Em. Wall et al., A NOVEL POXVIRUS GENE AND ITS HUMAN HOMOLOG ARE SIMILAR TO AN ESCHERICHIA-COLI LYSOPHOSPHOLIPASE, Virus research, 52(2), 1997, pp. 157-167
A novel poxvirus gene has been characterized within the genome of ectr
omelia virus. It has significant similarity to a family of lysophospho
lipases suggesting that it may function in the degradation of lysophos
pholipids. Since these molecules are active in the stimulation of infl
ammation, we hypothesize that this gene may play a role in virus virul
ence. This gene is expressed early in the ectromelia virus replication
cycle, before DNA replication. We have also characterized a human cDN
A that encodes a protein which is 49.5% identical to the ectromelia vi
rus protein. By its presence in multiple cDNA libraries, this human ge
ne 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 indi
cative of a serine-aspartic acid-histidine catalytic triad, similar to
those used by true lipases and a number of esterases. (C) 1997 Elsevi
er Science B.V.