In vitro assembly of nucleocapsid-like particles from purified recombinant capsid protein of dengue-2 virus

• Published in: Archives of virology Vol. 154; no. 4; pp. 695 - 698
• Main Authors: López, Carlos, Gil, Lázaro, Lazo, Laura, Menéndez, Ivón, Marcos, Ernesto, Sánchez, Jorge, Valdés, Iris, Falcón, Viviana, de la Rosa, María C, Márquez, Gabriel, Guillén, Gerardo, Hermida, Lisset
• Format: Journal Article
• Language: English
• Published: Vienna Vienna : Springer Vienna 01.04.2009; Springer Vienna; Springer; Springer Nature B.V
• Subjects: Biological and medical sciences; Biomedical and Life Sciences; Biomedicine; Brief Report; Capsid Proteins - genetics; Capsid Proteins - metabolism; Chromatography; Dengue fever; Dengue virus; Dengue Virus - physiology; Dengue virus type 2; DNA, Single-Stranded - metabolism; E coli; Encephalitis; Escherichia coli; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; Genomes; Hepatitis; Infectious Diseases; Medical Microbiology; Microbiology; Microscopy; Microscopy, Electron, Transmission; Miscellaneous; Molecular weight; Protein Binding; Proteins; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Virology; Virosomes - genetics; Virosomes - metabolism; Virosomes - ultrastructure; Virus Assembly; Viruses; Cation Exchange Chromatography; Capsid Protein; Yellow Fever; Yellow Fever Virus; Dengue Virus; Virus; Dengue group virus; Nucleocapsid; Dengue virus 2; Recombinant protein; Flaviviridae; Capsid; Flavivirus; In vitro
• ISSN: 0304-8608; 1432-8798
• DOI: 10.1007/s00705-009-0350-8

The capsid protein is one of the three structural proteins of flaviviruses and is the building block of the nucleocapsid. It has also a predominant role in the replication of dengue virus. To obtain nucleocapsid-like particles from recombinant dengue-2 capsid protein produced in E. coli, a purification process using cation exchange chromatography was established. The purified protein exhibited a molecular mass corresponding to a dimer; therefore, similar to that reported for alphaviruses, an in vitro assembly reaction using single-stranded DNA was performed. In all cases, particles were obtained independently of the specificity and the length of the oligonucleotides used. The present work is the first report of in vitro assembly of the recombinant dengue capsid protein, which could constitute a powerful tool in the development of vaccine candidates.