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Biochem Biophys Res Commun. 2004 Apr 2;316(2):468-75.

A perforin-like protein from a marine mollusk.

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Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92093-0202, USA.


Abalone (gastropod mollusks) express a protein, abMpeg1, which is a homolog of two mammalian proteins that share homology with mammalian perforin, a cytolytic and immune-regulatory protein of lymphocytes. One of the mammalian proteins, Mpeg1, is expressed in mature macrophage and prion-infected mouse brains, while the other, Epcs50, is expressed in ectoplacental cone cells of the invading placenta. Although the functions of these three proteins remain unknown, their structural similarity to mammalian perforin suggests that they may be involved in cell killing, the inflammatory response or tissue invasion. Consistent with these proposed functions, the Mpeg1 gene family shows the signature of positive Darwinian selection (adaptive evolution). The perforin-homology domain of abMpeg1 contains the cytolytic "helix-turn-helix" domain of perforin, supporting the idea that abMpeg1 is a cytolytic protein of the abalone innate immune system. The alpha-helices of abMpeg1 are amphipathic as are those of perforin. The conservation among abMpeg1, mammalian Mpeg1, and Epcs50 shows that Mpeg1 proteins represent a novel, ancient protein family of probable immunological function.

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