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The nucleotide sequence of cDNA coding for the structural proteins of foot-and-mouth disease virus.
The complete nucleotide sequence of cDNA coding for the structural capsid polypeptides of foot-and-mouth disease virus (FMDV) (strain A(10)61) has been determined. Portions of the flanking sequence coding for the nonstructural proteins p20a and p52 are also provided. The three larger structural polypeptides VP1, VP2 and VP3 have unmodified Mrs of 23248, 24649 and 24213, respectively. The size of the smaller polypeptide, VP4, can only be estimated at 7360 because the 5'-limit of its coding region is not yet known with certainty. The sequence data for VP1 (the major immunising antigen) and the amino-terminal quarter of p52 are compared with the data of Kurz et al. (Nucl. Acids Res. 9 (1981) 1919-1931) for a different serotype (O1K). This shows that variation is much greater in the region coding for VP1 than in that coding for p52. This is reflected in the level of amino acid sequence variation predicted for the two proteins. Analysis of relative codon usage reveals a strong bias in favour of C and G over U and A in the third base position. The dinucleotide frequencies show a bias against A-U and U-A, and for A-C and C-A.
PMID: 6282711 [PubMed - indexed for MEDLINE]
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Cited by 17 PubMed Central articles
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Homologous sequences in non-structural proteins from cowpea mosaic virus and picornaviruses.
Franssen H, Leunissen J, Goldbach R, Lomonossoff G, Zimmern D.
EMBO J. 1984 Apr; 3(4):855-861.
[EMBO J. 1984]
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Primary structure and gene organization of the middle-component RNA of cowpea mosaic virus.
van Wezenbeek P, Verver J, Harmsen J, Vos P, van Kammen A.
EMBO J. 1983; 2(6):941-6.
[EMBO J. 1983]
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The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region.
Palmenberg AC, Kirby EM, Janda MR, Drake NL, Duke GM, Potratz KF, Collett MS.
Nucleic Acids Res. 1984 Mar 26; 12(6):2969-85.
[Nucleic Acids Res. 1984]
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