The solution conformational features of two highly homologous antigenic peptides of foot-and-mouth disease virus serotype A, variants A and USA, correlate with their serological properties

Journal of Peptide Science

Volumn 2, Issue 2, 1996, Pages 91-105

  Pegna, Monica ^a,b   Molinari, Henriette ^b,c   Zetta, Lucia ^b   Melacini, G ^b,g   Gibbons, William A ^d   Brown, Fred ^e   Rowlands, Dave ^f   Chan, E ^a   Mascagni, Paolo ^a  

^a Italfarmaco SpA   (Italy)

^b CNR   (Italy)

^c UNIVERSITY OF VERONA   (Italy)

^d UNIVERSITY OF LONDON   (United Kingdom)

^e PLUM ISLAND ANIMAL DISEASE CENTER   (United States)

^f Department of Molecular Sciences   (United Kingdom)

^g UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

FMDV; NMR spectroscopy; NOE constraints; RGD (Arg Gly Aasp); Structure activity correlation

Indexed keywords

FOOT-AND-MOUTH DISEASE VIRUS;

ARGINYL-GLYCYL-ASPARTIC ACID; ARGINYLGLYCYLASPARTIC ACID; OLIGOPEPTIDE; PEPTIDE FRAGMENT; VIRUS ENVELOPE PROTEIN;

AMINO ACID SEQUENCE; APHTHOVIRUS; ARTICLE; CHEMISTRY; CLASSIFICATION; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SEROTYPING; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; APHTHOVIRUS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SEROTYPING; STRUCTURE-ACTIVITY RELATIONSHIP; VIRAL ENVELOPE PROTEINS;

EID: 0030089408     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(199603)2:2<91::AID-PSC50>3.0.CO;2-M     Document Type: Article

References (26)

1. D. J. Rowlands, B. E. Clark, A. R. Carrol, F. Brown, B. H. Nicholson, J. L. Bittle, R. A. Houghten and R. A. Lerner (1983). Chemical basis of antigenic variation in foot-and-mouth disease virus. Nature, 306, 694-697.
2. G. Siligardi, A. F. Drake, P. Mascagni, D. Rowlands, F. Brown and W. A. Gibbons (1991). A CD strategy for the study of polypeptide folding/unfolding. A synthetic foot-and-mouth disease virus immunogenlc peptide. Int. J Peptide Protein Res., 38, 519-527.
3. G. Siligardi, A. F. Drake, P. Mascagni, D. Rowlands, F. Brown and W. A. Gibbons (1991). Correlation between the conformations elucidated by CD spectroscopy and the antigenic properties of four peptides of the foot-and-mouth disease virus. Eur. J. Biochem., 199, 545-551.
4. 1H NMR spectra of proteins. Biochemistry, 29, 1829-1834.
5. A. Bax, M. Ikura, L. E. Kay, D. E. Torchla and R. Tschudin (1990). Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins. J. Magn. Reson., 86, 304-309.
6. H. Molinari, G. Esposito, R. Consonni, M. Pegna and L. Zetta (1992). Distance evaluation via heteronuclear SQC-NOESY experiments. J. Biomol. NMR, 289-299.
7. K. Wuethrich: NMR of Proteins and Nucleic Acids, Wiley, New York 1986.
8. 1H spin system identification in macromolecules. J. Am. Chem. Soc., 110, 7870-7872.
9. S. Macura and R. R. Ernst (1980). Elucidation of cross relaxation in liquids by two-dimensional NMR. Mol. Phys., 41, 95-117.
10. D. Neuhaus and M. Williamson: The Nuclear Overhauser Effect in Structural and Conformational Analysis, VCH, New York 1989.
11. E. T. Olejniczak, R. T. Gambe Jr and S. w. Fesik (1986). Accounting for spin diffusion in the analysis of 2D NOE data. J. Magn. Reson., 67, 28-32.
12. G. Esposito and A. Pastore (1988). An alternative method for distance evaluation from NOESY spectra. J. Magn. Reson., 76, 331-336.
13. G. C. Johnson Jr, T. G. Pagano, C. T. Basson, J. A. Madri, P. Gooley and I. M. Armitage (1993). Biologically active Arg-Gly-Asp oligopeptides assume a type II β-turn in solution. Biochemistry, 32, 268-273.
14. M. C. Vega, C. Aleman, E. Giralt and J. J. Perez (1992). Conformational study of a nine residue fragment of the antigenic loop of foot-and-mouth disease virus. J. Biomol. Struct. Dynamics, 10, 1-8.
15. G. D. Rose, L. M. Gierasch and J. A. Smith (1985). Turns in peptides and proteins. Adv. Protein Chem., 37, 1-109.
16. T. F. Havel, J. D. Kuntz and G. M. Crippen (1983). The theory and practice of distance geometry. Bull. Math. Biol 45, 655-720.
17. 1H proximities in solution. Bull. Math. Biol., 46, 673-698.
18. R. Fletcher and C. M. Reeves (1964). Function minimization by conjugate gradients. Comput. J., 7, 149-167.
19. W. Braun (1987). Distance geometry and related methods for protein structure determination from NMR data. Q. Rev. Biophys., 19, 115-157.
20. 1H nuclear magnetic resonance and restrained molecular dynamics. J. Mol. Biol., 186, 435-455.
21. R. Kaptein, E. R. P. Zuiderberg, R. M. Scheek, R. Boelens and W. F. van Gunsteren (1985). A protein structure from nuclear magnetic resonance data of lac repressor headpiece. J. Mol. Biol., 182, 179-182.
22. J. de Vlieg, R. M. Scheek, W. F. van Gunsteren, H. J. C. Berendsen, R. Kaptein and J. Thomason (1988). Combined procedure of distance geometry and restrained molecular dynamics techniques for protein structure determination from nuclear magnetic resonance data: application to the DNA binding domain of lac repressor from Escherichia coli. Proteins: Struct. Funct. Genet., 3, 209-218.
23. C. R. Cantor and P. R. Schimmel: Biophysical Chemistry. Part I: The Conformation of Biological Macromolecules, W. H. Freeman, New York 1980.
24. E. N. Baker and R. E. Hubbard (1984). Hydrogen bonding in globular proteins. Prog. Biophys. Mol. Biol., 44, 97-179.
25. E. T. Harper and G. D. Rose (1993). Helix stop signals in proteins and peptides: the capping box. Biochemistry, 32, 7605-7609.
26. G. Fox, N. R. 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, 625-637.