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- W2989239630 abstract "Influenza virus is unique among enveloped viruses since it does not rely on the cellular ESCRT machinery for budding. Instead, viruses encode their own scission machine, the M2 protein. M2 is targeted to the edge of the viral assembly site, where it inserts an amphiphilic helix into the membrane to induce curvature. Cellular proteins utilize a similar mechanism for scission of vesicles. We show that the helix of M2 can be replaced by helices from cellular proteins with only small effects on virus replication. No evidence was obtained that budding is disturbed, but individual mutants exhibit other defects in M2 that explain the reduced virus titers. In contrast, no virus could be generated if the helix of M2 is deleted or replaced by irrelevant sequences. These experiments support the concept that M2 requires an amphiphilic helix to induce membrane curvature, but its biophysical properties are more important than the amino acid sequence." @default.
- W2989239630 created "2019-11-22" @default.
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- W2989239630 date "2020-01-17" @default.
- W2989239630 modified "2023-10-17" @default.
- W2989239630 title "Amphipathic Helices of Cellular Proteins Can Replace the Helix in M2 of Influenza A Virus with Only Small Effects on Virus Replication" @default.
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- W2989239630 doi "https://doi.org/10.1128/jvi.01605-19" @default.
- W2989239630 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7000973" @default.
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