Cryo-EM Structure of Chikungunya Virus in Complex with the Mxra8 Receptor

Katherine Basore; Arthur S. Kim; Christopher A. Nelson; Rong Zhang; Brittany K. Smith; Carla Uranga; Lo Vang; Ming Cheng; Michael L. Gross; Jonathan Smith; Michael S. Diamond; Daved H. Fremont

doi:10.1016/j.cell.2019.04.006

Cryo-EM Structure of Chikungunya Virus in Complex with the Mxra8 Receptor

Katherine Basore, Arthur S. Kim, Christopher A. Nelson, Rong Zhang, Brittany K. Smith, Carla Uranga, Lo Vang, Ming Cheng, Michael L. Gross, Jonathan Smith, Michael S. Diamond, Daved H. Fremont

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116 Scopus citations

Abstract

Basore et al. describe an X-ray crystal structure of Mxra8, an entry receptor for arthritogenic alphaviruses, and cryo-EM structures of Mxra8 bound to CHIKV. Mxra8 has an unusual Ig-like domain architecture with a head-to-head arrangement, with domain 1 emanating from a loop of domain 2. Mxra8 binds into a complex quaternary cleft formed between two E2-E1 heterodimers within a trimeric spike, while also contacting E1 from a neighboring spike. Mxra8 occupancy is lower when E3 protein is retained on the virion.

Original language	English
Pages (from-to)	1725-1737.e16
Journal	Cell
Volume	177
Issue number	7
DOIs	https://doi.org/10.1016/j.cell.2019.04.006
State	Published - Jun 13 2019

Keywords

HDX mass spectrometry
alphavirus
cryo-electron microscopy
infection
protein crystallography
surface plasmon resonance
virus receptor

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10.1016/j.cell.2019.04.006

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title = "Cryo-EM Structure of Chikungunya Virus in Complex with the Mxra8 Receptor",

abstract = "Basore et al. describe an X-ray crystal structure of Mxra8, an entry receptor for arthritogenic alphaviruses, and cryo-EM structures of Mxra8 bound to CHIKV. Mxra8 has an unusual Ig-like domain architecture with a head-to-head arrangement, with domain 1 emanating from a loop of domain 2. Mxra8 binds into a complex quaternary cleft formed between two E2-E1 heterodimers within a trimeric spike, while also contacting E1 from a neighboring spike. Mxra8 occupancy is lower when E3 protein is retained on the virion.",

keywords = "HDX mass spectrometry, alphavirus, cryo-electron microscopy, infection, protein crystallography, surface plasmon resonance, virus receptor",

author = "Katherine Basore and Kim, {Arthur S.} and Nelson, {Christopher A.} and Rong Zhang and Smith, {Brittany K.} and Carla Uranga and Lo Vang and Ming Cheng and Gross, {Michael L.} and Jonathan Smith and Diamond, {Michael S.} and Fremont, {Daved H.}",

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month = jun,

day = "13",

doi = "10.1016/j.cell.2019.04.006",

language = "English",

volume = "177",

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AU - Basore, Katherine

AU - Kim, Arthur S.

AU - Nelson, Christopher A.

AU - Zhang, Rong

AU - Smith, Brittany K.

AU - Uranga, Carla

AU - Vang, Lo

AU - Cheng, Ming

AU - Gross, Michael L.

AU - Smith, Jonathan

AU - Diamond, Michael S.

AU - Fremont, Daved H.

PY - 2019/6/13

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AB - Basore et al. describe an X-ray crystal structure of Mxra8, an entry receptor for arthritogenic alphaviruses, and cryo-EM structures of Mxra8 bound to CHIKV. Mxra8 has an unusual Ig-like domain architecture with a head-to-head arrangement, with domain 1 emanating from a loop of domain 2. Mxra8 binds into a complex quaternary cleft formed between two E2-E1 heterodimers within a trimeric spike, while also contacting E1 from a neighboring spike. Mxra8 occupancy is lower when E3 protein is retained on the virion.

KW - HDX mass spectrometry

KW - alphavirus

KW - cryo-electron microscopy

KW - infection

KW - protein crystallography

KW - surface plasmon resonance

KW - virus receptor

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JO - Cell

JF - Cell

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ER -

Cryo-EM Structure of Chikungunya Virus in Complex with the Mxra8 Receptor

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Keywords

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