About: Assembly/disassembly of a complex icosahedral virus to incorporate heterologous nucleic acids

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Assembly/disassembly of a complex icosahedral virus to incorporate heterologous nucleic acids
Creator	Carrascosa, José Castón, José Mata, Carlos Pascual, Elena
source	PMC
abstract	Hollow protein containers are widespread in nature, and include virus capsids as well as eukaryotic and bacterial complexes. Protein cages are studied extensively for applications in nanotechnology, nanomedicine and materials science. Their inner and outer surfaces can be modified chemically or genetically, and the internal cavity can be used to template, store and/or arrange molecular cargos. Virus capsids and virus-like particles (VLP, noninfectious particles) provide versatile platforms for nanoscale bioengineering. Study of capsid protein self-assembly into monodispersed particles, and of VLP structure and biophysics is necessary not only to understand natural processes, but also to infer how these platforms can be redesigned to furnish novel functional VLP. Here we address the assembly dynamics of infectious bursal disease virus (IBDV), a complex icosahedral virus. IBDV has a ~70 nm-diameter T = 13 capsid with VP2 trimers as the only structural subunits. During capsid assembly, VP2 is synthesized as a precursor (pVP2) whose C terminus is cleaved. The pVP2 C terminus has an amphipathic helix that controls VP2 polymorphism. In the absence of the VP3 scaffolding protein, necessary for control of assembly, 466/456-residue pVP2 intermediates bearing this helix assemble into VLP only when expressed with an N-terminal His(6) tag (the HT-VP2-466 protein). HT-VP2-466 capsids are optimal for genetic insertion of proteins (cargo space ~78 000 nm(3)). We established an in vitro assembly/disassembly system of HT-VP2-466-based VLP for heterologous nucleic acid packaging and/or encapsulation of drugs and other molecules. HT-VP2-466 (empty) capsids were disassembled and reassembled by dialysis against low-salt/basic pH and high-salt/acid pH buffers, respectively, thus illustrating the reversibility in vitro of IBDV capsid assembly. HT-VP2-466 VLP also packed heterologous DNA by non-specific confinement during assembly. These and previous results establish the bases for biotechnological applications based on the IBDV capsid and its ability to incorporate exogenous proteins and nucleic acids.
has issue date	2017-12-13(xsd:dateTime)
bibo:doi	10.1088/1361-648x/aa96ec
bibo:pmid	29083994
has license	no-cc
sha1sum (hex)	deb16146b53f1a1ef2755f819c1aec785f98649b
schema:url	https://doi.org/10.1088/1361-648x/aa96ec
resource representing a document's title	Assembly/disassembly of a complex icosahedral virus to incorporate heterologous nucleic acids
has PubMed Central identifier	PMC7103166
has PubMed identifier	29083994
schema:publication	J Phys Condens Matter
resource representing a document's body	covid:deb16146b53f1a1ef2755f819c1aec785f98649b#body_text
is schema:about of	named entity 'empty' named entity 'protein' named entity 'basic' named entity 'complexes' named entity 'DNA' »more»

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