title: Expression at the cell surface of native fusion protein of the Newcastle disease virus (NDV) strain Italien from cloned cDNA.
abstract: 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.
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003062:Codon; D004247:DNA / Q000032:analysis* / Q000302:isolation & purification; D006031:Glycosylation; D009522:Newcastle disease virus / Q000032:analysis*; D014616:Vaccinia virus / Q000235:genetics; D014760:Viral Fusion Proteins / Q000032:analysis* / Q000235:genetics
chemical_list: D003062:Codon; D014760:Viral Fusion Proteins; D004247:DNA