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PMID: 6261259 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

The structural polypeptides of aphthovirus are phosphoproteins.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 12 ·1980-12-00 ·Pages 7444-7

La Torre JL, Grubman MJ, Baxt B, Bachrach HL

Abstract

Analysis of aphthovirus A12, strain 119ab, grown in the presence of inorganic 32P revealed that two of the major viral polypeptides, VP4 and trypsin-sensitive protein VP3, were highly phosphorylated. The other major polypeptides, VP1 and VP2, were also phosphorylated but to a much lesser extent. Polypeptides VP0 and P56, of which there are approximately one of two copies per aphthovirion, were also labeled with 32P. Phosphoserine and phosphothreonine appeared to be the amino acids labeled with 32P.

MeSH Terms
Aphthovirus/analysis Isoelectric Point Phosphoproteins/analysis Serine/analysis Threonine/analysis Viral Proteins/analysis
Chemicals
Phosphoproteins Viral Proteins Threonine Serine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
La Torre J L
Grubman M J
Baxt B
Bachrach H L
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22 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.77.12.7444
Published
1980-12-00
Pages
7444-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC350520
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.77.12.7444 PMC Full Text View journal details
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