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2XBO

Equine Rhinitis A Virus in Complex with its Sialic Acid Receptor

Summary for 2XBO
Entry DOI10.2210/pdb2xbo/pdb
Related2WFF 2WS9
Related PRD IDPRD_900025
DescriptorP1, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total)
Functional Keywordsvirus, capsid
Biological sourceEQUINE RHINITIS A VIRUS
More
Total number of polymer chains4
Total formula weight85902.34
Authors
Fry, E.E.,Tuthill, T.J.,Harlos, K.,Walter, T.S.,Rowlands, D.J.,Stuart, D.I. (deposition date: 2010-04-14, release date: 2010-09-22, Last modification date: 2024-05-08)
Primary citationFry, E.E.,Tuthill, T.J.,Harlos, K.,Walter, T.S.,Rowlands, D.J.,Stuart, D.I.
The Crystal Structure of Equine Rhinitis a Virus in Complex with its Sialic Acid Receptor.
J.Gen.Virol., 91:1971-, 2010
Cited by
PubMed Abstract: Equine rhinitis A virus (ERAV) shares many features with foot-and-mouth disease virus (FMDV) and both are classified within the genus Aphthovirus of the family Picornaviridae. ERAV is used as a surrogate for FMDV research as it does not require high-level biosecurity. In contrast to FMDV, which uses integrins as cellular receptors, the receptor for ERAV has been reported to involve the sugar moiety sialic acid. This study confirmed the importance of sialic acid for cell entry by ERAV and reports the crystal structure of ERAV particles complexed with the receptor analogue 3'-sialyllactose. The receptor is attached to the rim of a capsid pit adjacent to the major immunogenic site and distinct from the sialic acid binding site used by a related picornavirus, the cardiovirus Theiler's murine encephalitis virus. The structure of the major antigenic determinant of the virus, previously identified from antibody escape mutations, is also described as the EF loop of VP1, which forms a hairpin stretching across the capsid surface close to the icosahedral fivefold axis, neighbouring the receptor-binding site, and spanning two protomeric units.
PubMed: 20427563
DOI: 10.1099/VIR.0.020420-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4 Å)
Structure validation

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