## Abstract Potential energy surfaces of the model peptide HCO‐L‐Ala‐NH~2~ were calculated using polarizable continuum model (PCM) for the description of aqueous solution at RHF/3‐21G, RHF/6‐31+G(d), and B3LYP/6‐31+G(d) levels of theory. Energy minima were optimized at all three levels as well as a
Sindbis virus as a model for studies of conformational changes in a metastable virus and the role of conformational changes in in vitro antibody neutralisation
✍ Scribed by Raquel Hernandez; Angel Paredes
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 423 KB
- Volume
- 19
- Category
- Article
- ISSN
- 1052-9276
- DOI
- 10.1002/rmv.619
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✦ Synopsis
Abstract
Sindbis virus has long been the prototypical alphavirus used in the study of assembly of icosahedral viruses which contain membranes. Much is known about the assembly pathway and molecular architecture of this virus, and models of mechanisms of infection and release of the viral RNA have been proposed. This review will focus on the structural aspects of in vitro antibody neutralisation of a metastable alphavirus, Sindbis virus, which results from antibody induced conformational changes. For the alphaviruses, structures of in vitro antibody induced conformational neutralisation for Sindbis virus, and receptor occlusion for Sindbis and Ross River virus (RRV) have been reported. A model is presented which could extend the mechanism of antibody induced conformational neutralisation to any metastable virus structure. Copyright © 2009 John Wiley & Sons, Ltd.
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