SARS-CoV-2 virus-like-particles via liposomal reconstitution of spike glycoproteins

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Autor(es): dc.contributorToronto Metropolitan University-
Autor(es): dc.contributorUnity Health Toronto-
Autor(es): dc.contributorUniversity of Toronto-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorThe First Affiliated Hospital of Guangzhou Medical University-
Autor(es): dc.contributorUniversity of Calgary-
Autor(es): dc.creatorMcColman, Sarah-
Autor(es): dc.creatorShkalla, Klaidi-
Autor(es): dc.creatorSidhu, Pavleen-
Autor(es): dc.creatorLiang, Jady-
Autor(es): dc.creatorOsman, Selena-
Autor(es): dc.creatorKovacs, Norbert-
Autor(es): dc.creatorBokhari, Zainab-
Autor(es): dc.creatorForjaz Marques, Ana Carolina-
Autor(es): dc.creatorLi, Yuchong-
Autor(es): dc.creatorLin, Qiwen-
Autor(es): dc.creatorZhang, Haibo-
Autor(es): dc.creatorCramb, David T.-
Data de aceite: dc.date.accessioned2025-08-21T20:04:19Z-
Data de disponibilização: dc.date.available2025-08-21T20:04:19Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2023-07-14-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1039/d3na00190c-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/297607-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/297607-
Descrição: dc.descriptionThe SARS-CoV-2 virus, implicated in the COVID-19 pandemic, recognizes and binds host cells using its spike glycoprotein through an angiotensin converting enzyme 2 (ACE-2) receptor-mediated pathway. Recent research suggests that spatial distributions of the spike protein may influence viral interactions with target cells and immune systems. The goal of this study has been to develop a liposome-based virus-like particle (VLP) by reconstituting the SARS-CoV-2 spike glycoprotein within a synthetic nanoparticle membrane, aiming to eventually establish tunability in spike protein presentation on the nanoparticle surface. Here we report on first steps to this goal, wherein liposomal SARS-CoV-2 VLPs were successfully produced via detergent mediated spike protein reconstitution. The resultant VLPs are shown to successfully co-localize in vitro with the ACE-2 receptor on lung epithelial cell surfaces, followed by internalization into these cells. These VLPs are the first step toward the overall goal of this research which is to form an understanding of the relationship between spike protein surface density and cell-level immune response, eventually toward creating better vaccines and anti-viral therapeutics.-
Descrição: dc.descriptionHealth Research-
Descrição: dc.descriptionScience and Engineering Research Council-
Descrição: dc.descriptionHospital for Sick Children-
Descrição: dc.descriptionThe Research Council-
Descrição: dc.descriptionUniversity of Calgary-
Descrição: dc.descriptionUniversity of Toronto-
Descrição: dc.descriptionDepartment of Chemistry and Biology Faculty of Science Toronto Metropolitan University-
Descrição: dc.descriptionKeenan Research Centre for Biomedical Science St. Michael's Hospital Unity Health Toronto-
Descrição: dc.descriptionDepartment of Physiology University of Toronto-
Descrição: dc.descriptionFaculdade de Ciências Farmacêuticas Seção Técnica de Graduação Universidade Estadual Paulista, SP-
Descrição: dc.descriptionThe State Key Laboratory of Respiratory Disease Guangzhou Institute of Respiratory Disease The First Affiliated Hospital of Guangzhou Medical University, Guangdong-
Descrição: dc.descriptionDepartments of Anaesthesia and Physiology Interdepartmental Division of Critical Care Medicine University of Toronto-
Descrição: dc.descriptionDepartment of Chemistry Faculty of Science University of Calgary-
Descrição: dc.descriptionFaculdade de Ciências Farmacêuticas Seção Técnica de Graduação Universidade Estadual Paulista, SP-
Formato: dc.format4167-4181-
Idioma: dc.languageen-
Relação: dc.relationNanoscale Advances-
???dc.source???: dc.sourceScopus-
Título: dc.titleSARS-CoV-2 virus-like-particles via liposomal reconstitution of spike glycoproteins-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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