Reverse-transcriptase

Reverse transcriptase (RT) is an enzyme used by retroviruses, including HIV, to replicate their RNA into DNA. This process, known as reverse transcription, is essential for the virus to integrate into the host cell's genome and begin producing new virus particles. RT is a target for several antiretroviral drugs, which inhibit its function and slow the progression of the virus.

Structure

RT is a protein composed of two subunits, p66 and p51. The p66 subunit contains both the polymerase active site, which carries out the DNA synthesis, and the RNase H active site, which degrades the RNA template. The p51 subunit is structurally similar to p66, but lacks these active sites.

Function

The primary function of RT is to convert the single-stranded RNA genome of the retrovirus into double-stranded DNA. This process occurs in several steps:

1. The RT enzyme binds to the viral RNA and begins synthesizing a complementary DNA (cDNA) strand.
2. Once the cDNA strand is complete, the RT enzyme degrades the original RNA template.
3. The RT enzyme then synthesizes a second DNA strand complementary to the cDNA strand, resulting in a double-stranded DNA molecule.

This double-stranded DNA molecule can then integrate into the host cell's genome, where it serves as a template for the production of new virus particles.

Clinical significance

Because of its crucial role in the life cycle of retroviruses, RT is a major target for antiretroviral drugs. These drugs, known as reverse transcriptase inhibitors, work by blocking the function of RT, thereby preventing the virus from replicating. There are two main types of reverse transcriptase inhibitors: nucleoside reverse transcriptase inhibitors (NRTIs) and non-nucleoside reverse transcriptase inhibitors (NNRTIs).

See also

• Reverse transcription
• Retrovirus
• Antiretroviral drug
• Reverse transcriptase inhibitor

Reverse-transcriptase Resources
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