Virus-like particles (VLP) could enable a wide variety of biomedical applications in therapy, drug delivery, and imaging. They are biocompatible and can be self-assembled into larger structured materials for additional functionality and potentially better biodistribution, which is still a challenging aspect. Here we investigate the role of the VLPs size and resulting Caspar Klug symmetry in forming clusters out of these building blocks, showing that the onset point for clustering is determined by steric considerations of the binding site and binding agent. The clustering is independent of cargo and the data suggests that rotational symmetry in the T = 3 capsid allows for hexagonal close packed structures, whereas the T = 1 capsid that lacks a six-fold and twofold rotational axis does not show such organization.
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http://dx.doi.org/10.1002/mabi.201400326 | 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 PDFProtein Sci
January 2025
Department of Physical Chemistry, Institute of Biotechnology, and Unit of Excellence in Chemistry Applied to Biomedicine and Environment, School of Sciences, University of Granada, Granada, Spain.
The ubiquitin E2 variant domain of TSG101 (TSG101-UEV) plays a pivotal role in protein sorting and virus budding by recognizing PTAP motifs within ubiquitinated proteins. Disruption of TSG101-UEV/PTAP interactions has emerged as a promising strategy for the development of host-oriented broad-spectrum antivirals with low susceptibility to resistance. TSG101 is a challenging target characterized by an extended and flat binding interface, low affinity for PTAP ligands, and complex binding energetics.
View Article and Find Full Text PDFBiotechnol Bioeng
December 2024
Institute of Process Engineering in Life Sciences, Section IV: Biomolecular Separation Engineering, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.
Virus-like particles (VLPs) are a versatile technology for the targeted delivery of genetic material through packaging and potential surface modifications for directed delivery or immunological issues. Although VLP production is relatively simple as they can be recombinantly produced using microorganisms such as Escherichia coli, their current downstream processing often relies on individually developed purification strategies. Integrating size-selective separation techniques may allow standardized platform processing across VLP purification.
View Article and Find Full Text PDFVaccine
December 2024
Mucosal Immunoogy Laboratory, Biomedicine Research Unit, Faculty of Higher Studies Iztacala, National Autonomous University of Mexico. Avenida de los Barrios 1, Los Reyes Iztacala, Tlalnepantla, Estado de México 54090, Mexico. Electronic address:
The development of a protective HIV vaccine remains a challenge given the high antigenic diversity and mutational rate of the virus, which leads to viral escape and establishment of reservoirs in the host. Modern antigen design can guide immune responses towards conserved sites, consensus sequences or normally subdominant epitopes, thus enabling the development of broadly neutralizing antibodies and polyfunctional lymphocyte responses. Conventional epitope vaccines can often be impaired by low immunogenicity, a limitation that may be overcome by using a carrier system.
View Article and Find Full Text PDFExpert Rev Vaccines
December 2024
Guangzhou Patronus Biotech Co, Ltd, Guangzhou, China.
Background: LYB001 is a recombinant protein COVID-19 vaccine displaying a receptor-binding domain (RBD) in a highly immunogenic array on virus-like particles (VLPs). This study assessed the immunogenicity and safety of LYB001 as a booster.
Research Design And Methods: In this randomized, active-controlled, double-blinded, phase 3 trial, participants aged ≥18 years received a booster with LYB001 or ZF2001 (Recombinant COVID-19 Vaccine).
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