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N-terminal amino acid sequences in the major capsid proteins of foot-and-mouth disease virus types A, O, and C
- Source :
- Journal of Virology. 16:1248-1253
- Publication Year :
- 1975
- Publisher :
- American Society for Microbiology, 1975.
-
Abstract
- Sequences of amino acids at the N-termini of virus proteins VP1, VP2, and VP3 were determined for foot-and-mouth disease virus types A12 strain 119, O1Brugge and C3Resende. In the polyacrylamide gel electrophoresis system used to purify the proteins, VP3 migrated faster than VP1 or VP2; and in the virion, VP3 could be cleaved by trypsin into VP3a and VP3b. The N-terminal amino acids for each of the virus types were glycine in VP1, aspartic acid in VP2, and threonine in VP3. No divergences in sequence across the virus types were indicated until at least the fourth position in VP1, and the third in VP3. For virus types A12, O1 and C3, the sequences were, respectively: for VP1 (Gly-ile-phe,pro,val---), (Gly,ile,phe---) and Gly-ile-phe,ala---); for VP2 (Asp,X,met---), (Asp---) and Asp-leu---); and for VP3 (Thr-thr-ala-thr---), (Thr-thr-ser---) and (Thr-thr---). Unresolved mixtures of VP3a and VP3b, from either A12 or O1 viruses, appeared to have the N-terminal amino acids threonine, which is presumed to be the same threonine as in uncleaved VP3 and serine, which is generated by the tryptic cleavage.
- Subjects :
- Threonine
viruses
Immunology
Glycine
Biology
Microbiology
Serine
Leucyl Aminopeptidase
Viral Proteins
Aphthovirus
Virology
Aspartic acid
medicine
Amino Acid Sequence
Amino Acids
Serotyping
Polyacrylamide gel electrophoresis
Amino acid synthesis
Dansyl Compounds
chemistry.chemical_classification
Aspartic Acid
virus diseases
biochemical phenomena, metabolism, and nutrition
Trypsin
Molecular biology
Amino acid
Biochemistry
chemistry
Insect Science
Asparagine
Research Article
medicine.drug
Subjects
Details
- ISSN :
- 10985514 and 0022538X
- Volume :
- 16
- Database :
- OpenAIRE
- Journal :
- Journal of Virology
- Accession number :
- edsair.doi.dedup.....113f9176b2612c4712d3af64b884c609
- Full Text :
- https://doi.org/10.1128/jvi.16.5.1248-1253.1975