The structural polypeptides of aphthovirus are phosphoproteins

Analysis of aphthovirus A12, strain 119ab, grown in the presence of inorganic32P revealed that two of the major viral polypeptides, VP4and trypsin-sensitive protein VP3, were highly phosphorylated. The other major polypeptides, VP1and VP2, were also phosphorylated but to a much lesser extent. Polype...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1980-12, Vol.77 (12), p.7444-7447
Hauptverfasser:	La Torre, J.L. (ARS, USDA, Greenport, NY), Grubman, M.J, Baxt, B, Bachrach, H.L
Format:	Artikel
Sprache:	eng
Schlagworte:	ACIDE AMINE AMINO ACIDS AMINOACIDOS APHTHOVIRUS Aphthovirus - analysis ELECTROFORESIS ELECTROPHORESE ELECTROPHORESIS FOSFOPROTEINAS FOSFORILACION Gels HAMSTER HAMSTERS Isoelectric Point Kidney cells PEPTIDE PEPTIDES PEPTIDOS PHOSPHOPROTEINE PHOSPHOPROTEINS Phosphoproteins - analysis PHOSPHORYLATION Picornaviridae Radioactive decay RNA Serine - analysis Threonine - analysis Viral Proteins - analysis Virions Virology VIRUS FIEBRE AFTOSA VIRUS FIEVRE APHTEUSE Viruses
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Zusammenfassung:	Analysis of aphthovirus A12, strain 119ab, grown in the presence of inorganic32P revealed that two of the major viral polypeptides, VP4and trypsin-sensitive protein VP3, were highly phosphorylated. The other major polypeptides, VP1and VP2, were also phosphorylated but to a much lesser extent. Polypeptides VP0and P56, of which there are approximately one or two copies per aphthovirion, were also labeled with32P. Phosphoserine and phosphothreonine appeared to be the amino acids labeled with32P.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.77.12.7444