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Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines

The past decade has witnessed the development of numerous systems for the presentation of antigens on the surface of self-assembling macromolecules. Although the sites for insertion were initially chosen empirically, the determination of the three-dimensional structures of a number of carrier macrom...

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Detalles Bibliográficos
Autores principales: Lomonossoff, George P, Johnson, John E
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Ltd. 1996
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7133382/
https://www.ncbi.nlm.nih.gov/pubmed/8728650
http://dx.doi.org/10.1016/S0959-440X(96)80072-8
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author Lomonossoff, George P
Johnson, John E
author_facet Lomonossoff, George P
Johnson, John E
author_sort Lomonossoff, George P
collection PubMed
description The past decade has witnessed the development of numerous systems for the presentation of antigens on the surface of self-assembling macromolecules. Although the sites for insertion were initially chosen empirically, the determination of the three-dimensional structures of a number of carrier macromolecules has enabled structure-based insertional mutagenesis to be used increasingly. Furthermore, it is now feasible to determine the structure of an inserted sequence as presented in a heterologous environment, making it possible to correlate the detailed structure of a peptide with its immunological properties.
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spelling pubmed-71333822020-04-08 Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines Lomonossoff, George P Johnson, John E Curr Opin Struct Biol Article The past decade has witnessed the development of numerous systems for the presentation of antigens on the surface of self-assembling macromolecules. Although the sites for insertion were initially chosen empirically, the determination of the three-dimensional structures of a number of carrier macromolecules has enabled structure-based insertional mutagenesis to be used increasingly. Furthermore, it is now feasible to determine the structure of an inserted sequence as presented in a heterologous environment, making it possible to correlate the detailed structure of a peptide with its immunological properties. Published by Elsevier Ltd. 1996-04 2002-02-11 /pmc/articles/PMC7133382/ /pubmed/8728650 http://dx.doi.org/10.1016/S0959-440X(96)80072-8 Text en Copyright © 1996 Published by Elsevier Ltd. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Lomonossoff, George P
Johnson, John E
Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
title Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
title_full Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
title_fullStr Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
title_full_unstemmed Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
title_short Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
title_sort use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7133382/
https://www.ncbi.nlm.nih.gov/pubmed/8728650
http://dx.doi.org/10.1016/S0959-440X(96)80072-8
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