Cryo-EM structure of the mature and infective Mayaro virus at 4.4 Å resolution reveals features of arthritogenic alphaviruses
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Updated: Nov 4, 2025

Advancing High-Resolution Imaging of Virus Assemblies in Liquid and Ice
Published on: July 20, 2022
Helder V Ribeiro-Filho1, Lais D Coimbra1, Alexandre Cassago2
1Brazilian Biosciences National Laboratory, Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, SP, Brazil.
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 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.
Insights
Researchers revealed the structure of Mayaro virus (MAYV), an emerging arbovirus. This structural insight into MAYV provides a foundation for understanding its disease mechanisms and developing targeted antiviral therapies.
Area of Science:
- Virology
- Structural Biology
- Infectious Diseases
Background:
- Mayaro virus (MAYV) is an emerging arbovirus in the Americas.
- MAYV infection can cause a severe arthritogenic disease.
- The virus's biology is not fully understood, with knowledge often extrapolated from related alphaviruses.
Purpose of the Study:
- To determine the high-resolution structure of Mayaro virus (MAYV).
- To elucidate the structural features and protein interactions of MAYV.
- To identify potential targets for antiviral interventions.
Main Methods:
- Cryo-electron microscopy was used to obtain the structure of MAYV virions.
- Analysis of viral protein organization and interactions.
- Identification of specific MAYV epitopes and glycosylation sites.
Main Results:
- The structure of MAYV was determined at 4.4 Å resolution.
- Typical alphavirus features and organization were observed.
- Specific interactions, including a hydrophobic pocket between E1 and E2 proteins, MAYV-specific conformational epitopes, and glycosylation sites affecting host receptor binding (MXRA8) and spike-protein interactions, were identified.
Conclusions:
- The MAYV structure reveals typical alphavirus characteristics and unique features.
- Identified structural elements, such as glycosylation sites and protein interactions, offer potential targets for MAYV-specific antiviral strategies.
- This structural information advances the understanding of MAYV pathogenesis and antiviral development.
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