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Protein-protein interactions in an alphavirus membrane
1Cell Research Institute, University of Texas, Austin 78713-7640.
Journal of Virology
|March 1, 1991
Summary
This study reveals how Sindbis virus envelope glycoproteins E1 and E2 form distinct heterodimers and assemble into capsomeres. These interactions organize the icosahedral structure of the mature Sindbis virus virion.
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- The Sindbis virus surface is composed of E1 and E2 envelope glycoproteins.
- Understanding the organization of these glycoproteins is crucial for comprehending virus assembly and structure.
Purpose of the Study:
- To determine the near-neighbor associations and planar organization of Sindbis virus E1 and E2 envelope glycoproteins.
- To elucidate the structural basis of the icosahedral surface of Sindbis virus.
Main Methods:
- Utilized homobifunctional chemical cross-linkers with varying span distances.
- Analyzed protein-protein interactions between E1 and E2 glycoproteins.
Main Results:
- Identified E1-E2 heterodimers as the virus protomeric units, existing in two distinct conformational states.
- Demonstrated that three E1-E2 heterodimers form trimeric capsomeres, stabilized by E1-E1 interactions.
- Showed E2-E2 interactions organize capsomeres into pentameric and hexameric units, with E1-E1 interactions maintaining the icosahedral lattice.
Conclusions:
- The study provides a detailed model for the arrangement of Sindbis virus envelope glycoproteins.
- These findings offer insights into the self-assembly mechanisms of enveloped viruses.
- The conformational plasticity of E1-E2 heterodimers is key to forming the icosahedral structure.