Ubiquitination in influenza a virus-host interactions

As a key pathogen responsible for zoonotic respiratory tract infections, Influenza A virus (IAV) is capable of undergoing antigenic drift and antigenic shift. These two mechanisms result in annual global epidemics caused by IAV, with occasional pandemics. Ubiquitination is an important post-translational modification that maintains cellular homeostasis and internal balance by participating in various biological processes within cells, and it is also a crucial host antiviral defense mechanism. Mutation of gene sites in IAV-encoded proteins is a crucial mechanism for viruses to evolve and adjust to the host environment. This article systematically reviews the mechanisms of interaction between key amino acid residues of IAV-encoded proteins undergoing ubiquitination and host proteins, as well as the effects of experimental mutations, aiming to deeply elucidate the interaction between influenza virus and the host.