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The first virally encoded cytochrome p450.

David C Lamb¹, Li Lei, Andrew G S Warrilow

¹Institute of Life Science, Swansea University, United Kingdom. d.c.lamb@swansea.ac.uk

Journal of Virology

|June 12, 2009

Summary

Giant viruses, like Mimivirus, possess unique cytochrome P450 (CYP) genes. Researchers identified and characterized the first viral CYP protein, but its specific function and C-terminal domain remain elusive.

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Area of Science:

Virology
Biochemistry
Genomics

Background:

The genome of the giant virus Acanthamoeba polyphaga mimivirus (Mimivirus) contains two predicted cytochrome P450 (CYP) genes.
One gene product (YP_143162) exhibits partial homology to sterol 14-demethylase (CYP51) and possesses an uncharacterized C-terminal domain.

Purpose of the Study:

To characterize the first identified viral cytochrome P450 protein from Mimivirus.
To investigate the enzymatic activity and substrate binding of the viral CYP protein.

Main Methods:

Expression of the Mimivirus CYP gene (YP_143162) lacking its N-terminal domain in Escherichia coli.
Spectroscopic analysis (CO difference spectrum) to confirm CYP protein identity.
Analysis of lipid and sterol substrate binding and enzymatic activity.

Main Results:

The expressed viral protein was confirmed as a cytochrome P450, showing a CO difference maximum at 448 nm.
Analysis revealed no significant perturbation of the CYP heme environment upon binding of lipid and sterol substrates.
No enzymatic activity was detected when using 14-methyl sterols as substrates.

Conclusions:

The study formally identifies and characterizes the first viral cytochrome P450 protein.
The function of this viral CYP protein and its associated C-terminal domain remains unknown, warranting further investigation.