{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T14:07:33Z","timestamp":1778594853872,"version":"3.51.4"},"reference-count":116,"publisher":"Portland Press Ltd.","issue":"1","license":[{"start":{"date-parts":[[2023,2,23]],"date-time":"2023-02-23T00:00:00Z","timestamp":1677110400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2023,3,31]]},"abstract":"<jats:p>Eukaryotic pathogens with an intracellular parasitic lifestyle are shielded from extracellular threats during replication and growth. In addition to many nutrients, parasites scavenge host cell lipids to establish complex membrane structures inside their host cells. To counteract the disturbance of the host cell plasma membrane they have evolved strategies to regulate phospholipid asymmetry. In this review, the function and importance of lipid asymmetry in the interactions of intracellular protozoan parasites with the target and immune cells of the host are highlighted. The malaria parasite Plasmodium infects red blood cells and extensively refurbishes these terminally differentiated cells. Cholesterol depletion and an altered intracellular calcium ion homeostasis can lead to disruption in erythrocyte membrane asymmetry and increased exposure of phosphatidylserine (PS). Binding to the PS receptor on monocytes and macrophages results in phagocytosis and destruction of infected erythrocytes. Leishmania parasites display apoptotic mimicry by actively enhancing PS exposure on their surface to trigger increased infection of macrophages. In extracellular Toxoplasma gondii a P4-type ATPase\/CDC50 co-chaperone pair functions as a flippase important for exocytosis of specialised secretory organelles. Identification and functional analysis of parasite lipid-translocating proteins, i.e. flippases, floppases, and scramblases, will be central for the recognition of the molecular mechanisms of parasite\/host interactions. Ultimately, a better understanding of parasitic diseases, host immunity, and immune escape by parasites require more research on the dynamics of phospholipid bilayers of parasites and the infected host cell.<\/jats:p>","DOI":"10.1042\/etls20220089","type":"journal-article","created":{"date-parts":[[2023,2,23]],"date-time":"2023-02-23T15:38:28Z","timestamp":1677166708000},"page":"67-79","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["The enemy within: lipid asymmetry in intracellular parasite\u2013host interactions"],"prefix":"10.1042","volume":"7","author":[{"given":"Merryn","family":"Fraser","sequence":"first","affiliation":[{"name":"1Research School of Biology, Australian National University, Canberra, Australia"},{"name":"2Department of Molecular Parasitology, Institute of Biology, Humboldt University, Berlin, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kai","family":"Matuschewski","sequence":"additional","affiliation":[{"name":"2Department of Molecular Parasitology, Institute of Biology, Humboldt University, Berlin, Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7369-1058","authenticated-orcid":false,"given":"Alexander G.","family":"Maier","sequence":"additional","affiliation":[{"name":"1Research School of Biology, Australian National University, Canberra, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2023,2,23]]},"reference":[{"key":"2023033115021295500_","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1038\/s41586-019-1344-7112","article-title":"Structure and autoregulation of a P4-ATPase lipid flippase","volume":"571","year":"2019","journal-title":"Nature"},{"key":"2023033115021295500_","doi-asserted-by":"publisher","first-page":"2264","DOI":"10.1038\/s41467-020-16155-2","article-title":"ABCG2 transports anticancer drugs via a closed-to-open switch","volume":"11","year":"2020","journal-title":"Nat. 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