Adenosine deaminase acting on RNA1 (ADAR1) was previously reported to affect HIV-1 replication. We report data showing that ADAR1 interacts with the HIV-1 p55 Gag protein, the major structural protein of the immature virus capsid. Furthermore, we found that the endogenous ADAR1 is incorporated into virions purified from the supernatant of primary HIV-1-infected CD4<sup>+</sup> T lymphocytes. Additional experiments demonstrated that the expression of the p55 Gag protein is sufficient for ADAR1 incorporation into virus-like particles (VLPs).Overall, our data originally support the evidence that ADAR1 can be part of the cell protein array uploaded in HIV-1 particles.
Orecchini, E., Federico, M., Doria, M., Arenaccio, C., Giuliani, E., Ciafrè, S.A., et al. (2015). The ADAR1 editing enzyme is encapsidated into HIV-1 virions. VIROLOGY, 485, 475-480 [10.1016/j.virol.2015.07.027].
The ADAR1 editing enzyme is encapsidated into HIV-1 virions
ARENACCIO, CLAUDIA;
2015-01-01
Abstract
Adenosine deaminase acting on RNA1 (ADAR1) was previously reported to affect HIV-1 replication. We report data showing that ADAR1 interacts with the HIV-1 p55 Gag protein, the major structural protein of the immature virus capsid. Furthermore, we found that the endogenous ADAR1 is incorporated into virions purified from the supernatant of primary HIV-1-infected CD4+ T lymphocytes. Additional experiments demonstrated that the expression of the p55 Gag protein is sufficient for ADAR1 incorporation into virus-like particles (VLPs).Overall, our data originally support the evidence that ADAR1 can be part of the cell protein array uploaded in HIV-1 particles.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
