Linked Life Data

9820150

Source:http://linkedlifedata.com/resource/pubmed/id/9820150

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-12-7
pubmed:abstractText
A fraction of the large surface protein (L) of duck hepatitis B virus (DHBV) is phosphorylated at serine or threonine residues (E. Grgacic & D. Anderson, Journal of Virology 68, 7344-7350, 1994). We now report the identification of phosphorylation sites in DHBV L protein. Using site-directed mutagenesis, we have identified serine-118 (S118) as the major phosphorylation site, accepting approximately 64% of the total phosphate groups incorporated in L, and resulting in retarded migration of phosphorylated L in SDS-PAGE. Proline-119 is indispensable for S118 phosphorylation. Mutation of other serine/threonine residues which are followed by prolines (T79, T89, S117 and T155) together with S118 further reduced phosphorylation to around 19% of wild-type. Non-equilibrium pH gel electrophoresis (NEPHGE) and SDS-PAGE of 33P-labelled L protein revealed two phosphorylated L species, while protein with the S118 to alanine mutation was detected as only one labelled species, consistent with multiple phosphorylations in wild-type L. Together, these results demonstrate that serine 118 is the major phosphorylation site for a proline-directed kinase, and that a proportion of L molecules are additionally phosphorylated at one of a number of secondary sites. DHBV mutants encoding L proteins with minimal phosphorylation (alanine mutants) or mimicking constitutive phosphorylation (aspartic acid mutants) remained infectious both in cell culture and in ducks, demonstrating that L phosphorylation may play only a minor role in DHBV replication.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
79 ( Pt 11)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2743-51
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Normal phosphorylation of duck hepatitis B virus L protein is dispensable for infectivity.
pubmed:affiliation
Hepatitis Research Unit, Macfarlane Burnet Centre for Medical Research, Fairfield, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't