A NOVEL POXVIRUS GENE AND ITS HUMAN HOMOLOG ARE SIMILAR TO AN ESCHERICHIA-COLI LYSOPHOSPHOLIPASE

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.