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Structural comparison of two strains of foot-and-mouth disease virus subtype O1 and a laboratory antigenic variant, G67

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dc.contributor.advisor Abu Ghazaleh, Robin
dc.contributor.author Lea, Susan
dc.contributor.author Abu Ghazaleh, Robin
dc.contributor.author Blakemore, Wendy
dc.contributor.author Curry, Stephen
dc.contributor.author Fry, Elizabeth
dc.contributor.author Jackson, Terry
dc.contributor.author King, Andrew
dc.contributor.author Logan, Derek
dc.contributor.author Newman, John
dc.contributor.author Stuart, David
dc.date.accessioned 2022-01-18T11:44:48Z
dc.date.accessioned 2022-05-22T08:56:31Z
dc.date.available 2022-01-18T11:44:48Z
dc.date.available 2022-05-22T08:56:31Z
dc.date.issued 1995-06-30
dc.identifier.other https://doi.org/10.1016/S0969-2126(01)00191-5
dc.identifier.uri http://localhost:8080/xmlui/handle/123456789/8421
dc.description.abstract Background: Foot-and-mouth disease viruses (FMDVs) are members of the picornavirus family and cause an economically important disease of cloven-hoofed animals. To understand the structural basis of antigenic variation in FMDV, we have determined the structures of two viruses closely related to strain O1BFS whose structure is known. Results The two new structures are, like O1BFS, both serotype O viruses. The first, O1 Kaüfbeuren (O1K), is a field isolate dating from an outbreak of FMD in Europe in the 1960s. The second, called G67, is a quadruple mutant of O1K, generated in the laboratory, that bears point mutations conferring resistance to neutralization by monoclonal antibodies, specific for each of the four major antigenic sites defined previously. The availability of the three related virus structures permits a detailed analysis of the way amino acid substitutions influence antigenicity. Structural changes are seen to be limited, in general, to the substituted side chain. For example, the GH loop of VP1, a highly antigenic and mobile protuberance which becomes ordered only under reducing conditions, was essentially indistinguishable in the three viruses despite the accumulation of up to four changes within its 15-residue sequence. At one of the other antigenic sites, however, changes between the two field strains did perturb both side-chain and main-chain structures in the vicinity. Conclusion The conservation of conformation of the GH loop of VP1 adds to the evidence implicating an integrin as the cellular receptor for FMDV, since this loop contains a conserved RGD (Arg-Gly-Asp) sequence structurally similar to the same tripeptide in some other integrin-binding proteins. Structural changes required for the virus to escape neutralization by monoclonal antibodies are generally small. The more extensive type of structural change exhibited by the field isolates probably reflects differing selective pressures operating in vivo and in vitro. en_US
dc.publisher Cell Press en_US
dc.subject antigenicity, evolutionary strategies, foot-and-mouth disease virus, picornavirus structure en_US
dc.title Structural comparison of two strains of foot-and-mouth disease virus subtype O1 and a laboratory antigenic variant, G67 en_US
dc.type Article en_US


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