Virus-like particles (VLPs) modified through different molecular technologies are employed as delivery vehicles or platforms for heterologous antigen display. We have recently created a norovirus (NoV) VLP platform, where two influenza antigens, the extracellular domain of matrix protein M2 (M2e) or the stem domain of the major envelope glycoprotein hemagglutinin (HA2) are displayed on the surface of the NoV VLPs by SpyTag/SpyCatcher conjugation. To demonstrate the feasibility of the platform to deliver foreign antigens, this study examined potential interference of the conjugation with induction of antibodies against conjugated M2e peptide, HA2, and NoV VLP carrier. High antibody response was induced by HA2 but not M2e decorated VLPs. Furthermore, HA2-elicited antibodies did not neutralize the homologous influenza virus in vitro. Conjugated NoV VLPs retained intact receptor binding capacity and self-immunogenicity. The results demonstrate that NoV VLPs could be simultaneously used as a platform to deliver foreign antigens and a NoV vaccine.
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http://dx.doi.org/10.1016/j.virol.2021.12.001 | DOI Listing |
Vaccines (Basel)
November 2024
Shanghai Zerun Biotech Co., Ltd., Building 9, 1690 Zhangheng Road, Pudong, Shanghai 201203, China.
Background: Cervical cancer is associated with persistent infection of high-risk human papillomaviruses (HPVs). Prophylactic HPV vaccines have been recommended and have significant efficacy in preventing cervical cancer. Multivalent HPV vaccines have a better preventative effect on HPV-related diseases.
View Article and Find Full Text PDFArch Virol
January 2025
Center for Translational Medicine, Affiliated Infectious Diseases Hospital of Zhengzhou University (Henan Infectious Diseases Hospital, The Sixth People's Hospital of Zhengzhou), Zhengzhou, 450000, People's Republic of China.
Trypsin digestion of the GII.6 norovirus (NoV) major capsid protein VP1 promotes its binding to histo-blood group antigens (HBGAs), which are believed to be co-receptors for NoVs. In our previous study, we found that trypsin digestion led to the disassembly of GII.
View Article and Find Full Text PDFCurr Res Microb Sci
November 2024
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia.
The threat of influenza A virus (IAV) remains an annual health concern, as almost 500,000 people die each year due to the seasonal flu. Current flu vaccines are highly dependent on embryonated chicken eggs for production, which is time consuming and costly. These vaccines only confer moderate protections in elderly people, and they lack cross-protectivity; thereby requiring annual reformulation to ensure effectiveness against contemporary circulating strains.
View Article and Find Full Text PDFJ Orthop
June 2025
Department of Orthopaedic Surgery, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Introduction: Despite randomized controlled trials (RCTs) largely supporting volar locking plates (VLPs) for the management of distal radius fractures (DRFs), surgeons often opt for non-invasive interventions such as casting. This study used the fragility index (FI), reverse fragility index (rFI), and fragility quotient (FQ) to assess the statistical robustness of RCTs assessing the efficacy of VLP in DRF management.
Methods: PubMed, Embase, and MEDLINE were queried for RCTs evaluating VLP versus casting for DRFs published from January 1st, 2000-June 30, 2024.
Int J Mol Sci
November 2024
Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology Russian Academy of Sciences, 119334 Moscow, Russia.
Virus-like particles (VLPs) are an attractive vehicle for the delivery of Cas nuclease and guide RNA ribonucleoprotein complexes (RNPs). Most VLPs are produced by packaging SpCas9 and its sgRNA, which is expressed from the RNA polymerase III (Pol III)-transcribed U6 promoter. VLPs assemble in the cytoplasm, but U6-driven sgRNA is localized in the nucleus, which hinders the efficient formation and packaging of RNPs into VLPs.
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