作者: Michael S. Mitchell , József Tözsér , Gerald Princler , Patricia A. Lloyd , Ashleigh Auth
关键词: Infectivity 、 Polymerase 、 RNase H 、 Biology 、 Virology 、 Immunoprecipitation 、 Virus 、 Reverse transcriptase 、 Molecular biology 、 Protease 、 Protein subunit
摘要: It is not known whether the low infectivity and virion-associated polymerase activity of human T-cell lymphotropic virus type-1 (HTLV-1) are due to quantity or quality reverse transcriptase (RT), because protein has yet been fully characterized. We have developed anti-RT antibodies constructed HTLV-1 expression plasmids that express truncated hemagglutinin-tagged Pol polyproteins examine maturation composition RT. detected proteins corresponding RT-integrase (IN) (pr98) RT (p62) as well smaller containing (p49) RNase H domains. identified amino acid sequences in polyprotein cleaved by protease yield IN. also cleavage sites within give rise p49 fragment. Immunoprecipitation an epitope-tagged p62 subunit coprecipitated p49, indicating complex can exist a p62/p49 heterodimer analogous HIV-1 (p66/p51).