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Significance Nipah and Hendra viruses are pathogenic zoonotic henipaviruses, transmitted from wildlife to humans, and potential epidemic threats. Zoonoses from wildlife hosts to humans require overcoming barriers that limit cross-species transmission. Successful usage of virus entry receptors represents a bottleneck to zoonosis. Conserved ephrins are recognized entry receptors for henipaviruses like Nipah virus. Here, we characterize the ephrin entry receptor usage of Cedar virus (CedV), a related henipavirus with unknown zoonotic potential that is nonpathogenic in animals known to be susceptible to Nipah and Hendra disease. We discovered that CedV utilizes 4 different ephrins, 3 of which are unique receptors for CedV, and determined that a single natural amino acid difference between human and mouse ephrin-A1 can dictate functional receptor usage., Cedar virus (CedV) is a bat-borne henipavirus related to Nipah virus (NiV) and Hendra virus (HeV), zoonotic agents of fatal human disease. CedV receptor-binding protein (G) shares only ∼30% sequence identity with those of NiV and HeV, although they can all use ephrin-B2 as an entry receptor. We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. The CedV G receptor-binding site is structurally distinct from other henipaviruses, underlying its capability to accommodate additional ephrin receptors. We also show that CedV can enter cells through mouse ephrin-A1 but not human ephrin-A1, which differ by 1 residue in the key contact region. This is evidence of species specific ephrin receptor usage by a henipavirus, and implicates additional ephrin receptors in potential zoonotic transmission.