Brazilian National Council for Scientific and Technological Development (CNPq)
440379/2016-4
Brazil
Sao Paulo Research Foundation (FAPESP)
2018/03917-6
Brazil
Citation
Journal: Nat Commun / Year: 2021 Title: Cryo-EM structure of the mature and infective Mayaro virus at 4.4 Å resolution reveals features of arthritogenic alphaviruses. Authors: Helder V Ribeiro-Filho / Lais D Coimbra / Alexandre Cassago / Rebeca P F Rocha / João Victor da Silva Guerra / Rafael de Felicio / Carolina Moretto Carnieli / Luiza Leme / Antonio Cláudio ...Authors: Helder V Ribeiro-Filho / Lais D Coimbra / Alexandre Cassago / Rebeca P F Rocha / João Victor da Silva Guerra / Rafael de Felicio / Carolina Moretto Carnieli / Luiza Leme / Antonio Cláudio Padilha / Adriana F Paes Leme / Daniela B B Trivella / Rodrigo Villares Portugal / Paulo Sérgio Lopes-de-Oliveira / Rafael Elias Marques / Abstract: Mayaro virus (MAYV) is an emerging arbovirus of the Americas that may cause a debilitating arthritogenic disease. The biology of MAYV is not fully understood and largely inferred from related ...Mayaro virus (MAYV) is an emerging arbovirus of the Americas that may cause a debilitating arthritogenic disease. The biology of MAYV is not fully understood and largely inferred from related arthritogenic alphaviruses. Here, we present the structure of MAYV at 4.4 Å resolution, obtained from a preparation of mature, infective virions. MAYV presents typical alphavirus features and organization. Interactions between viral proteins that lead to particle formation are described together with a hydrophobic pocket formed between E1 and E2 spike proteins and conformational epitopes specific of MAYV. We also describe MAYV glycosylation residues in E1 and E2 that may affect MXRA8 host receptor binding, and a molecular "handshake" between MAYV spikes formed by N262 glycosylation in adjacent E2 proteins. The structure of MAYV is suggestive of structural and functional complexity among alphaviruses, which may be targeted for specificity or antiviral activity.
History
Deposition
Nov 5, 2020
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Header (metadata) release
Apr 21, 2021
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Map release
Apr 21, 2021
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Update
Jun 9, 2021
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Current status
Jun 9, 2021
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Spherical aberration corrector: Cs corrrector used to minimise the spherical aberration
Image recording
Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number real images: 9100 / Average exposure time: 4.26 sec. / Average electron dose: 30.0 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Software - Name: IMAGIC (ver. 2019) / Software - details: Full data set CTF correction Details: Per particle CTF correction based on IMAGIC movie spectra of all images simultaneously (Full data set CTF correction).
Startup model
Type of model: OTHER / Details: Angular Reconstitution random startup
Final reconstruction
Applied symmetry - Point group: I (icosahedral) / Algorithm: EXACT BACK PROJECTION / Resolution.type: BY AUTHOR / Resolution: 4.4 Å / Resolution method: FSC 1/2 BIT CUT-OFF / Software - Name: IMAGIC (ver. 2019) / Software - details: with software extensions Details: Random assignment of 3D membership to multiple 3D reconstructions during refinements, based on angular reconstitution. Number images used: 40179
Initial angle assignment
Type: ANGULAR RECONSTITUTION / Software - Name: IMAGIC (ver. 2019) Details: Angular reconstitution used originally in random startup mode, later in refinement mode using anchor sets
Final angle assignment
Type: ANGULAR RECONSTITUTION / Software - Name: IMAGIC (ver. 2019) Details: Angular reconstitution in refinement mode using anchor sets and local alignments
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