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http://dx.doi.org/10.1016/j.rec.2019.07.001 | DOI Listing |
Sci Rep
December 2024
Department of Anatomy, Faculty of Science, Mahidol University, 272 Rama VI Road, Ratchathewi, Bangkok, 10400, Thailand.
SARS-CoV-2, the cause of COVID-19, primarily targets lung tissue, leading to pneumonia and lung injury. The spike protein of this virus binds to the common receptor on susceptible tissues and cells called the angiotensin-converting enzyme-2 (ACE2) of the angiotensin (ANG) system. In this study, we produced chimeric Macrobrachium rosenbergii nodavirus virus-like particles, presenting a short peptide ligand (ACE2tp), based on angiotensin-II (ANG II), on their outer surfaces to allow them to specifically bind to ACE2-overexpressing cells called ACE2tp-MrNV-VLPs.
View Article and Find Full Text PDFFront Immunol
December 2024
Laboratory of Molecular Medicine, Department of Clinical Immunology, Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark.
Throughout the COVID-19 pandemic, the emergence of new viral variants has challenged public health efforts, often evading antibody responses generated by infections and vaccinations. This immune escape has led to waves of breakthrough infections, raising questions about the efficacy and durability of immune protection. Here we focus on the impact of SARS-CoV-2 Delta and Omicron spike mutations on ACE-2 receptor binding, protein stability, and immune response evasion.
View Article and Find Full Text PDFMol Ther Nucleic Acids
December 2024
McAllister Heart Institute, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Direct cardiac reprogramming of fibroblasts into induced cardiomyocytes (iCMs) can be achieved by ectopic expression of cardiac transcription factors (TFs) via viral vectors. However, risks like genomic mutations, viral toxicity, and immune response limited its clinical application. Transactivation of endogenous TFs emerges as an alternative approach that may partially mitigate some of the risks.
View Article and Find Full Text PDFCommun Biol
December 2024
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Study of mechanisms by which antibodies recognize different viral strains is necessary for the development of new drugs and vaccines to treat COVID-19 and other infections. Here, we report 2.5 Å cryo-EM structure of the SARS-CoV-2 Delta trimeric S-protein in complex with Fab of the recombinant analog of REGN10987 neutralizing antibody.
View Article and Find Full Text PDFSmall
December 2024
Chemical Biology Unit, Institute of Nano Science and Technology (INST), Sector 81, Mohali, Punjab, 140306, India.
Dynamic peptide networks represent an attractive structural space of supramolecular polymers in the realm of emergent complexity. Point mutations in the peptide sequence exert profound effects over the landscapes of self-assembly with an intricate interplay among the structure-function relationships. Herein, the pathway complexity of an arginine-rich peptide is studied, FmocVFFARR derived by the mutation of minimalist amyloid-inspired peptide amphiphile FmocVFFAKK, thereby focusing on its pathway-dependent self-assembly behavior.
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