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Provirus silencing, or proviral silencing, is the repression of expression of proviral genes in cells. A provirus is a viral DNA that has been incorporated into the chromosome of a host cell, often by retroviruses such as HIV. [1] Endogenous retroviruses are always in the provirus state in the host cell and replicate through reverse ...
A provirus does not directly make new DNA copies of itself while integrated into a host genome in this way. Instead, it is passively replicated along with the host genome and passed on to the original cell's offspring; all descendants of the infected cell will also bear proviruses in their genomes.
A retrovirus is a type of virus that inserts a DNA copy of its RNA genome into the DNA of a host cell that it invades, thus changing the genome of that cell. [2] After invading a host cell's cytoplasm, the virus uses its own reverse transcriptase enzyme to produce DNA from its RNA genome, the reverse of the usual pattern, thus retro (backward).
Diagram displaying the integration of viral DNA into a host genome. Endogenous retroviruses can play an active role in shaping genomes. Most studies in this area have focused on the genomes of humans and higher primates, but other vertebrates, such as mice and sheep, have also been studied in depth.
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The body uses its immune system to protect itself from bacteria, viruses and other disease-causing beings, and when it fails to do so immunodeficiency diseases occur. One such disease is acquired immunodeficiency syndrome which is most commonly a result of an infection by the human immunodeficiency virus (HIV). [1]
In the life cycle of retroviruses, proviral DNA is incorporated in transcription of the DNA of the cell being infected. Since retroviruses need to change their pre-mRNA into DNA so that this DNA can be integrated within the DNA of the host it is affecting, the formation of that DNA template is a vital step for retrovirus replication.
The polymerase is a monomeric protein with two distinct functional domains. Site-directed mutagenesis experiments support the proposition that this protein displays a structural and functional similarity to the Klenow fragment of the Escherichia coli Polymerase I enzyme; [3] it comprises a C-terminal polymerase domain and a spatially separated N-terminal domain with a 3'-5' exonuclease activity.