Protein Variants | Comment | Organism |
---|---|---|
additional information | an HIV-1 mutant can tolerate an about 10fold higher RNase H activity | Human Immunodeficiency Virus |
additional information | naturally occurring polymophisms at position 294 in HIV-2 are Q, E, L, H, and K | Human Immunodeficiency Virus |
Q294P | site-directed mutagenesis, the Q294P mutant of HIV-2 RT has about 10fold higher RNase H activity than the wild-type. Infectious HIV-2 cannot bear the replacement of the RT's Gln294 by the HIV-1 RT Pro counterpart, as it results in substantially reduced HIV-2 replication and fast reversions to the wild-type Gln294 virus | Human Immunodeficiency Virus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | antiretroviral drugs inhibit the reverse-transcriptase (RT) of HIV. The differences between HIV-1 and HIV-2 RTs explain why some of the anti-HIV-1 drugs are not effective against HIV-2. One major difference between the two HIV RTs is the low ribonuclease H (RNase H) activity of HIV-2 RT relative to HIV-1 RT | Human Immunodeficiency Virus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human Immunodeficiency Virus | - |
HIV-1 | - |
Human Immunodeficiency Virus | - |
HIV-2 | - |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease H | - |
Human Immunodeficiency Virus |
RNase H | - |
Human Immunodeficiency Virus |
General Information | Comment | Organism |
---|---|---|
malfunction | an HIV-1 mutant can tolerate an about 10fold higher RNase H activity | Human Immunodeficiency Virus |
malfunction | the Q294P mutant of HIV-2 RT has about 10fold higher RNase H activity than the wild-type. Infectious HIV-2 cannot bear the replacement of the RT's Gln294 by the HIV-1 RT Pro counterpart, as it results in substantially reduced HIV-2 replication and fast reversions to the wild-type Gln294 virus. Critical role of maintaining low RT-associated RNase H activity in HIV-2 | Human Immunodeficiency Virus |
physiological function | low ribonuclease H (RNase H) activity of HIV-2 reverse transcriptase (RT) relative to HIV-1 RT. Residue Gln294 in HIV-2 RT accounts for this RNase H reduction (the comparable residue in HIV-1 RT is Pro294), as the Q294P mutant of HIV-2 RT has about 10fold higher RNase H activity | Human Immunodeficiency Virus |