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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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1. Acharya, R.,, E. Fry,, D. Stuart,, G. Fox,, D. Rowlands,, and F. Brown. 1989. The 3-dimensional structure of foot-and-mouth-disease virus at 2.9-A resolution. Nature 337: 709716.
2. Bachrach, H. L.,, D. M. Moore,, P. D. McKercher,, and J. Polatnick. 1975. Immune and antibody responses to an isolated capsid protein of foot and mouth disease virus. J. Immunol. 115:16361641.
3. Baranowski, E.,, C. M. Ruiz-Jarabo,, and E. Domingo. 2001. Evolution of cell recognition by viruses. Science 292:11021105.
4. Baranowski, E.,, C. M. Ruiz-Jarabo,, N. Sevilla,, D. Andreu,, E. Beck,, and E. Domingo. 2000. Cell recognition by foot-and-mouth disease virus that lacks the RGD integrin-binding motif: flexibility in aphthovirus receptor usage. J. Virol. 74:16411647.
5. Baxt, B.,, and Y. Becker. 1990. The effect of peptides containing the arginine-glycine-aspartic acid sequence on the adsorbtion of foot-and-mouth disease virus to tissue culture cells. Virus Genes 4:7383.
6. Baxt, B.,, V. Vakharia,, D. M. Moore,, A. J. Franke,, and D. O. Morgan. 1989. Analysis of neutralizing antigenic sites on the surface of type A12 foot-and-mouth disease virus. J. Virol. 63:21432151.
7. Beck, E.,, G. Feil,, and K. Strohmaier. 1983. The molecular basis of the antigenic variation of foot-and-mouth disease virus. EMBO J. 2:555559.
8. Berinstein, A.,, M. Roivainen,, T. Hovi,, P. Mason,, and B. Baxt. 1995. Antibodies to the vitronectin receptor (intergrin avb3) inhibit binding and infection of foot and mouth disease virus to cultured cells. J. Virol. 69:26642666.
9. Bittie, J. L.,, R. A. Houghten,, H. Alexander,, T. M. Shinnick,, J. G. Sutcliffe,, R. A. Lerner,, D. J. Rowlands,, and F. Brown. 1982. Protection against foot and mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature 298:3033.
10. Brown, F. 1995. Antibody recognition and neutralization of foot-and-mouth disease virus. Semin. Virol. 6:243248.
11. Brown, F.,, and C. J. Smale. 1970. Demonstration of three specific sites on the surface of foot-and-mouth disease virus by antibody complexing. J. Gen. Virol. 7:115127.
12. Crowther, J. R.,, S. Farias,, W. C. Carpenter,, and A. R. Samuel. 1993. Identification of a fifth neutralizable site on type O foot-and-mouth disease virus following characterization of single and quintuple monoclonal antibody escape mutants. J. Gen. Virol. 74(Pt. 8):15471553.
13. Curry, S.,, E. Fry,, W. Blakemore,, R. Abu-Ghazaleh,, T. Jackson,, A. King,, S. Lea,, J. Newman,, D. Rowlands,, and D. Stuart. 1996. Perturbations in the surface structure of A22 Iraq foot-and-mouth disease virus accompanying coupled changes in host cell specificity and antigenicity. Structure 4:135145.
14. Di Marchi, R.,, G. Brooke,, C. Gale,, V. Cracknell,, T. Doel,, and N. Mowat. 1986. Protection of cattle against foot and mouth disease virus by a synthetic peptide. Science 232:639641.
15. Domingo, E.,, N. Verdaguer,, W. F. Ochoa,, C. M. Ruiz-Jarabo,, N. Sevilla,, E. Baranowski,, M. G. Mateu,, and J. Fita. 1999. Biochemical and structural studies with neutralizing antibodies raised against foot-and-mouth disease virus. Virus Res. 62:169175.
16. Dunn, C. S.,, A. R. Samuel,, L. A. Pullen,, and J. Anderson. 1998. The biological relevance of virus neutralisation sites for virulence and vaccine protection in the guinea pig model of foot-and-mouth disease. Virology 247: 5161.
17. Fox, G.,, N. Parry,, P. V. Barnett,, B. McGinn,, D. J. Rowlands,, and F. Brown. 1989. The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid). J. Gen. Virol. 70:625637.
18. Francis, M. J.,, and B. E. Clarke. 1989. Peptide vaccines based on enhanced immunogenicity of peptide epitopes presented with T cell determinants or hepatitis B core protein. Methods Enzymol. 178:659.
19. Haydon, D. T.,, A. D. Bastos,, N. J. Knowles,, and A. R. Samuel. 2001. Evidence for positive selection in foot-and-mouth disease virus capsid genes from field isolates. Genetics 157:715.
20. Hewat, E. A.,, N. Verdaguer,, I. Fita,, W. Blakemore,, S. Brookes,, A. King,, J. Newman,, E. Domingo,, M. G. Mateu,, and D. I. Stuart. 1997. Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop. EMBO J. 16:14921500.
21. Jackson, T.,, D. Sheppard,, M. Denyer,, W. Blakemore,, and A. M. Q. King. 2000. The epithelial integrin avb6 is a receptor for foot-and-mouth disease virus. J. Virol. 74: 49494956.
22. Kitson, J. D.,, D. McCahon,, and G. J. Belsham. 1990. Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus: evidence for the involvement of the three surface exposed capsid proteins in four antigenic sites. Virology 179:2634.
23. Kleid, D. G.,, D. G. Yansura,, B. Small,, D. Dowbenko,, D. Moore,, M. J. Grubman,, P. D. McKercher,, D. O. Morgan,, B. H. Robertson,, and H. L. Bachrach. 1981. Cloned viral protein vaccine for foot and mouth disease; response in cattle and swine. Science 214:11251129.
24. Lea, S.,, J. Hernandez,, W. Blakemore,, E. Brocchi,, S. Curry,, E. Domingo,, E. Fry,, R. Abu-Ghazaleh,, A. King,, J. Newman,, D. Stuart,, and M. G. Mateu. 1994. The structure and antigenicity of a type C foot-and-mouth disease virus. Structure 2:123139.
25. Mason, P.,, E. Rieder,, and B. Baxt. 1994. RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway. Proc. Natl. Acad. Sci. USA 91:19321936.
26. Mason, R. W.,, B. Baxt,, F. Brown,, J. Harber,, A. Murdin,, and E. Wimmer. 1993. Antibody-complexed foot-and-mouth-disease virus, but not poliovirus, can infect normally unsusceptible cells via the Fc receptor. Virology 192: 568577.
27. Mateu, M. G.,, J. A. Camarero,, E. Giralt,, D. Andreu,, and E. Domingo. 1995. Direct evaluation of the immunodominance of a major antigenic site of foot-and-mouth disease virus in a natural host. Virology 206:298306.
28. Mateu, M. G.,, M. L. Valero,, D. Andreu,, and E. Domingo. 1996. Systematic replacement of amino acid residues within an Arg-Gly-Asp-containing loop of foot-and-mouth disease virus and effect on cell recognition. J. Biol. Chem. 271:1281412819.
29. McCahon, D.,, J. R. Crowther,, G. J. Belsham,, J. D. Kitson,, M. Duchesne,, P. Have,, R. H. Meloen,, D. O. Morgan,, and F. De Simone. 1989. Evidence for at least four antigenic sites on type O foot-and-mouth disease virus involved in neutralization; identification by single and multiple site monoclonal antibody-resistant mutants. J. Gen. Virol. 70(Pt. 3):639645.
30. Meloen, R.,, D. J. Rowlands,, and F. Brown. 1979. Comparison of the antibodies elicited by the individual structural polypeptides of foot and mouth disease virus and poliovirus. J. Gen. Virol. 45:761763.
31. Ochoa, W. F.,, S. G. Kalko,, M. G. Mateu,, P. Gomes,, D. Andreu,, E. Domingo,, I. Fita,, and N. Verdaguer. 2000. A multiply substituted G-H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: a role for water molecules. J. Gen. Virol. 81:14951505.
32. Palmenberg, A. C., 1989. Sequence alignments of picornalviral capsid proteins, p. 211241. In B. L. Semler, and E. Ehrenfeld (ed.), Molecular Aspects of Picornavirus Infection and Detection. American Society for Microbiology, Washington, D.C..
33. Parry, N.,, G. Fox,, D. Rowlands,, F. Brown,, E. Fry,, R. Acharya,, D. Logan,, and D. Stuart. 1990. Structural and serological evidence for a novel mechanism of antigenic variation in foot-and-mouth disease virus. Nature 347: 569572.
34. Parry, N. R.,, E. J. Ouldridge,, P. V. Barnett,, B. E. Clarke,, M. J. Francis,, J. D. Fox,, D. J. Rowlands,, and F. Brown. 1989. Serological prospects for peptide vaccines against foot-and-mouth disease virus. J. Gen. Virol. 70(Pt. ll):29192930.
35. Pfaff, E.,, M. Mussgay,, H. O. Bohm,, G. E. Schulz,, and H. Schaller. 1982. Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus. EMBO J. 1:869874.
36. Rieder, E.,, A. Berinstein,, B. Baxt,, A. Kang,, and P. W. Mason. 1996. Propagation of an attenuated virus by design: engineering a novel receptor for a noninfectious foot-and-mouth disease virus. Proc. Natl Acad. Sci. USA 93:1042810433.
37. Rowlands, D. J., 1993. Progress towards peptide vaccines for foot-and-mouth disease, p. 5486. In R. Panday,, S. Hogland,, and G. Prasad (ed.), Veterinary Vaccines. Springer-Verlag, New York, N.Y..
38. Rowlands, D. J.,, B. E. Clarke,, A. R. Carroll,, F. Brown,, B. H. Nicholson,, J. L. Bittie,, R. A. Houghten,, and R. A. Lerner. 1983. Chemical basis of antigenic variation in foot-and-mouth disease virus. Nature 306: 694697.
39. Rowlands, D. J.,, D. V. Sangar,, and F. Brown. 1971. Relationship of the antigenic structure of foot-and-mouth disease virus to the process of infection. J. Gen. Virol. 13: 8593.
40. Sa-Carvalho, D.,, E. Rieder,, B. Baxt,, R. Rodarte,, A. Tanuri,, and P. W. Mason. 1997. Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle. J. Virol. 71:51155123.
41. Saiz, J. C.,, J. Cairo,, M. Medina,, D. Zuidema,, C. Abrams,, G. J. Belsham,, E. Domingo,, and J. M. Vlak. 1994. Unprocessed foot-and-mouth disease virus capsid precursor displays discontinuous epitopes involved in viral neutralization. J. Virol. 68:45574564.
42. Strohmaier, K.,, R. Franze,, and K. H. Adam. 1982. Location and characterization of the antigenic portion of the FMDV immunizing protein. J. Gen. Virol. 59:295306.
43. Taboga, O.,, C. Tami,, E. Carrillo,, J. I. Nunez,, A. Rodriguez,, J. C. Saiz,, E. Blanco,, M. L. Valero,, X. Roig,, J. A. Camarero,, D. Andreu,, M. G. Mateu,, E. Giralt,, E. Domingo,, F. Sobrino,, and E. L. Palma. 1997. A large-scale evaluation of peptide vaccines against foot-and-mouth disease: lack of solid protection in cattle and isolation of escape mutants. J. Virol. 71:26062614.
44. Thomas, A. A.,, R. J. Woortmeijer,, W. Puijk,, and S. J. Barteling. 1988. Antigenic sites on foot-and-mouth disease virus type A10. J. Virol. 62:27822789.
45. Van Regenmortel, M. H.,, G. Guichard,, N. Benkirane,, J. P. Briand,, S. Muller,, and F. Brown. 1998. The potential of retro-inverso peptides as synthetic vaccines. Dev. Biol. Stand. 92:139143.
46. Verdaguer, N.,, M. G. Mateu,, D. Andreu,, E. Giralt,, E. Domingo,, and I. Fita. 1995. Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody: direct involvement of the Arg-Gly-Asp motif in the interaction. EMBO J. 14: 16901696.
47. Verdaguer, N.,, M. G. Mateu,, J. Bravo,, E. Domingo, and 1. Fita. 1996. Induced pocket to accommodate the cell attachment Arg-Gly-Asp motif in a neutralizing antibody against foot-and-mouth-disease vims. J. Mol. Biol. 256: 364376.
48. Wild, T. F.,, and F. Brown. 1967. Nature of the inactivating action of trypsin on foot-and-mouth disease virus. J. Gen. Virol. 1:247250.

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