About: Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus

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About: Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus
Creator	Wang, Lin-Fa Xu, Yan Cattaneo, Roberto Xu, Kai Amaya, Moushimi Marsh, Glenn Broder, Christopher Cheliout, Sofia Laing, Eric Navaratnarajah, Chanakha Nikolov, B Petzing, Stephanie Silva, Da Sterling, Spencer
Source	PMC
abstract	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.
has issue date	2019-10-08(xsd:dateTime)
bibo:doi	10.1073/pnas.1911773116
bibo:pmid	31548390
has license	cc-by-nc-nd
sha1sum (hex)	ca3d3e317e5c694091583d23c1cbcd0b68c88d27
schema:url	https://doi.org/10.1073/pnas.1911773116
resource representing a document's title	Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus
has PubMed Central identifier	PMC6789926
has PubMed identifier	31548390
schema:publication	Proc Natl Acad Sci U S A
resource representing a document's body	covid:ca3d3e317e5c694091583d23c1cbcd0b68c88d27#body_text
is schema:about of	named entity 'residue' named entity 'enter' named entity 'human' named entity 'ephrin' named entity 'species' named entity 'functional' covid:arg/ca3d3e317e5c694091583d23c1cbcd0b68c88d27 named entity 'virus' named entity 'ephrin' named entity 'Hendra virus' named entity 'zoonotic transmission' named entity 'specific' named entity 'Cedar' named entity 'potential' named entity 'ephrin receptor' named entity 'NiV' named entity 'zoonotic transmission' named entity 'ephrin-A5' named entity 'zoonotic' named entity 'crystal structure' named entity 'ephrin-A2' named entity 'receptor' named entity 'ephrin receptors' named entity 'Hepes' named entity 'neurons' named entity 'conformational change' named entity 'ephrin-B1' named entity 'ephrin-A1' named entity 'Crystallographic' named entity 'henipavirus' named entity 'ephrin-A1' named entity 'Virus' named entity 'luciferase' named entity 'henipavirus' named entity 'Cell Lines' named entity 'ephrins' named entity 'encephalitis' named entity 'ephrin-B2' named entity 'Protein' named entity 'binding site' named entity '1:2' named entity 'DNA plasmids' named entity 'Glycoproteins' named entity 'Gene Synthesis' named entity 'glycosylphosphatidylinositol' named entity 'GFP' named entity 'cryoprotectant' named entity 'ephrin-A1' named entity 'competitively inhibits' named entity 'GFP' named entity 'mutation' named entity 'cell entry' named entity 'mice' named entity 'ephrin-A1' named entity 'G-H' named entity 'glycoproteins' named entity 'leader sequence' named entity 'ephrin-B1' named entity 'ephrin-B2' named entity 'UniProt' named entity 'binding pocket' named entity 'amino acid' named entity 'innate immune' named entity 'ephrin-B1' named entity 'Mutagenesis' named entity 'protein' named entity 'protein' named entity 'plasmids'

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