ORBi: Espion D. - Expression At The Cell-Surface Of Native Fusion Protein Of The Newcastle-Disease Virus (Ndv) Strain Italien From Cloned Cdna

Reference : Expression At The Cell-Surface Of Native Fusion Protein Of The Newcastle-Disease Virus (...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/34893

Title :	Expression At The Cell-Surface Of Native Fusion Protein Of The Newcastle-Disease Virus (Ndv) Strain Italien From Cloned Cdna
Language :	English
Author, co-author :	Espion, D. [> > > >]
	Dehenau, S. [> > > >]
	Letellier, C. [> > > >]
	Wemers, Cd. [> > > >]
	Brasseur, Robert [Université Libre de Bruxelles - ULB > > Laboratoire Chimie-Physique des Macromolecules aux Interfaces > >]
	Young, Jf. [> > > >]
	Gross, M. [> > > >]
	Rosenberg, M. [> > > >]
	Meulemans, G. [> > > >]
	Burny, A. [> > > >]
Publication date :	1987
Journal title :	Archives of Virology
Volume :	95
Issue/season :	1-2
Pages :	79-95
Audience :	International
ISSN :	0304-8608
Abstract :	[en] A cDNA library was constructed with poly(A)+-mRNAs from NDV-Italien infected BHK-21 cells. A clone, that hybridized to the F gene mRNA, was sequenced. A long open reading frame encodes for a protein of 553 amino acids, with a calculated molecular weight of 59,153, consisting of twelve cysteine residues and six potential glycosylation sites. The protein sequence contains a hydrophobic region at the N-terminus of F1 and a presumptive long transmembrane fragment near the C-terminus. Comparison of the F proteins from NDV strains Italien and Australia-Victoria shows that the sequences are very similar, with conservation of most cysteine residues and of the potential glycosylation sites. The F coding sequence was inserted into the genome of vaccinia virus under the control of vaccinia P7.5 transcriptional regulatory sequences. Expression of F protein was demonstrated by indirect immunofluorescence with five anti-F monoclonal antibodies known to react with conformational epitopes.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/34893
Other URL :	http://www.ncbi.nlm.nih.gov/pubmed/3592986

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