{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T21:25:58Z","timestamp":1790803558620,"version":"4.1.0"},"reference-count":61,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2024,10,22]],"date-time":"2024-10-22T00:00:00Z","timestamp":1729555200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/doi.org\/10.1128\/ASMCopyrightv2"},{"start":{"date-parts":[[2024,10,22]],"date-time":"2024-10-22T00:00:00Z","timestamp":1729555200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100004794","name":"Centre National de la Recherche Scientifique","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100004794","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"crossref","award":["Retro-Placenta"],"award-info":[{"award-number":["Retro-Placenta"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2024,10,22]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:sec>\n            <jats:title\/>\n            <jats:p>\n              <jats:italic>Syncytins<\/jats:italic>\n              are envelope genes of retroviral origin that play a critical role in the formation of a syncytial structure at the fetomaternal interface\n              <jats:italic>via<\/jats:italic>\n              their fusogenic activity. The mouse placenta is unique among placental mammals since the fetomaternal interface comprises two syncytiotrophoblast layers (ST-I and ST-II) instead of one observed in all other hemochorial placentae. Each layer specifically expresses a distinct mouse syncytin, namely syncytin-A (SynA) for ST-I and syncytin-B (SynB) for ST-II, which have been shown to be essential to placentogenesis and embryonic development. The cellular receptor for SynA has been identified as the membrane protein LY6E and is not the receptor for SynB. Here, by combining a cell\u2013cell fusion assay with the screening of a human ORFeome-derived expression library, we identified the transmembrane multipass sodium-dependent phosphate transporter 1 PiT1\/SLC20A1 as the receptor for SynB. Transfection of cells with the cloned receptor, but not the closely related PiT2\/SLC20A2, leads to their fusion with cells expressing SynB, with no cross-reactive fusion activity with SynA. The interaction between the two partners was further demonstrated by immunoprecipitation. PiT1\/PiT2 chimera and truncation experiments identified the PiT1 N-terminus as the major determinant for SynB-mediated fusion. RT-qPCR analysis of PiT1 expression on a panel of mouse adult and fetal tissues revealed a concomitant increase of PiT1 and SynB specifically in the developing placenta. Finally, electron microscopy analysis of the placenta of PiT1 null embryo before they die (E11.5) disclosed default of ST-II formation with lack of syncytialization, as previously observed in cognate SynB null placenta, and consistent with the present identification of PiT1 as the SynB partner.\n            <\/jats:p>\n            <jats:sec>\n              <jats:title>IMPORTANCE<\/jats:title>\n              <jats:p>\n                Syncytins are envelope genes of endogenous retroviruses, coopted for a physiological function in placentation. They are fusogenic proteins that mediate cell\u2013cell fusion by interacting with receptors present on the partner cells. Here, by devising an\n                <jats:italic>in vitro<\/jats:italic>\n                fusion assay that enables the screening of an ORFeome-derived expression library, we identified the long-sought receptor for syncytin-B (SynB), a mouse syncytin responsible for syncytiotrophoblast formation at the fetomaternal interface of the mouse placenta. This protein \u2013 PiT1\/SLC20A1 \u2013 is a multipass transmembrane protein, also known as the receptor for a series of infectious retroviruses. Its profile of expression is consistent with a role in both ancestral endogenization of a SynB founder retrovirus and present-day mouse placenta formation, with evidence\u2014in PiT1 knockout mice\u2014of unfused cells at the level of the cognate placental syncytiotrophoblast layer.\n              <\/jats:p>\n            <\/jats:sec>\n          <\/jats:sec>","DOI":"10.1128\/jvi.00915-24","type":"journal-article","created":{"date-parts":[[2024,9,17]],"date-time":"2024-09-17T17:00:36Z","timestamp":1726592436000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":9,"title":["Sodium-dependent phosphate transporter PiT1\/SLC20A1 as the receptor for the endogenous retroviral envelope syncytin-B involved in mouse placenta formation"],"prefix":"10.1128","volume":"98","author":[{"ORCID":"https:\/\/orcid.org\/0009-0007-4252-6894","authenticated-orcid":false,"given":"Guillaume","family":"Mousseau","sequence":"first","affiliation":[{"name":"Viroxis, Institut Gustave Roussy, Villejuif, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"No\u00e9mie","family":"Pr\u00e9ault","sequence":"additional","affiliation":[{"name":"Unit\u00e9 Physiologie et Pathologie Mol\u00e9culaires des R\u00e9trovirus Endog\u00e8nes et Infectieux, CNRS UMR 9196, Institut Gustave Roussy, Universit\u00e9 Paris-Saclay, Villejuif, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sylvie","family":"Souquere","sequence":"additional","affiliation":[{"name":"AMMICA UMS-3655, Institut Gustave Roussy, Universit\u00e9 Paris-Saclay, Villejuif, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caroline","family":"Bireau","sequence":"additional","affiliation":[{"name":"Unit\u00e9 Physiologie et Pathologie Mol\u00e9culaires des R\u00e9trovirus Endog\u00e8nes et Infectieux, CNRS UMR 9196, Institut Gustave Roussy, Universit\u00e9 Paris-Saclay, Villejuif, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia","family":"Cassonnet","sequence":"additional","affiliation":[{"name":"Unit\u00e9 de G\u00e9n\u00e9tique Mol\u00e9culaire des Virus \u00e0 ARN, D\u00e9partement Virologie, Institut Pasteur, Paris, France"},{"name":"UMR3569, Centre National de la Recherche Scientifique, Paris, France"},{"name":"Universit\u00e9 Paris Diderot, Sorbonne Paris Cit\u00e9, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Agathe","family":"Bacquin","sequence":"additional","affiliation":[{"name":"Viroxis, Institut Gustave Roussy, Villejuif, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurent","family":"Beck","sequence":"additional","affiliation":[{"name":"Nantes Universit\u00e9, CNRS, Inserm, l'Institut 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