A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus

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Pryce , R , Azarm , K , Rissanen , I , Harlos , K , Bowden , T A & Lee , B 2020 , ' A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus ' , Life Science Alliance , vol. 3 , no. 1 , 201900578 . https://doi.org/10.26508/lsa.201900578

Title: A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus
Author: Pryce, Rhys; Azarm, Kristopher; Rissanen, Ilona; Harlos, Karl; Bowden, Thomas A.; Lee, Benhur
Contributor: University of Helsinki, Helsinki Institute of Life Science HiLIFE
Date: 2020-01
Language: eng
Number of pages: 15
Belongs to series: Life Science Alliance
ISSN: 2575-1077
URI: http://hdl.handle.net/10138/312433
Abstract: The emergent zoonotic henipaviruses, Hendra, and Nipah are responsible for frequent and fatal disease outbreaks in domestic animals and humans. Specificity of henipavirus attachment glycoproteins (G) for highly species-conserved ephrin ligands underpins their broad host range and is associated with systemic and neurological disease pathologies. Here, we demonstrate that Cedar virus (CedV)—a related henipavirus that is ostensibly nonpathogenic—possesses an idiosyncratic entry receptor repertoire that includes the common henipaviral receptor, ephrin-B2, but, distinct from pathogenic henipaviruses, does not include ephrin-B3. Uniquely among known henipaviruses, CedV can use ephrin-B1 for cellular entry. Structural analyses of CedV-G reveal a key region of molecular specificity that directs ephrin-B1 utilization, while preserving a universal mode of ephrin-B2 recognition. The structural and functional insights presented uncover diversity within the known henipavirus receptor repertoire and suggest that only modest structural changes may be required to modulate receptor specificities within this group of lethal human pathogens.
Subject: 3111 Biomedicine
NIPAH-VIRUS
HENDRA-VIRUS
CRYSTAL-STRUCTURE
HEMAGGLUTININ-NEURAMINIDASE
ATTACHMENT GLYCOPROTEIN
RECEPTOR
TRANSMISSION
RECOGNITION
INFECTION
BATS
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