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Phosphorylation of the budgerigar fledgling disease virus major capsid protein VP1The structural proteins of the budgerigar fledgling disease virus, the first known nonmammalian polyomavirus, were analyzed by isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The major capsid protein VP1 was found to be composed of at least five distinct species having isoelectric points ranging from pH 6.45 to 5.85. By analogy with the murine polyomavirus, these species apparently result from different modifications of an initial translation product. Primary chicken embryo cells were infected in the presence of 32Pi to determine whether the virus structural proteins were modified by phosphorylation. SDS-PAGE of the purified virus structural proteins demonstrated that VP1 (along with both minor capsid proteins) was phosphorylated. Two-dimensional analysis of the radiolabeled virus showed phosphorylation of only the two most acidic isoelectric species of VP1, indicating that this posttranslational modification contributes to VP1 species heterogeneity. Phosphoamino acid analysis of 32P-labeled VP1 revealed that phosphoserine is the only phosphoamino acid present in the VP1 protein.
Document ID
20050000661
Document Type
Reprint (Version printed in journal)
Authors
Haynes, J. I. 2nd (Kansas State University Manhattan 66506-4901)
Consigli, R. A.
Spooner, B. S.
Date Acquired
August 22, 2013
Publication Date
July 1, 1992
Publication Information
Publication: Journal of virology
Volume: 66
Issue: 7
ISSN: 0022-538X
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: CA07319
CONTRACT_GRANT: CA09418
Distribution Limits
Public
Copyright
Other
Keywords
Non-NASA Center
NASA Discipline Cell Biology