Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-7-31
pubmed:databankReference
pubmed:abstractText
In Marek's disease virus (MDV) serotype 2 (MDV2) genome, a gene equivalent to the glycoprotein E (gE) of other alphaherpesviruses was identified and sequenced. The primary translation product comprises 488 amino acids with a M(r) of 54.3 kDa. The predicted amino acid sequence possesses several characteristics typical of membrane glycoproteins, including a N-terminal hydrophobic signal sequence, C-terminal transmembrane and cytoplasmic domains, and extra-cellular region containing four potential N-linked glycosylation sites. Compared with other MDV serotypes, MDV2 gE showed 47.3% identity with MDV1 gE, and 38.9% identity with HVT gE at the amino acid level. In transcriptional analyses, a 2.0 kb mRNA which starts between 65 and 86 bps upstream of the potential translational initiation codon of gE was identified as the gE-specific transcript. By a recombinant baculovirus, this potential gE coding region was expressed as several specific products from 66 to 72 kDa. These products were susceptible to tunicamycin treatment, indicating that they were glycoprotein in nature. Further, the expressed gE reacted with all chicken-antisera raised to each of the three serotypes of MDV (strains GA, SB-1, and FC126), suggesting that gE is expressed by all three serotypes of MDV in infected cells and conserves common antigenic epitope(s) beyond those that are serotype specific.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0168-1702
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Characterization and expression of the Marek's disease virus serotype 2 glycoprotein E in recombinant baculovirus-infected cells: initial analysis of its DNA sequence and antigenic properties.
pubmed:affiliation
Department of Veterinary Microbiology, Faculty of Agriculture, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't