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The pseudotypic paradox.

The Journal of General Virology

|November 1, 1982

Summary

This summary is machine-generated.

Enveloped viruses exhibit non-specific glycoprotein mixing during dual infections but specifically exclude cellular proteins. This suggests a shared viral budding mechanism and a common evolutionary origin for virus envelope glycoproteins.

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Area of Science:

Virology
Molecular Biology
Evolutionary Biology

Background:

Enveloped viruses assemble surface glycoproteins during replication.
The mechanisms governing glycoprotein incorporation into new virions are not fully understood.
Previous studies indicate both mixing and exclusion phenomena in viral glycoprotein assembly.

Purpose of the Study:

To investigate the specificity of virion surface glycoprotein assembly in enveloped viruses.
To explore the potential shared molecular mechanisms underlying glycoprotein incorporation and exclusion.
To examine the evolutionary implications of observed glycoprotein assembly patterns.

Main Methods:

Analysis of glycoprotein composition in progeny virions from dual-infected cells.

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Comparison of viral glycoprotein incorporation with cellular protein exclusion.

Comparative analysis of glycoprotein assembly mechanisms across different enveloped viruses.

Main Results:

Enveloped viruses efficiently mix glycoproteins from unrelated co-infecting viruses.
Non-viral cellular surface proteins are largely excluded from progeny virions.
A common mechanism for specific glycoprotein assembly and cellular protein exclusion appears conserved among enveloped viruses.

Conclusions:

Enveloped viruses possess a conserved mechanism for specific glycoprotein assembly and cellular protein exclusion.
This conserved mechanism suggests a potential single ancestral origin for virus envelope surface structures.
Further research into the molecular basis of this mechanism could reveal novel antiviral strategies.