Characterization of a Paramyxovirus from a Fer de Lance viper (Bothrops jararaca): partial nucleotide sequence of the putative fusion protein.
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.
Junqueira de Azevedo
I L
IL
Centro de Biotecnologia Instituto Butantan, São Paulo, Brazil.
Prieto da Silva
A R
AR
Carmona
E
E
Ho
P L
PL
D000595:Amino Acid Sequence; D000818:Animals; D017837:Bothrops / Q000821:virology*; D003001:Cloning, Molecular; D016679:Genome, Viral; D008969:Molecular Sequence Data; D010802:Phylogeny; D018108:Respirovirus / Q000737:chemistry / Q000145:classification / Q000235:genetics*; D016415:Sequence Alignment; D014760:Viral Fusion Proteins / Q000235:genetics*
D014760:Viral Fusion Proteins