Journal
BIOCHIMIE
Volume 94, Issue 3, Pages 870-878Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2011.12.006
Keywords
Virus-like particles; Protein refolding; Nanotechnology; Virus structure
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Funding
- Instituto de Ciencia y Tecnologia del Distrito Federal (ICyTDF), Mexico [PIFUTP08-104]
- Consejo Nacional de Ciencia y Tecnologia (CONACyT), Mexico [99857]
- Alexander von Humboldt Foundation, Germany
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Virus-like particles (VLPs) are biological nanoparticles identical to the natural virions, but without genetic material. VLPs are suitable for the analysis of viral infection mechanisms, vaccine production, tissue-specific drug delivery, and as biological nanomaterials. Human parvovirus B19 (B19) infects humans; therefore VLPs derived from this virus have enormous potential in medicine and diagnostics. Current production of self-assembled VLPs derived from B19 is typically carried out in eukaryotic expression systems. However many applications of VLPs require access to its internal core. Consequently, the processes of disassembly and further reassembly of VLPs are critical both for purification of viral proteins, and for encapsulation purposes. Herein we report the in vitro self-assembly of B19 VLPs derived from the recombinant VP2 protein expressed in Escherichia coli and the effects of pH and ionic strength on the assembly process. Our results demonstrate that VP2 is able to form VLPs completely in vitro. At neutral pH, homogeneous VLPs assemble, while at acidic and basic pHs, with low ionic strength, the major assemblies are small intermediates. The in vitro self-assembled VLPs are highly stable at 37 degrees C, and a significant fraction of particles remain assembled after 30 min at 80 degrees C. (C) 2011 Elsevier Masson SAS. All rights reserved.
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