Modulation of cell surface transport and lipid raft localization by the cytoplasmic tail of the influenza virus hemagglutinin

• DOI: 10.1111/cmi.12491
• Publication Date: 2015-08-04T18:51:57Z
• Authors: Silvia Scolari; Katharina Imkeller; Fabian Jolmes; Michael Veit; Andreas Herrmann; Roland Schwarzer
• Keywords: Palmitoylation; Lipid raft; Ectodomain; Transport protein

Viral glycoproteins are highly variable in their primary structure, but on the other hand feature a high functional conservation to fulfil versatile tasks during pathogenic life cycle. Typically, all protein domains optimized that indispensable functions can be assigned small conserved motifs or even individual amino acids. The cytoplasmic tail of many viral spike proteins, although particular relevance for virus biology, is often only insufficiently characterized. Hemagglutinin (HA), receptor-binding influenza comprises short 13 acids exhibits three palmitoylation sites. However, importance these modifications and general intracellular trafficking lateral membrane organization remains elusive. In this study, we generated HA core proteins consisting transmembrane domain, minor part ectodomain, tagged with yellow fluorescent protein. Different mutation truncation variants chimeric were investigated using confocal microscopy, characterize role plasma Golgi apparatus. addition, assessed raft partitioning by Foerster resonance energy transfer an established marker. We revealed substantial influence length distribution surface exposure proteins. A complete removal hampers physiological protein, whereas partial compensated palmitoylations. Plasma was found imperatively require palmitoylations, cysteine at position 551 turned out most relevance. Our data shed further light tight interconnection between elements suggest function palmitoylations both sorting anterograde glycoprotein.