The primary structure of the cytoplasmic tail domain of influenza hemagglutinin regulates its co-clustering with phosphatidylinositol 4,5-bisphosphate

Abstract

The influenza glycoprotein hemagglutinin (HA) is highly involved in the attachment, entry, and assembly stages of the viral life cycle. Previous work has observed co-localization and evidence for an interaction between HA and the host cell lipid phosphatidylinositol 4,5-bisphosphate (PIP2) (Curthoys et al. 2019 Biophysical J. 116:893), although the details of this interaction are not yet fully understood. While mutations in HA occur frequently, in general there are 3 cysteines and 1-2 basic residues in the cytoplasmic tail domain (CTD) which remain highly conserved.