{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Qazi S"],"funding":["American Heart Association","Amgen","MJ Murdock Charitable Trust","Office of Experimental Program to Stimulate Competitive Research","National Institute of General Medical Sciences","NIGMS NIH HHS","National Science Foundation"],"pagination":["1191-6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7734702"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(3)"],"pubmed_abstract":["Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) RNA-guided endonucleases are powerful new tools for targeted genome engineering. These nucleases provide an efficient and precise method for manipulating eukaryotic genomes; however, delivery of these reagents to specific cell-types remains challenging. Virus-like particles (VLPs) derived from bacteriophage P22, are robust supramolecular protein cage structures with demonstrated utility for cell type-specific delivery of encapsulated cargos. Here, we genetically fuse Cas9 to a truncated form of the P22 scaffold protein, which acts as a template for capsid assembly as well as a specific encapsulation signal for Cas9. Our results indicate that Cas9 and a single-guide RNA are packaged inside the P22 VLP, and activity assays in"],"journal":["Molecular pharmaceutics"],"pubmed_title":["Programmed Self-Assembly of an Active P22-Cas9 Nanocarrier System."],"pmcid":["PMC7734702"],"funding_grant_id":["P20GM103500","R01 GM108888","P20 GM103500","R01GM108888","EPS-110134","BMAT- 1507282"],"pubmed_authors":["McCoy K","Wilkinson RA","Qazi S","Wiedenheft B","Miettinen HM","Douglas T"],"additional_accession":[]},"is_claimable":false,"name":"Programmed Self-Assembly of an Active P22-Cas9 Nanocarrier System.","description":"Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR) RNA-guided endonucleases are powerful new tools for targeted genome engineering. These nucleases provide an efficient and precise method for manipulating eukaryotic genomes; however, delivery of these reagents to specific cell-types remains challenging. Virus-like particles (VLPs) derived from bacteriophage P22, are robust supramolecular protein cage structures with demonstrated utility for cell type-specific delivery of encapsulated cargos. Here, we genetically fuse Cas9 to a truncated form of the P22 scaffold protein, which acts as a template for capsid assembly as well as a specific encapsulation signal for Cas9. Our results indicate that Cas9 and a single-guide RNA are packaged inside the P22 VLP, and activity assays in","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Mar","modification":"2025-04-22T02:08:02.388Z","creation":"2021-02-20T10:54:11Z"},"accession":"S-EPMC7734702","cross_references":{"pubmed":["26894836"],"doi":["10.1021/acs.molpharmaceut.5b00822"]}}