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The nucleotide sequence of cDNA coding for the structural proteins of foot-and-mouth disease virus
Authors:J C Boothroyd  T J Harris  D J Rowlands  P A Lowe
Affiliation:1. Department of Immunochemistry, Wellcome Research Laboratories, Langley Court, Beckenham, Kent BR3 3BS, U.K.;1. Department of Biochemistry, Animal Virus Research Institute, Pirbright, Woking, Surrey GU24 ONF U.K.
Abstract: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.
Keywords:cDNA  DNA complementary to viral RNA  FMDV  foot-and-mouth disease virus  kb  kilobasesor kilobase pairs  SDS  sodium dodecyl sulfate  VP  viral protein
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