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In humans, this diversity is mainly generated by lysophospholipid acyltransferases (LPLATs), yet the evolutionary distribution and diversity of LPLATs across organisms remain poorly understood, particularly in pathogens. Here, we systematically identified candidate LPLAT proteins belonging to two major families in representative prokaryotic and eukaryotic species and reconstructed their phylogenetic relationships. The analysis reveals a marked expansion and diversification of LPLATs in vertebrates and suggests the possibility of pathogen-specific LPLAT expansions. These findings suggest that the diversification of membrane phospholipid remodeling enzymes may accompany increasing biological complexity and pathogenicity. This study provides an evolutionary framework for understanding phospholipid metabolism and highlights pathogen LPLATs as potential targets for exploring host defense mechanisms.<\/jats:p>","DOI":"10.3389\/fimmu.2026.1838657","type":"journal-article","created":{"date-parts":[[2026,8,10]],"date-time":"2026-08-10T05:31:22Z","timestamp":1786339882000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["An evolutionary analysis of lysophospholipid acyltransferases generating membrane phospholipid diversity"],"prefix":"10.3389","volume":"17","author":[{"given":"Hideo","family":"Shindou","sequence":"first","affiliation":[{"name":"Department of Lipid Life Science, National Institute of Global Health and Medicine, Japan Institute for Health Security (JIHS)","place":["Shinjuku-ku, Tokyo, Japan"]},{"name":"Department of Medical Lipid Science, Graduate School of Medicine, The University of Tokyo","place":["Bunkyo-ku, Tokyo, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yosuke","family":"Kawai","sequence":"additional","affiliation":[{"name":"Human Population Genomics laboratory, Department of Informatics, National Institute of Genetics. 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