A novel poxvirus gene and its human homolog are similar to an E. coli lysophospholipase.
A novel poxvirus gene has been characterized within the genome of ectromelia virus. It has significant similarity to a family of lysophospholipases suggesting that it may function in the degradation of lysophospholipids. Since these molecules are active in the stimulation of inflammation, we hypothesize that this gene may play a role in virus virulence. This gene is expressed early in the ectromelia virus replication cycle, before DNA replication. We have also characterized a human cDNA that encodes a protein which is 49.5% identical to the ectromelia virus protein. By its presence in multiple cDNA libraries, this human gene is known to be expressed in a variety of body tissues and is likely to function in the normal regulation of lysophospholipid levels. This family of proteins have conserved blocks of amino acids that are indicative of a serine-aspartic acid-histidine catalytic triad, similar to those used by true lipases and a number of esterases.
Wall
E M
EM
Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
Cao
J
J
Chen
N
N
Buller
R M
RM
Upton
C
C
D000595:Amino Acid Sequence; D001483:Base Sequence; D002460:Cell Line; D004279:DNA, Viral; D004481:Ectromelia virus / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology*; D015870:Gene Expression; D005814:Genes, Viral; D006801:Humans; D008245:Lysophospholipase / Q000235:genetics*; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D004279:DNA, Viral; D008245:Lysophospholipase