The Transmembrane Conformation of the Influenza B Virus M2 Protein in Lipid Bilayers.

ABSTRACT: Influenza A and B viruses cause seasonal flu epidemics. The M2 protein of influenza B (BM2) is a membrane-embedded tetrameric proton channel that is essential for the viral lifecycle. BM2 is a functional analog of AM2 but shares only 24% sequence identity for the transmembrane (TM) domain. The structure and function of AM2, which is targeted by two antiviral drugs, have been well characterized. In comparison, much less is known about the structure of BM2 and no drug is so far available to inhibit this protein. Here we use solid-state NMR spectroscopy to investigate the conformation of BM2(1-51) in phospholipid bilayers at high pH, which corresponds to the closed state of the channel. Using 2D and 3D correlation NMR experiments, we resolved and assigned the ¹³C and ¹⁵N

SUBMITTER: Mandala VS 

PROVIDER: S-EPMC6403292 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature