Structural studies on foot-and-mouth disease virusReportar como inadecuado




Structural studies on foot-and-mouth disease virus - Descarga este documento en PDF. Documentación en PDF para descargar gratis. Disponible también para leer online.

Reference: Lea, Susan Mary., (1993). Structural studies on foot-and-mouth disease virus. Dphil. University of Oxford.Citable link to this page:

 

Structural studies on foot-and-mouth disease virus

Abstract: Foot-and-mouth disease viruses (FMDVs) constitute the aphthovirus genus of thePicornaviridae. The structures of Oi subtype viruses OiK and G67 have been solvedand comparisons reveal the structural basis of monoclonal antibody escape mutationsin G67. Escape mutations are seen to occur at surface-exposed residues and toprovoke structural changes limited to the altered side chains. Comparisons of thestructures of O1 and O1BFS (Acharya et al., Nature 337, 709-716 (1989)) suggestthat changes occurring 'in-the-field' in response to polyclonal antibody pressure maybe subtly different from mutations produced by monoclonal antibody pressure in vitro.Field mutations are seen to alter less exposed residues and to have more far-reachingstructural effects than the in vitro, monoclonal provoked mutations.Crystals of G67 are seen to be 'intimately twinned', the data possessing extra symmetrydue to a mis-packing of the crystals. A protocol, based on current real-spaceaveraging procedures with a novel constraint imposed, has been used successfully todeconvolute these data. This method might be more generally applied to deconvolutethe wavelength overlaps that occur when using the Laue method.The structures of C-S8cl and mutant SD6-6 have been solved at a resolutionof 3.5Å. These structures enable comparisons between members of different FMDVserotypes to be made for the first time, namely: serotype 0 (O1BFS) and serotypeC (C-S8cl). Flexibility of the Arg-Gly-Asp containing G-H loop of VP1 is seento be amongst the most conserved structural features. This loop is implicated inreceptor binding and possible roles for the observed flexibility are discussed. The CS8clstructure also reveals more detail in previously disordered regions of the capsid,namely: the N-terminal residues of VP2 and potential myristate density under the5-fold axis of the virion.Analysis of structures from the Protein Data Bank reveals different patterns ofamino acid use in proteins involved in the two halves of the immune recognition eventi.e. immunoglobulins and viruses. These patterns seem to be based not only onthe characteristics of the most used amino acids but also on characteristics of thenucleotide codons used to code for them.

Type of Award:Dphil Level of Award:Doctoral Awarding Institution: University of Oxford Notes:The digital copy of this thesis has been made available thanks to the generosity of Dr Leonard Polonsky

Contributors

Stuart, D. I.More by this contributor

RoleSupervisor

 

Dave StuartMore by this contributor

RoleSupervisor

 Bibliographic Details

Issue Date: 1993Identifiers

Urn: uuid:438dc0ae-b899-40fd-84dc-03d3fc1a537f

Source identifier: 603835867 Item Description

Type: Thesis;

Language: eng Subjects: Foot-and-mouth disease virus Tiny URL: td:603835867

Relationships





Autor: Lea, Susan Mary. - institutionUniversity of Oxford facultyLife and Environmental Sciences Division - - - - Contributors Stuart, D

Fuente: https://ora.ox.ac.uk/objects/uuid:438dc0ae-b899-40fd-84dc-03d3fc1a537f



DESCARGAR PDF




Documentos relacionados