African swine fever virus protein p54 interacts with the microtubular motor complex through direct binding to light-chain dynein

Dynein is a minus-end-directed microtubule-associated motor protein involve d in cargo transport in the cytoplasm. African swine fever virus (ASFV), a large DNA virus, hijacks the microtubule motor complex cellular transport m achinery during virus infection of the cell through direct binding of virus protein p54 to the light chain of cytoplasmic dynein (LC8). Interaction of p54 and LC8 occurs both in vitro and in cells, and the two proteins coloca lize at the microtubular organizing center during viral infection. p50/dyna mitin, a dominant-negative inhibitor of dynein-dynactin function, impeded A SFV infection, suggesting an essential role for dynein during virus infecti on. A 13-amino-acid domain of p54 was sufficient for binding to LC8, an SQT motif within this domain being critical for this binding. Direct binding o f a viral structural protein to LC8, a small molecule of the dynein motor c omplex, could constitute a molecular mechanism for microtubule-mediated vir us transport.