title: Nucleotide and predicted amino acid sequence analysis of the fusion protein and hemagglutinin-neuraminidase protein genes among Newcastle disease virus isolates. Phylogenetic relationships among the Paramyxovirinae based on attachment glycoprotein sequences.
abstract: Highly virulent Newcastle disease virus (NDV) isolates are List A pathogens for commercial poultry, and reports of their isolation among member nations must be made to the Office of International Epizootes (OIE). The virus is classified as a member of the order Mononegavirales in the family Paramyxoviridae of the subfamily Paramyxovirinae. Two interactive surface glycoproteins, the fusion (F) and hemagglutinin-neuraminidase (HN) proteins, play essential roles in NDV attachment and fusion of cells during infection. Antibodies to the F or HN proteins are capable of virus neutralization; however, no full-length sequences are available for these genes from recently obtained virulent isolates. Therefore, nucleotide and predicted amino acid sequences of the F and HN protein genes from 16 NDV isolates representing highly virulent viruses from worldwide sources were obtained for comparison to older virulent isolates and vaccine strains. The F protein amino acid sequence was relatively conserved among isolates maintaining potential glycosylation sites and C residues for disulfide bonds. A dibasic amino acid motif was present at the cleavage site among more virulent isolates, while the low virulence viruses did not have this sequence. However, a Eurasian collared dove virus had a K114Q substitution at the F cleavage site unique among NDV isolates. The HN protein among NDV isolates maintained predicted catalytic and active site residues necessary for neuraminidase activity and hemagglutination. Length of the HN for the Eurasian collared dove isolate and a previously reported heat resistant virulent isolate were longer relative to other more recent virulent isolates. Phylogenetically NDV isolates separated into four groups with more recent virulent isolates forming a diverse branch, while all the avian paramyxoviruses formed their own clade distinct from other members of the Paramyxoviridae.
authors.affiliation: Southeast Poultry Research Laboratory, Agricultural Research Service, US Department of Agriculture, 934 College Station Road, Athens 30605, GA USA. bseal@saa.ars.usda.gov
authors.forename: Bruce S
authors.initials: BS
authors.lastname: Seal
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D006023:Glycoproteins / Q000737:chemistry*; D006388:Hemagglutinins / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000737:chemistry / Q000235:genetics; D009522:Newcastle disease virus / Q000235:genetics* / Q000302:isolation & purification*; D010802:Phylogeny; D017421:Sequence Analysis; D014760:Viral Fusion Proteins / Q000737:chemistry / Q000235:genetics; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics*; D053585:Virus Attachment
chemical_list: D006023:Glycoproteins; D006388:Hemagglutinins; D014760:Viral Fusion Proteins; D014764:Viral Proteins; D009439:Neuraminidase