Membrane glycoproteins of Newcastle disease virus: nucleotide sequence of the hemagglutinin-neuraminidase cloned gene and structure/function relationship of predicted amino acid sequence

Glycoconj J. 2001 Apr;18(4):283-9. doi: 10.1023/a:1013756813921.

Abstract

The nucleotide sequence of the glycoprotein hemagglutinin-neuraminidase (HN) gene of the Newcastle disease virus (NDV) strain Clone-30 has been determined. The open reading frame of the HN gene contains 1731 nucleotides and encodes a protein of 577 amino acids. Three highly conserved patterns among all paramyxovirus HN glycoproteins, and one additional conserved species-specific region are present. The protein contains five potential N-glycosylation sites, all but one located in the C-terminal external domain. The secondary structure prediction shows that the C-terminal external domain is mostly arranged in beta-sheets, while alpha-helices are predominantly located in the N-terminal domain. The nucleotide sequence data of the HN gene reported in this paper has been deposited in the GenBank database, under accession number AF098289.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Glycosylation
  • HN Protein / chemistry*
  • HN Protein / genetics*
  • HN Protein / metabolism
  • Hydrophobic and Hydrophilic Interactions
  • Membrane Glycoproteins / chemistry*
  • Membrane Glycoproteins / genetics*
  • Membrane Glycoproteins / metabolism
  • Molecular Sequence Data
  • Newcastle disease virus / metabolism*
  • Protein Structure, Secondary
  • Structure-Activity Relationship

Substances

  • HN Protein
  • Membrane Glycoproteins

Associated data

  • GENBANK/AF098289