Abstract
Binding sialates to hemagglutinin-neuraminidase (HN) activates (triggers) the fusion protein (F) to start the membrane fusion process of paramyxovirus, but the mechanism by which the HN and F associate with each other to induce membrane fusion is still unclear. It is noteworthy to study the interaction domains of HN and F of paramyxovirus. To screen interacting domains of the HN and F proteins of Avian parainfluenza virus-2 (APIV-2) and identify the structure of binding proteins, the GST pull-down assay and mass spectroscopy (MS) and circular dichroism (CD) experiments were performed in this study. The study revealed that the globular head region of HN protein tends to form a complex with either the heptad repeat 1 (HR1) or the heptad repeat 2 (HR2) of F protein respectively. This paper discusses the novel fusion mechanism induced by paramyxovirus HN and F proteins.
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Wang, X., Zhang, G., Zhao, J. et al. Interacting domains of the HN and F Proteins of paramyxovirus. Chin. Sci. Bull. 50, 2598–2601 (2005). https://doi.org/10.1007/BF03183657
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DOI: https://doi.org/10.1007/BF03183657