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Abstract
The retroviral RNA genome encodes for three enzymes essential for virus replication: (i) the viral protease (PR), that converts the immature virion into a mature virus through the cleavage of precursor polypeptides; (ii) the reverse transcriptase (RT), responsible for the conversion of the single-stranded genomic RNA into double-stranded proviral DNA; and (iii) the integrase (IN) that inserts the proviral DNA into the host cell genome. All of them are important targets for therapeutic intervention. This Special Issue provides authoritative reviews on the most recent research towards a better understanding of structure-function relationships in retroviral enzymes. The Issue includes three reviews on retroviral PRs, seven on RT and reverse transcription, and four dedicated to viral integration. [...]
Highlights
The retroviral RNA genome encodes for three enzymes essential for virus replication: (i) the viral protease (PR), that converts the immature virion into a mature virus through the cleavage of precursor polypeptides; (ii) the reverse transcriptase (RT), responsible for the conversion of the single-stranded genomic RNA into double-stranded proviral DNA; and (iii) the integrase (IN) that inserts the proviral
Understanding the specificity of these enzymes should be helpful to design broad-spectrum inhibitors targeting human immunodeficiency virus type 1 (HIV-1) and other retroviruses
Reverse transcription is a relatively complex process that initiates after binding of a specific cellular tRNA to the primer binding site (PBS) located in the 5 ́-end of the viral genome
Summary
The retroviral RNA genome encodes for three enzymes essential for virus replication: (i) the viral protease (PR), that converts the immature virion into a mature virus through the cleavage of precursor polypeptides; (ii) the reverse transcriptase (RT), responsible for the conversion of the single-stranded genomic RNA into double-stranded proviral DNA; and (iii) the integrase (IN) that inserts the proviral. Understanding the specificity of these enzymes should be helpful to design broad-spectrum inhibitors targeting human immunodeficiency virus type 1 (HIV-1) and other retroviruses. PR interactions with inhibitors or substrates, or dimer stability; as well as distal mutations that transmit changes to the active site of the enzyme are discussed in the light of the structural information available in the review authored by Weber and Agniswamy [3].
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