Simian virus 40 chromatin interaction with the capsid proteins

¹Purdue University, Department of Chemistry, West Lafayette, Indiana 47907.

Journal of Biomolecular Structure & Dynamics

|December 1, 1983

Summary

Investigating simian virus 40 (SV40) assembly, this study analyzed temperature-sensitive mutants to understand capsid protein roles in forming the SV40 chromosome. Findings suggest VP1 protein domains are crucial for viral assembly and capsid structure.

Area of Science:

Virology
Molecular Biology
Structural Biology

Background:

Cellular core histones package Simian Virus 40 (SV40) DNA into nucleosomes, forming the SV40 chromosome.
Understanding how viral capsid proteins assemble this chromatin into infectious virions is crucial for virology research.

Purpose of the Study:

To investigate the roles of SV40 capsid proteins (VP1, VP2, VP3) in the assembly of the SV40 chromosome into virions.
To analyze the interactions between capsid proteins and encapsidated chromatin during viral assembly.

Main Methods:

Analysis of nucleoproteins accumulating in cells infected with temperature-sensitive SV40 assembly mutants (tsC, tsBC, tsB).
Electron microscopy to distinguish morphologically between different nucleoprotein complexes.
Treatment of mature wild-type virions with dithiothreitol (DTT) to probe capsid protein interactions.

Main Results:

Mutants exhibited distinct nucleoprotein accumulation patterns at nonpermissive temperatures, correlating with capsid protein composition.
tsC mutants accumulated 75 S chromatin, while tsBC and tsB mutants produced larger complexes (100-160 S) containing all capsid proteins.
Electron microscopy revealed tsBC complexes as chromatin with attached capsid proteins and tsB complexes as partially assembled virions.
Coinfection with tsB and tsC mutants at 40°C resulted in the assembly of 220 S virions.
Treatment of virions with DTT indicated surface-exposed disulfide bonds between VP1 proteins.

Conclusions:

The VP1 protein likely possesses discrete domains, each potentially serving a specific function in SV40 assembly.
Disulfide bonds between VP1 proteins are present on the virion surface, contributing to capsid integrity.

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Simian virus 40 chromatin interaction with the capsid proteins

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Related Experiment Videos

Simian virus 40 chromatin interaction with the capsid proteins

Area of Science:

Background:

Purpose of the Study:

Main Methods:

Main Results:

Conclusions:

Related Concept Videos

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