作者: N Elango , J E Coligan , R C Jambou , S Venkatesan
DOI: 10.1128/JVI.57.2.481-489.1986
关键词: Neuraminidase 、 HN Protein 、 Signal peptide 、 Peptide sequence 、 Biology 、 Sendai virus 、 Protein sequencing 、 Biochemistry 、 Molecular biology 、 Amino acid 、 Nucleic acid sequence
摘要: The nucleotide sequence of mRNA for the hemagglutinin-neuraminidase (HN) protein human parainfluenza type 3 virus obtained from corresponding cDNA clone had a single long open reading frame encoding putative 64,254 daltons consisting 572 amino acids. deduced was confirmed by limited N-terminal acid microsequencing CNBr cleavage fragments native HN that purified immunoprecipitation. is moderately hydrophobic and has four potential sites (Asn-X-Ser/Thr) N-glycosylation in C-terminal half molecule. It devoid both signal membrane anchorage domain characteristic hemagglutinin influenza fusion (F0) paramyxoviruses. Instead, it prominent region capable insertion beginning at 32 residues N terminus. This similar to neuraminidase recently reported structures proteins Sendai simian 5.