A recent unexpected finding revealed the possibility that an RNA helicase may potentially contribute roles in HIV-1 particle assembly and reverse transcription (34) . Using proteomic analyses, Roy et al. (34) reported that the DEAH protein RNA helicase A (RHA) was found associated with HIV-1 Gag and packaged into HIV-1 virions in an RNAdependent manner. When RHA was knocked down in cells, HIV-1 particles which were produced from these cells were significantly less infectious. This appears to be compatible with two possible explanations. First, it is conceivable that RHA participates in the formation of infectious virus particles either by shaping Gag-RNA interaction during viral particle assembly or by budding. Failure of RHA to properly restructure viral RNP could explain the observed reduced infectivity. Second, Roy et al. (34) reported evidence that HIV-1 particles that do not contain RHA showed reduced virionendogenous reverse transcriptase activity. In this respect, it may be that RHA assists HIV-1 reverse transcriptase to more efficiently copy RNA by unwinding RNA secondary structure or by promoting the interaction of viral RNA with the nucleocapsid protein in order to assemble a better reverse transcription complex.