A Mutation at Position 190 of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Interacts with Mutations at Positions 74 and 75 via the Template Primer
AUTOR(ES)
Boyer, Paul L.
FONTE
American Society for Microbiology
RESUMO
We have analyzed amino acid substitutions at position G190 in the reverse transcriptase (RT) of human immunodeficiency virus type 1 (HIV-1). The mutation G190E, which is responsible for resistance to certain nonnucleoside inhibitors, results in RT that has significantly less polymerase activity and that is less processive than wild-type RT. Its kinetic profile with respect to dGTP and poly(rC) · oligo(dG) is significantly altered compared to that of wild-type RT. The combination of either of the mutations L74V or V75I with the G190E mutation appears to be compensatory and mitigates many of the deleterious effects of the G190E mutation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=105433Documentos Relacionados
- Analysis of mutations at position 184 in reverse transcriptase of human immunodeficiency virus type 1.
- Amino Acid Substitutions at Position 190 of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Increase Susceptibility to Delavirdine and Impair Virus Replication
- Cross-Linking of the Fingers Subdomain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase to Template-Primer
- Marked infidelity of human immunodeficiency virus type 1 reverse transcriptase at RNA and DNA template ends.
- Mutation of Amino Acids in the Connection Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase That Contact the Template-Primer Affects RNase H Activity