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• W2013752918 abstract "The measles virus (MV) fusion apparatus consists of a fusion protein and an attachment protein named hemagglutinin (H). After receptor-binding through its cuboidal head, the H-protein transmits the fusion-triggering signal through its stalk to the fusion protein. However, the structural basis of signal transmission is unclear because only structures of H-heads without their stalk have been solved. On the other hand, the entire ectodomain structure of the hemagglutinin-neuraminidase protein of another Paramyxovirus revealed a four-helix bundle stalk. To probe the structure of the 95-residue MV H-stalk we individually substituted head-proximal residues (positions 103-153) with cysteine, and biochemically and functionally characterized the resultant proteins. Our results indicate that most residues in the central segment (positions 103-117) can be cross-linked by engineered disulfide bonds, and thus may be engaged in a tetrameric structure. While covalent tetramerization disrupts fusion triggering function, disulfide bond reduction restores it in most positions except Asp-113. The next stalk segment (residues 123-138) also has high propensity to form covalent tetramers, but since these cross-links have little or no effect on function, it can conduct the fusion-triggering signal while remaining in a stabilized tetrameric configuration. This segment may act as a spacer, maintaining H-heads at an optimal height. Finally, the head-proximal segment (residues 139-154) has very limited propensity to trap tetramers, suggesting bifurcation into two flexible linkers clamped by inter-subunit covalent links formed by natural Cys-139 and Cys-154. We discuss the modular structure of the MV H-stalk in the context of membrane fusion triggering and cell entry by Paramyxoviruses." @default.
• W2013752918 created "2016-06-24" @default.
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• W2013752918 date "2012-11-01" @default.
• W2013752918 modified "2023-10-05" @default.
• W2013752918 title "Membrane Fusion Triggering" @default.
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• W2013752918 doi "https://doi.org/10.1074/jbc.m112.410563" @default.
• W2013752918 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3493899" @default.
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• W2013752918 hasPublicationYear "2012" @default.
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