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Substructures and polypeptides of Visna virus.

F H Lin, H Thormar

Journal of Virology

|October 1, 1974

Summary

Visna virus proteins were separated into 10 polypeptides using chromatography. Virion disruption revealed a heavy fraction containing viral RNA and DNA polymerase, suggesting internal ribonucleoprotein complex formation.

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Area of Science:

Virology
Molecular Biology
Biochemistry

Background:

Visna virus is an important retrovirus with implications for understanding lentiviral structure and replication.
Characterizing viral protein components and their organization is crucial for understanding viral assembly and function.

Purpose of the Study:

To elucidate the protein composition and structural organization of Visna virus particles.
To identify the specific viral components associated with enzymatic activity and genetic material.

Main Methods:

Agarose gel column chromatography in guanidine hydrochloride to resolve viral proteins.
Potassium tartrate gradient centrifugation to separate disrupted virions into fractions.
Analysis of polypeptide composition, glycopolypeptides, viral RNA, and DNA polymerase activity in each fraction.

Main Results:

Visna virus proteins resolved into 10 polypeptides, with two containing glycopolypeptides.
Disrupted virions yielded two fractions (1.08 and 1.24 g/ml).
The light fraction (1.08 g/ml) contained most viral DNA polymerase activity, glycopolypeptides, and some RNA and proteins.
The heavy fraction (1.24 g/ml) contained the remaining viral RNA, most endogenous DNA polymerase activity, and a major internal polypeptide (GuHCl6).

Conclusions:

Virion disruption, even under mild conditions, leads to significant degradation of subviral structures.
The heavy fraction represents a core ribonucleoprotein complex containing viral RNA and the majority of endogenous DNA polymerase activity.
A major internal polypeptide (GuHCl6) is a key component of the Visna virus ribonucleoprotein complex.

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