tetano
Editor, Senior Moderator
Biochim Biophys Acta Biomembr. 2019 May 30. pii: S0005-2736(19)30118-X. doi: 10.1016/j.bbamem.2019.05.021. [Epub ahead of print]
[h=1]The distal cytoplasmic tail of the influenza A M2 protein dynamically extends from the membrane.[/h] Kim G[SUP]1[/SUP], Raymond HE[SUP]1[/SUP], Herneisen AL[SUP]1[/SUP], Wong-Rolle A[SUP]1[/SUP], Howard KP[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The influenza A M2 protein is a multifunctional membrane-associated homotetramer that orchestrates several essential events in the viral infection cycle. The monomeric subunits of the M2 homotetramer consist of an N-terminal ectodomain, a transmembrane domain, and a C-terminal cytoplasmic domain. The transmembrane domain forms a four-helix proton channel that promotes uncoating of virions upon host cell entry. The membrane-proximal region of the C-terminal domain forms a surface-associated amphipathic helix necessary for viral budding. The structure of the remaining ~34 residues of the distal cytoplasmic tail has yet to be fully characterized despite the functional significance of this region for influenza infectivity. Here, we extend structural and dynamic studies of the poorly characterized M2 cytoplasmic tail. We used SDSL-EPR to collect site-specific information on the mobility, solvent accessibility, and conformational properties of residues 61-70 of the full-length, cell-expressed M2 protein reconstituted into liposomes. Our analysis is consistent with the predominant population of the C-terminal tail dynamically extending away from the membranes surface into the aqueous medium. These findings provide insight in hypotheses than the C-terminal domain serves as a sensor of changes in both membrane composition and binding of other viral proteins that helps regulate how the multifunctional M2 protein participates in critical events in the viral infection cycle.
Copyright ? 2019. Published by Elsevier B.V.
[h=4]KEYWORDS:[/h] Cytoplasmic tail; Electron paramagnetic resonance; Full-length influenza A M2 protein; Site-directed spin labeling
PMID: 31153909 DOI: 10.1016/j.bbamem.2019.05.021
[h=1]The distal cytoplasmic tail of the influenza A M2 protein dynamically extends from the membrane.[/h] Kim G[SUP]1[/SUP], Raymond HE[SUP]1[/SUP], Herneisen AL[SUP]1[/SUP], Wong-Rolle A[SUP]1[/SUP], Howard KP[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The influenza A M2 protein is a multifunctional membrane-associated homotetramer that orchestrates several essential events in the viral infection cycle. The monomeric subunits of the M2 homotetramer consist of an N-terminal ectodomain, a transmembrane domain, and a C-terminal cytoplasmic domain. The transmembrane domain forms a four-helix proton channel that promotes uncoating of virions upon host cell entry. The membrane-proximal region of the C-terminal domain forms a surface-associated amphipathic helix necessary for viral budding. The structure of the remaining ~34 residues of the distal cytoplasmic tail has yet to be fully characterized despite the functional significance of this region for influenza infectivity. Here, we extend structural and dynamic studies of the poorly characterized M2 cytoplasmic tail. We used SDSL-EPR to collect site-specific information on the mobility, solvent accessibility, and conformational properties of residues 61-70 of the full-length, cell-expressed M2 protein reconstituted into liposomes. Our analysis is consistent with the predominant population of the C-terminal tail dynamically extending away from the membranes surface into the aqueous medium. These findings provide insight in hypotheses than the C-terminal domain serves as a sensor of changes in both membrane composition and binding of other viral proteins that helps regulate how the multifunctional M2 protein participates in critical events in the viral infection cycle.
Copyright ? 2019. Published by Elsevier B.V.
[h=4]KEYWORDS:[/h] Cytoplasmic tail; Electron paramagnetic resonance; Full-length influenza A M2 protein; Site-directed spin labeling
PMID: 31153909 DOI: 10.1016/j.bbamem.2019.05.021