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Chapter 5 : Antigenic Variation in Foot-and-Mouth Disease Virus

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Antigenic Variation in Foot-and-Mouth Disease Virus, Page 1 of 2

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Abstract:

Antigenic variation in foot-and-mouth disease (FMD) is important for both practical and fundamental reasons. In the first place, it has considerable importance in the control of the disease by vaccination because vaccines providing protection against one of the seven serotypes afford no protection against viruses belonging to the other six serotypes. Equally important, the wide spectrum of antigenic variation within the serotypes provides similar control problems. The second reason is the opportunity that antigenic variation provides for studying the immunochemistry of the virus. It is of particular interest that a major antigenic feature of the virus is coincident with the cell receptor-binding motif. This provides the intriguing challenge of trying to understand how the apparently conflicting requirements of maintaining receptor-binding specificity while allowing antigenic variation to occur in the same structural feature are resolved. The discovery of serotypes stemmed from the observation that animals in the field could become infected on more than one occasion. Cross-resistance analyses involving panels of monoclonal antibodies and panels of resistant viruses are used to map the mutations into nonoverlapping sites. Acquisition of the ability to bind to heparin sulfate at cell surfaces has been seen in foot-and-mouth disease virus (FMDV), as it has in other tissue culture-adapted viruses.

Citation: Rowlands D, Brown F. 2002. Antigenic Variation in Foot-and-Mouth Disease Virus, p 51-58. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch5

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Foot-and-mouth disease virus
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Equine rhinitis A virus
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Figures

Image of FIGURE 1
FIGURE 1

Identification of antigenic determinants on the VP1 protein of FMDV, serotype O1. The abilities of purified intact protein and enzymatically or chemically cleaved fragments to elicit virus-neutralizing antibodies in mice were determined. The precise locations of the cleavage points were ascertained by direct sequencing and comparison with the amino acid sequence predicted from the nucleic acid sequence. The fine location of the sites was deduced by comparing the active and nonactive fragments. Modified from reference .

Citation: Rowlands D, Brown F. 2002. Antigenic Variation in Foot-and-Mouth Disease Virus, p 51-58. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch5
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Image of FIGURE 2
FIGURE 2

Space-filling model of FMDV, serotype O1, showing the location of antibody-selected mutations (indicated in white) that define the antigenic sites. The transparent balloons show the potential space occupancy of the major antigenic site, site 1, associated with the mobile G-H loop of VP1. Arrows indicate the individual antigenic sites. Figure generously supplied by E. Fry and D. Stuart, Oxford, United Kingdom.

Citation: Rowlands D, Brown F. 2002. Antigenic Variation in Foot-and-Mouth Disease Virus, p 51-58. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch5
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Image of FIGURE 3
FIGURE 3

Model of the antigenic site 1 (the VP1 G-H loop) of FMDV, serotype O1, as determined from the crystal structure of reduced virus. The RGD residues that are key components of the receptor-binding properties of the sequence are shown at the bend joining the helical regions of the loop. Figure generously supplied by E. Fry and D. Stuart, Oxford, United Kingdom.

Citation: Rowlands D, Brown F. 2002. Antigenic Variation in Foot-and-Mouth Disease Virus, p 51-58. In Semler B, Wimmer E (ed), Molecular Biology of Picornavirus. ASM Press, Washington, DC. doi: 10.1128/9781555817916.ch5
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References

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