to enhance the solubility of rhBMP-2, including coexpression with molecular chaperones, vesicle-mediated secretory expression, fusion expression with synthetic intrinsically disordered proteins (SynIDPs), and fusion expression with small-molecule peptide tags.
View Article and Find Full Text PDFJ Adv Nurs
September 2025
School of Nursing, Paramedicine and Healthcare Sciences, Charles Sturt University, Bathurst, New South Wales, Australia.
Aim: The aim of this integrative review was to explore registered nurses' understandings of organisational culture and cultures of care in aged care.
Design: Integrative literature review.
Methods: A literature search was conducted of Medline (OVID), CINAHL Plus with Full Text, Scopus, Proquest Nursing and Allied Health, and Informit databases in June 2024.
Bioresour Technol
September 2025
State Key Laboratory of Food Science and Resources, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China; School of Biotechnology and Key Laboratory of Industrial Biotechnology Ministry of Education, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China; International Joint Laboratory on Fo
Recombinant proteins have been widely applied in the food, biomedical, and scientific fields. Prokaryotic expression systems are preferred platforms for recombinant protein production due to their rapid growth and high protein yields. Nevertheless, disparities between recombinant expression environment and native physiological conditions frequently result in protein misfolding, leading to aggregation into non-functional inclusion bodies or proteolytic degradation.
View Article and Find Full Text PDFRehabilitacion (Madr)
September 2025
Department of Physical Education, Malabar College of Advanced Studies, Vengara, Kerala, India.
Research on sports for persons with disabilities (PWDs) has grown significantly in recent years, particularly in parasports, disability sports, and adapted sports. Numerous studies have consistently highlighted the role of sports as a powerful tool for promoting social integration, enhancing psychological well-being, and improving the physical health of PWDs. However, comprehensive reviews on the development and progression of this field remain limited.
View Article and Find Full Text PDFProtein Expr Purif
September 2025
Department of Brewing Engineering, Moutai Institute, Zunyi, 564507, PR China.
Aldehyde dehydrogenase 2 (ALDH2) plays a critical role in ethanol metabolism by converting toxic acetaldehyde to acetate. To investigate its functional mechanisms and potential therapeutic applications for alcohol-related diseases, heterologous expression of ALDH2 is essential. However, ALDH2 often forms inclusion bodies when expressed in Escherichia coli.
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