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With the emergence of more variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the immune evasion of these variants from existing vaccines, the development of broad-spectrum vaccines is urgently needed. In this study, we designed a novel SARS-CoV-2 receptor-binding domain (RBD) subunit (RBD5m) by integrating five important mutations from SARS-CoV-2 variants of concern (VOCs). The neutralization activities of antibodies induced by the RBD5m candidate vaccine are more balanced and effective for neutralizing different SARS-CoV-2 VOCs in comparison with those induced by the SARS-CoV-2 prototype strain RBD. Our results suggest that the RBD5m vaccine is a good broad-spectrum vaccine candidate able to prevent disease from several different SARS-CoV-2 VOCs.
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http://dx.doi.org/10.3390/vaccines10101653 | DOI Listing |
Phys Chem Chem Phys
September 2025
School of Chemistry and Chemical Engineering, University of Jinan, Jinan 250022, P. R. China.
The COVID-19 pandemic remains a global health crisis, with successive SARS-CoV-2 variants exhibiting enhanced transmissibility and immune evasion. Notably, the Omicron variant harbors extensive mutations in the spike protein's receptor-binding domain (RBD), altering viral fitness. While temperature is a critical environmental factor modulating viral stability and transmission, its molecular-level effects on variant-specific RBD-human angiotensin-converting enzyme 2 (hACE2) interactions remain underexplored.
View Article and Find Full Text PDFMacromol Biosci
September 2025
Department of Pharmaceutical Technology, Faculty of Pharmacy, Ankara University, Tandogan, Ankara, Turkey.
The COVID-19 pandemic caused by the novel coronavirus SARS-CoV-2 has highlighted the critical need for safe and effective vaccines. In this study, subunit nanovaccine formulations were developed using the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein encapsulated in polymeric nanoparticles composed of poly(ethylene glycol)-block-poly(ε-caprolactone) (PEG-PCL). Two surfactants, poly(vinyl alcohol) (PVA) and sodium cholate (SC), were evaluated during formulation via a modified water-in-oil-in-water (w/o/w) emulsion-solvent evaporation method.
View Article and Find Full Text PDFJ Virol Methods
September 2025
Laboratorio de Inmunología, Centro de Investigación en Alimentación y Desarrollo, A.C. Hermosillo, Sonora, Mexico. Electronic address:
Bispecific antibodies (bsAbs) offer an alternative to monoclonal antibody (mAb) cocktails for addressing the loss of efficacy due to the rapid emergence of SARS-CoV-2 mutants. The structure and specificity of the parental antibodies influence the development of a highly neutralizing bsAb. To design an effective bsAb, the recognition of 44 single-chain fragment variable (scFv) antibodies against variants of SARS-CoV-2 was evaluated, along with an assessment of their ability to competitively bind to the receptor-binding domain (RBD) compared to the most potent neutralizing mAbs.
View Article and Find Full Text PDFCell Rep
September 2025
Virginia Tech Fralin Biomedical Research Institute Cancer Research Center DC, Children's National Research & Innovation Campus, Washington, DC, USA; Department of Biomedical Sciences and Pathobiology (DBSP), Virginia-Maryland College of Veterinary Medicine, Virginia Tech, Blacksburg, VA, USA; Center
Nuclear receptor binding set domain protein 1 (NSD1) is a key histone methyltransferase that catalyzes di-methylation of lysine 36 of histone H3 (H3K36me2), essential for active chromatin domains. While the loss of NSD1 activity halts embryonic development and its aberrant gain drives oncogenesis in leukemia and glioma, the regulatory mechanisms remain poorly understood. Here, we uncover that NSD1 requires allosteric activation through the aromatic pocket of its Pro-Trp-Trp-Pro 2 (PWWP2) domain.
View Article and Find Full Text PDFJ Thorac Oncol
September 2025
Department of Pathology and Clinical Laboratories, National Cancer Center Hospital East, Kashiwa, Chiba, Japan; Course of Advanced Clinical Research of Cancer, Juntendo University Graduate School of Medicine, Tokyo, Japan; Division of Innovative Pathology and Laboratory Medicine, Exploratory Oncolog
Introduction: Nuclear receptor-binding SET domain 3 (NSD3) has been implicated as a driver of lung squamous cell carcinoma (LUSC) in preclinical studies. However, its clinicopathological characteristics and prognostic significance remain unclear. To address this, we performed histopathological analysis of patient tissues.
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