Characterization of a Paramyxovirus from a Fer de Lance viper (Bothrops jararaca): partial nucleotide sequence of the putative fusion protein

Arch Virol. 2001;146(1):51-7. doi: 10.1007/s007050170190.

Abstract

During the generation of Expressed Sequence Tags (ESTs) from the Fer de Lance viper (Bothrops jararaca) venom glands, a partial cDNA (clone H8) coding for a protein with all the features of a paramyxovirus fusion protein was characterized. It has 920 bp and codes for a partial protein of 279 amino acids. Two potential N-glycosylation sites are present in the sequence which also possesses a typical membrane anchoring domain made of a stretch of hydrophobic amino acids. The polyadenylation signal sequence was identified. When compared to other fusion proteins, it showed the highest sequence similarity (37-39%) with those of human parainfluenza 3 and Sendai virus.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bothrops / virology*
  • Cloning, Molecular
  • Genome, Viral*
  • Molecular Sequence Data
  • Phylogeny
  • Respirovirus / chemistry
  • Respirovirus / classification
  • Respirovirus / genetics*
  • Sequence Alignment
  • Viral Fusion Proteins / genetics*

Substances

  • Viral Fusion Proteins

Associated data

  • GENBANK/AF251500