The distal cytoplasmic tail of the influenza A M2 protein dynamically extends from the membrane
| Autor: | Kathleen P. Howard, Alice L. Herneisen, Abigail Wong-Rolle, Grace Kim, Hayley E. Raymond |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Cytoplasm
Viral budding Population Biophysics 010402 general chemistry 01 natural sciences Biochemistry Ion Channels Article Viral Matrix Proteins 03 medical and health sciences education Virus Release 030304 developmental biology 0303 health sciences education.field_of_study Chemistry Virus Assembly Cell Membrane Cell Biology Site-directed spin labeling 0104 chemical sciences Cell biology Transmembrane domain Membrane Ectodomain Influenza A virus Homotetramer |
| Zdroj: | Biochim Biophys Acta Biomembr |
| ISSN: | 1879-2642 |
| Popis: | 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 surfaceassociated 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. |
| Databáze: | OpenAIRE |
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