B23/nucleophosmin interacts with bovine immunodeficiency virus Rev protein and facilitates viral replication

The bovine immunodeficiency virus (BIV) Rev shuttling protein contains nuclear/nucleolar localization signals and nuclear import/export mechanisms that are novel among lentivirus Rev proteins. Several viral proteins localize to the nucleolus, which may play a role in processes that are essential to the outcome of viral replication. Although BIV Rev localizes to the nucleoli of transfected/infected cells and colocalizes with one of its major proteins, nucleophosmin (NPM1, also known as B23), the role of the nucleolus and B23 in BIV replication remains to be determined. Here, we demonstrate for the first time that BIV Rev interacts with nucleolar phosphoprotein B23 in cells. Using small interfering RNA (siRNA) technology, we show that depletion of B23 expression inhibits virus production by BIV-infected cells, indicating that B23 plays an important role in BIV replication. The interaction between Rev and B23 may represent a potential new target for the development of antiviral drugs against lentiviruses. •BIV Rev protein interacts with nucleolar protein nucleophosmin (B23).•Interaction between BIV Rev and B23 is independent of RNA.•BIV Rev and B23 interact through multiple binding sites within Rev bipartite NLS.•BIV Rev/B23 interaction is independent of nucleolar localization of Rev.•Knockdown of B23 results in a reduction of BIV viral titers in Cf2Th cells.