Publication Date:
1993-08-27
Description:
One of the three structural glycoproteins of classical swine fever virus (CSFV) is E0, a disulfide-bonded homodimer that induces virus-neutralizing antibodies and occurs in a virion-bound as well as a secreted form. E0 was shown to be similar to a family of fungal and plant ribonucleases. Purified E0 from CSFV-infected cells was a potent ribonuclease specific for uridine and inhibitable by zinc ions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, R -- Unger, G -- Stark, R -- Schneider-Scherzer, E -- Thiel, H J -- New York, N.Y. -- Science. 1993 Aug 27;261(5125):1169-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Faculty of Natural Sciences, University of Innsbruck, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8356450" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Classical swine fever virus/*chemistry/enzymology/genetics
;
Dithiothreitol/pharmacology
;
Hydrogen-Ion Concentration
;
Molecular Sequence Data
;
Oxidation-Reduction
;
RNA, Fungal/metabolism
;
Ribonucleases/*chemistry/isolation & purification/metabolism
;
Sequence Analysis
;
Single-Chain Antibodies
;
Substrate Specificity
;
Temperature
;
Uridine/metabolism
;
Viral Structural Proteins/*chemistry/isolation & purification/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
