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. 1981 Apr 24;9(8):1919–1931. doi: 10.1093/nar/9.8.1919

Nucleotide sequence and corresponding amino acid sequence of the gene for the major antigen of foot and mouth disease virus.

C Kurz, S Forss, H Küpper, K Strohmaier, H Schaller
PMCID: PMC326812  PMID: 6264400

Abstract

A segment of 1160 nucleotides of the FMDV genome has been sequenced using three overlapping fragments of cloned cDNA from FMDV strain O1K. This sequence contains the coding sequence for the viral capsid protein VP1 as shown by its homology to known and newly determined amino acid sequences from this man antigenic polypeptide of the FMDV virion. The structural gene for VP1 comprises 639 nucleotides which specify a sequence of 213 amino acids for the VP1 protein. The coding sequence is not flanked by start and stop codons which is consistent with the mode of biosynthesis of VP1 by post-translational processing of a polyprotein precursor.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adam K. H., Strohmaier K. Isolation of the coat proteins of foot-and-mouth disease virus and analysis of the composition and N-terminal endgroups. Biochem Biophys Res Commun. 1974 Nov 6;61(1):185–192. doi: 10.1016/0006-291x(74)90551-8. [DOI] [PubMed] [Google Scholar]
  2. Bachrach H. L., Moore D. M., McKercher P. D., Polatnick J. Immune and antibody responses to an isolated capsid protein of foot-and-mouth disease virus. J Immunol. 1975 Dec;115(6):1636–1641. [PubMed] [Google Scholar]
  3. Bachrach H. L., Morgan D. O., Moore D. M. Foot-and-mouth disease virus immunogenic capsid protein VPT: N-terminal sequences and immunogenic peptides obtained by CNBr and tryptic cleavages. Intervirology. 1979;12(2):65–72. doi: 10.1159/000149070. [DOI] [PubMed] [Google Scholar]
  4. Bachrach H. L., Swaney J. B., Vande Woude G. F. Isolation of the structural polypeptides of foot-and-mouth disease virus and analysis of their C-terminal sequences. Virology. 1973 Apr;52(2):520–528. doi: 10.1016/0042-6822(73)90347-4. [DOI] [PubMed] [Google Scholar]
  5. Burroughs J. N., Rowlands D. J., Sangar D. V., Talbot P., Brown F. Further evidence for multiple proteins in the foot-and-mouth disease virus particle. J Gen Virol. 1971 Oct;13(1):73–84. doi: 10.1099/0022-1317-13-1-73. [DOI] [PubMed] [Google Scholar]
  6. Clewell D. B., Helinski D. R. Supercoiled circular DNA-protein complex in Escherichia coli: purification and induced conversion to an opern circular DNA form. Proc Natl Acad Sci U S A. 1969 Apr;62(4):1159–1166. doi: 10.1073/pnas.62.4.1159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Doel T. R., Sangar D. V., Rowlands D. J., Brown F. A re-appraisal of the biochemical map of foot-and-mouth disease virus RNA. J Gen Virol. 1978 Nov;41(2):395–404. doi: 10.1099/0022-1317-41-2-395. [DOI] [PubMed] [Google Scholar]
  8. Kitamura N., Wimmer E. Sequence of 1060 3'-terminal nucleotides of poliovirus RNA as determined by a modification of the dideoxynucleotide method. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3196–3200. doi: 10.1073/pnas.77.6.3196. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Küpper H., Keller W., Kurz C., Forss S., Schaller H., Franze R., Strohmaier K., Marquardt O., Zaslavsky V. G., Hofschneider P. H. Cloning of cDNA of major antigen of foot and mouth disease virus and expression in E. coli. Nature. 1981 Feb 12;289(5798):555–559. doi: 10.1038/289555a0. [DOI] [PubMed] [Google Scholar]
  10. La Torre J. L., Grubman M. J., Baxt B., Bachrach H. L. The structural polypeptides of aphthovirus are phosphoproteins. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7444–7447. doi: 10.1073/pnas.77.12.7444. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Laporte J., Grosclaude J., Wantyghem J., Bernard S., Rouzé P. Neutralisation en culture cellulaire du pouvoir infectieuz du virus de la fièvre aphteuse par des sérums provenant de porcs immunisés à l'aide d'une protéine virale purifiée. C R Acad Sci Hebd Seances Acad Sci D. 1973 Jun 18;276(25):3399–3401. [PubMed] [Google Scholar]
  12. Machleidt W., Otto J., Wachter E. Chromatography on microbore columns. Methods Enzymol. 1977;47:210–220. doi: 10.1016/0076-6879(77)47026-5. [DOI] [PubMed] [Google Scholar]
  13. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  14. Roberts R. J., Breitmeyer J. B., Tabachnik N. F., Myers P. A. A second specific endonuclease from Haemophilus aegyptius. J Mol Biol. 1975 Jan 5;91(1):121–123. doi: 10.1016/0022-2836(75)90375-7. [DOI] [PubMed] [Google Scholar]
  15. Sangar D. V. The replication of picornaviruses. J Gen Virol. 1979 Oct;45(1):1–13. doi: 10.1099/0022-1317-45-1-1. [DOI] [PubMed] [Google Scholar]
  16. Sanger F., Coulson A. R. The use of thin acrylamide gels for DNA sequencing. FEBS Lett. 1978 Mar 1;87(1):107–110. doi: 10.1016/0014-5793(78)80145-8. [DOI] [PubMed] [Google Scholar]
  17. Spiro R. G. Glycoproteins. Adv Protein Chem. 1973;27:349–467. doi: 10.1016/s0065-3233(08)60451-9. [DOI] [PubMed] [Google Scholar]
  18. Strohmaier K., Adam K. H. Comparative electrophoretic studies of foot-and-mouth disease virus proteins. J Gen Virol. 1974 Jan;22(1):105–114. doi: 10.1099/0022-1317-22-1-105. [DOI] [PubMed] [Google Scholar]
  19. Strohmaier K. The N-terminal sequence of three coat proteins of foot-and-mouth disease virus. Biochem Biophys Res Commun. 1978 Dec 29;85(4):1640–1645. doi: 10.1016/0006-291x(78)91191-9. [DOI] [PubMed] [Google Scholar]
  20. Subak-Sharpe H., Bürk R. R., Crawford L. V., Morrison J. M., Hay J., Keir H. M. An approach to evolutionary relationships of mammalian DNA viruses through analysis of the pattern of nearest neighbor base sequences. Cold Spring Harb Symp Quant Biol. 1966;31:737–748. doi: 10.1101/sqb.1966.031.01.094. [DOI] [PubMed] [Google Scholar]
  21. Vande Woude G. F., Bachrach H. L. Number and molecular weights of foot-and-mouth disease virus capsid proteins and the effects of maleylation. J Virol. 1971 Feb;7(2):250–259. doi: 10.1128/jvi.7.2.250-259.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Villa-Komaroff L., Efstratiadis A., Broome S., Lomedico P., Tizard R., Naber S. P., Chick W. L., Gilbert W. A bacterial clone synthesizing proinsulin. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3727–3731. doi: 10.1073/pnas.75.8.3727. [DOI] [PMC free article] [PubMed] [Google Scholar]

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