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Expression at the cell surface of native fusion protein of the Newcastle disease virus (NDV) strain Italien from cloned cDNA

par Espion, Danielle;De Henau, Suzanne;Letellier, Carine;Wemers, Claire-Dominique ;Brasseur, Robert ;Young, J.F.;Gross, Mitchell;Rosenberg, Martin;Meulemans, Georges ;Burny, Arsène
Référence Archives of virology, 95, 1-2, page (79-95)
Publication Publié, 1987-03

Article révisé par les pairs

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Résumé :

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. © 1987 Springer-Verlag.