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These adhesins include integrin \u03b1\u03b2 heterodimers in metazoans and single subunit transmembrane proteins in apicomplexans such as TRAP in Plasmodium and MIC2 in Toxoplasma. Here we show that the I domain of TRAP is essential for sporozoite gliding motility, mosquito salivary gland invasion and mouse infection. Its replacement with the I domain from Toxoplasma MIC2 fully restores tissue invasion and parasite transmission, while replacement with the aX I domain from human integrins still partially restores liver infection. Mutations around the ligand binding site allowed salivary gland invasion but led to inefficient transmission to the rodent host. These results suggest that apicomplexan parasites appropriated polyspecific I domains in part for their ability to engage with multiple ligands and to provide traction for emigration into diverse organs in distant phyla.<\/jats:p>","DOI":"10.7554\/elife.57572","type":"journal-article","created":{"date-parts":[[2020,7,10]],"date-time":"2020-07-10T05:00:11Z","timestamp":1594357211000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.57572","source":"Crossref","is-referenced-by-count":24,"title":["Evolutionarily distant I domains can functionally replace the essential ligand-binding domain of Plasmodium TRAP"],"prefix":"10.7554","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9108-454X","authenticated-orcid":true,"given":"Dennis","family":"Klug","sequence":"first","affiliation":[{"name":"Integrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany"},{"name":"Universit\u00e9 de Strasbourg, CNRS UPR9022, INSERM U963, 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