Crystal structure of equine rhinitis A virus in complex with its sialic acid receptor.

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...

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Main Authors: Fry, E, Tuthill, T, Harlos, K, Walter, T, Rowlands, D, Stuart, D
Format: Journal article
Language:English
Published: 2010
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author Fry, E
Tuthill, T
Harlos, K
Walter, T
Rowlands, D
Stuart, D
author_facet Fry, E
Tuthill, T
Harlos, K
Walter, T
Rowlands, D
Stuart, D
author_sort Fry, E
collection OXFORD
description 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.
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spelling oxford-uuid:ecf38491-447c-4ae4-8cac-3bf72b0e02342022-03-27T11:21:19ZCrystal structure of equine rhinitis A virus in complex with its sialic acid receptor.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:ecf38491-447c-4ae4-8cac-3bf72b0e0234EnglishSymplectic Elements at Oxford2010Fry, ETuthill, THarlos, KWalter, TRowlands, DStuart, DEquine 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.
spellingShingle Fry, E
Tuthill, T
Harlos, K
Walter, T
Rowlands, D
Stuart, D
Crystal structure of equine rhinitis A virus in complex with its sialic acid receptor.
title Crystal structure of equine rhinitis A virus in complex with its sialic acid receptor.
title_full Crystal structure of equine rhinitis A virus in complex with its sialic acid receptor.
title_fullStr Crystal structure of equine rhinitis A virus in complex with its sialic acid receptor.
title_full_unstemmed Crystal structure of equine rhinitis A virus in complex with its sialic acid receptor.
title_short Crystal structure of equine rhinitis A virus in complex with its sialic acid receptor.
title_sort crystal structure of equine rhinitis a virus in complex with its sialic acid receptor
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