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Production of VP3-only virus-like particles of Adeno-associated virus 2 in E. coli cells.
Fu, Chengyu; Gobbooru, Shruthi; Martino, Ashley T; Low, Woon-Kai.
Afiliação
  • Fu C; Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, St. John's University, 8000 Utopia Parkway, Queens, NY, 11439, USA.
  • Gobbooru S; Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, St. John's University, 8000 Utopia Parkway, Queens, NY, 11439, USA.
  • Martino AT; Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, St. John's University, 8000 Utopia Parkway, Queens, NY, 11439, USA.
  • Low WK; Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, St. John's University, 8000 Utopia Parkway, Queens, NY, 11439, USA. Electronic address: loww@stjohns.edu.
Protein Expr Purif ; 220: 106502, 2024 Aug.
Article em En | MEDLINE | ID: mdl-38754753
ABSTRACT
Adeno-associated Virus (AAV) is a promising vector for gene therapy. However, few studies have focused on producing virus-like particles (VLPs) of AAV in cells, especially in E. coli. In this study, we describe a method to produce empty VP3-only VLPs of AAV2 in E. coli by co-expressing VP3 and assembly-activating protein (AAP) of AAV2. Although the yields of VLPs produced with our method were low, the VLPs were able to self-assemble in E. coli without the need of in vitro capsid assembly. The produced VLPs were characterized by immunological detection and transmission electron microscopy (TEM). In conclusion, this study demonstrated that capsid assembly of AAV2 is possible in E. coli, and E. coli may be a candidate system for production of VLPs of AAV.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Dependovirus / Proteínas do Capsídeo / Escherichia coli Limite: Humans Idioma: En Revista: Protein Expr Purif Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Dependovirus / Proteínas do Capsídeo / Escherichia coli Limite: Humans Idioma: En Revista: Protein Expr Purif Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Estados Unidos