Moelling K 2012 Ribonucleases H or RNases H are conserved and exist in almost every organism. They generate and remove RNA primers, which are required for DNA replication. RNases H hydrolyze RNA in RNA-DNA hybrids. RNases H and related enzymes contribute to reduction of gene expression in antisense and small-interfering RNA mechanisms for gene silencing. Retroviruses code for RNases H, which are required for DNA provirus synthesis. Their RNase H is fused to the reverse transcriptase and essential for virus replication inside the cell. Retroviruses code for four enzymes, three of which have been targeted by antiretroviral therapies. A drug against the fourth one, the retroviral RNase H, does not yet exist. The viral but not cellular RNases H should be targeted by drug design. Some details will be discussed here. Furthermore, a compound is described, which enables the RNase H to kill cell-free HIV particles by driving the virus into suicide - with potential use as a microbicide. https://sonar.ch/global/documents/211641 eng info:eu-repo/semantics/altIdentifier/doi/10.1097/QAD.0b013e32835537d3 info:eu-repo/semantics/altIdentifier/pmid/22555171 AIDS (London, England). - 2012 Amino Acid Sequence Anti-Infective Agents DNA Replication Drug Design Gene Expression Regulation, Viral Gene Silencing HIV Reverse Transcriptase HIV-1 Humans Mutation Nucleic Acid Amplification Techniques RNA, Viral Ribonuclease H Virus Replication Targeting the retroviral ribonuclease H by rational drug design. http://purl.org/coar/resource_type/c_6501