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Here, we systematically mapped EBOV\u2010host interactions using affinity purification\u2010mass spectrometry (AP\u2010MS) and proximity labeling, generating a comprehensive protein\u2013protein interaction (PPI) network, of which 1728 are high\u2010confidence core PPIs involving nine EBOV proteins and 914 human interactors. Notably, we identified transmembrane 9 superfamily member 2 (TM9SF2) as a novel attachment factor that facilitates EBOV glycoprotein (GP)\u2010mediated entry. Mechanistic studies demonstrated that the receptor\u2010binding domain (RBD) of EBOV GP associates with the extracellular domain (ECD) of TM9SF2, enhancing cellular adhesion and viral attachment. Moreover, the anti\u2010TM9SF2 antibodies effectively attenuated EBOV GP\u2010mediated pseudovirus entry and infection in vitro. Additionally,\n                    <jats:italic>Tm9sf2<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>+\/<\/jats:italic>\n                    <\/jats:sup>\n                    <jats:italic>\n                      <jats:sup>\u2212<\/jats:sup>\n                    <\/jats:italic>\n                    knockout mice exhibited significantly reduced susceptibility to EBOV pseudoviruses. These findings provide critical insights into EBOV\u2013host interactions and establish TM9SF2 as a promising therapeutic target for antiviral intervention.\n                  <\/jats:p>","DOI":"10.1002\/imo2.70116","type":"journal-article","created":{"date-parts":[[2026,7,3]],"date-time":"2026-07-03T02:42:03Z","timestamp":1783046523000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["A multiplex interactome of Ebola virus proteins reveals TM9SF2 as a cell\u2010surface attachment factor that promotes viral entry"],"prefix":"10.1002","volume":"3","author":[{"given":"Limin","family":"Shang","sequence":"first","affiliation":[{"name":"State Key Laboratory of Medical Proteomics National Center for Protein Sciences (Beijing) Beijing 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