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Walleye dermal sarcoma virus reverse transcriptase is temperature sensitive.

Sharon K Fodor¹, Volker M Vogt¹

¹Department of Molecular Biology and Genetics, Biotechnology Building, Cornell University, Ithaca, NY 14853, USA1.

The Journal of General Virology

|May 25, 2002

Summary

This summary is machine-generated.

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Walleye dermal sarcoma virus reverse transcriptase (RT) functions similarly to mammalian RTs. This fish enzyme is inactivated above 15°C, showing no special cold adaptation for viral replication.

Area of Science:

Virology
Biochemistry
Molecular Biology

Background:

Walleye dermal sarcoma virus (WDSV) is a piscine retrovirus.
WDSV naturally replicates in fish at low temperatures (around 4°C).

Purpose of the Study:

To biochemically characterize the reverse transcriptase (RT) enzyme from WDSV.
To investigate the thermal properties and catalytic efficiency of WDSV RT.

Main Methods:

Purification of WDSV RT from virus particles.
Biochemical assays to determine enzyme kinetics (Km for TTP) and thermal stability.
Comparison of WDSV RT activity at different temperatures (4°C vs. 15°C) with recombinant human immunodeficiency virus type 1 RT.

Main Results:

Related Experiment Videos

WDSV RT sediments as a monomer in the absence of a template.
The enzyme exhibits a K(m) of 22 microM for TTP with a poly(rA)-oligo(dT) template.
WDSV RT is rapidly inactivated at temperatures above 15°C.
The temperature-dependent activity ratio (15°C/4°C) for WDSV RT is comparable to that of human immunodeficiency virus type 1 RT.

Conclusions:

WDSV RT shares biochemical properties with other retroviral RTs.
The enzyme is thermally labile and does not show enhanced activity at cold temperatures compared to HIV-1 RT.
These findings suggest WDSV RT may not possess unique cold-adaptation mechanisms for efficient function at low temperatures.