The antisense protein of the human immunodeficiency virus type I contains a leucine-rich nuclear export signal

Abstract

Acquired Immunodeficiency Syndrome (AIDS) is characterized by a substantial alteration of the immune system caused by the Human Immunodeficiency Virus (HIV). Numerous studies have been conducted since the emergence of this worldwide pandemic. The ability of this virus to produce an antisense protein (ASP) was suggested a few years after its isolation, but the existence of such a protein has been controverted for a long time. This protein is presumably involved in several viral replication-related pivotal mechanisms and could also play a role in viral persistence. Furthermore, as this protein is supposed to take part into pathways occurring in both the cytoplasm and the nucleus, it was suggested that ASP can shuttle between these two subcellular compartments. Since transport of macromolecules across the nuclear envelope often relies on specific signals, the objective is to investigate whether ASP possesses such a distinctive motif. Studies conducted in the context of this master’s thesis strongly support the existence of a leucine-rich Nuclear Export Signal within this antisense protein. Moreover, experimental data also underscore the potential involvement of cellular proteins in this export mechanism.