About: Virus‐Like Particles: Models for Assembly Studies and Foreign Epitope Carriers

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Virus‐Like Particles: Models for Assembly Studies and Foreign Epitope Carriers
Creator	Boguszewska-Ch Achuls Ka, Anna Haenn, Ann E-Lise Mal, Nkar, { Subbarao, Handanahal Um, Mahadevaiah
source	Elsevier; Medline; PMC
abstract	Publisher Summary Virus‐like particles (VLPs), formed by the structural elements of viruses, have received considerable attention over the past two decades. The number of reports on newly obtained VLPs has grown proportionally with the systems developed for the expression of these particles. The chapter outlines the recent achievements in two important fields of research brought about by the availability of VLPs produced in a foreign host. These are: (1) The requirements for VLP assembly and (2) the use of VLPs as carriers for foreign epitopes. VLP technology is a rapidly advancing domain of molecular and structural biology. Extensive progress in VLP studies was achieved as the insect cell based protein production system was developed. This baculovirus expression system has many advantages for the synthesis of viral structural proteins resulting in the formation of VLPs. It allows production of large amounts of correctly folded proteins while also providing cell membranes that can serve as structural elements for enveloped viruses. These features give us the opportunity to gain insights into the interactions and requirements accompanying VLP formation that are similar to the assembly events occurring in mammalian cells. Other encouraging elements are the ability to easily scale up the system and the simplicity of purification of the assembled VLPs. The growing number of VLPs carrying foreign protein fragments on their surface and studies on the successful assembly of these chimeric molecules is a promising avenue towards the development of a new technology, in which the newly designed VLPs will be directed to particular mammalian cell types by exposing specific binding domains. The progress made in modeling the surface of VLPs makes them to date the best candidates for the design of delivery systems that can efficiently reach their targets.
has issue date	2005-12-31(xsd:dateTime)
bibo:doi	10.1016/s0079-6603(05)80004-2
bibo:pmid	16164974
has license	els-covid
sha1sum (hex)	794906ba7f4f57e267f5b6af538f42a7c783d039
schema:url	https://doi.org/10.1016/s0079-6603%2805%2980004-2
resource representing a document's title	Virus‐Like Particles: Models for Assembly Studies and Foreign Epitope Carriers
has PubMed Central identifier	PMC7119358
has PubMed identifier	16164974
schema:publication	Progress in Nucleic Acid Research and Molecular Biology
resource representing a document's body	covid:794906ba7f4f57e267f5b6af538f42a7c783d039#body_text
is schema:about of	named entity 'Epitope' named entity 'FOREIGN' named entity 'ADR' named entity 'CARRIERS' named entity 'ASSEMBLY' named entity 'STUDIES' named entity 'VIRUS-LIKE PARTICLES' named entity 'MODELS' named entity 'SKA' named entity 'EPITOPE' named entity 'E. coli' named entity 'Sindbis' named entity 'capsid protein' named entity 'mammalian cells' named entity 'structural biology' named entity 'SINV' named entity 'icosahedral' named entity 'retrovirus' named entity 'protein' named entity 'immunoblotting' named entity 'Antigenic' named entity 'mammalian cells' named entity 'yeast' named entity 'immunogenicity' named entity 'Alfalfa mosaic virus' named entity 'myristoylation' named entity 'VLPs' named entity 'VLPs' named entity 'dimerization' named entity 'protein' named entity 'RNA' named entity 'nucleic acids' named entity 'heterologous' named entity 'scaffolding protein' named entity 'VP1' named entity 'mutation' named entity 'vaccine' named entity 'VLPs' named entity 'VLPs' named entity 'coat proteins' named entity 'Gag protein' named entity 'cell type' named entity 'VLP' named entity 'paracrystalline' named entity 'cadmium' named entity 'VP3' named entity 'Clostridium difficile toxin A' named entity 'virion' named entity 'JC polyomavirus' named entity 'cleavage' named entity 'VLPs' named entity 'VLPs' named entity 'VLPs' named entity 'capsid' named entity 'VLPs' named entity 'insect' named entity 'VLPs' named entity 'VLPs' named entity 'amino acid residues' named entity 'budding process' named entity '19, 20' named entity 'cell membranes' named entity 'RSV' named entity 'point mutation' named entity 'mammalian cells' named entity 'viral proteins' named entity 'transgenic' named entity 'VLP' named entity 'HBV' named entity 'glycoproteins' named entity 'heterologous' named entity 'icosahedral symmetry' named entity 'Coronaviridae' named entity 'C-terminal' named entity 'VP1' named entity 'VP3'

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