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Related Experiment Video

Updated: Jul 16, 2026

MicroRNA-based Regulation of Picornavirus Tropism

MicroRNA-based Regulation of Picornavirus Tropism

Published on: February 6, 2017

Structural refinement and analysis of Mengo virus.

S Krishnaswamy¹, M G Rossmann

¹Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.

Journal of Molecular Biology

|February 20, 1990

Summary

This study refines the 3 Angstrom resolution structure of Mengo encephalomyelitis virus, revealing its 60 protomer composition and subunit interactions. Key structural alterations and protein similarities to other viruses are detailed.

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Area of Science:

Structural Biology
Virology
Biochemistry

Background:

Mengo encephalomyelitis virus is an important pathogen.
Understanding viral structure is crucial for developing antiviral strategies.

Purpose of the Study:

To determine the high-resolution structure of Mengo encephalomyelitis virus.
To analyze the structural components and their interactions within the virus.

Main Methods:

X-ray crystallography at 3 Angstrom resolution.
Hendrickson-Konnert refinement with molecular replacement and icosahedral symmetry constraints.
Analysis of protein subunit composition, sequence alterations, and structural similarities.

Main Results:

The virus structure comprises 60 protomers, each with VP1, VP2, VP3, and VP4 subunits.
Identified sequence alterations in VP1 and VP3, and modified regions of weak density.
Characterized disulfide bridges, identified cis proline residues, and located a phosphate ion potentially involved in receptor attachment.
Detailed the hydrogen-bonding networks and hydrophobic/charged residue distribution around icosahedral axes.
Elucidated the interactions holding protomers, pentamers, and pentamers together.

Conclusions:

The refined structure provides detailed insights into Mengo virus architecture and subunit organization.
Structural comparisons reveal varying degrees of similarity with human rhinovirus 14 and southern bean mosaic virus.
Specific structural features likely relate to the virus's functional requirements and receptor interactions.