Despite the integral role of target membrane receptor binding in viral infection, key mechanistic questions about binding remain unelucidated for many viruses. Sendai Virus (SeV), the prototypical respirovirus studied here, binds to sialic acid conjugated glycolipids and glycoproteins in the target host cell. This binding is mediated by the SeV hemagglutinin-neuraminidase (HN) protein, which also exhibits neuraminidase activity. Here, we present data examining two mechanistic questions relating to SeV binding: 1) the role of the viral size distribution on SeV binding and mobility following binding and 2) how neuraminidase inhibition influences the viral binding process. We studied these questions using single virus binding assays to supported lipid bilayers (SLBs) as well as a fluorescence spectroscopy-based neuraminidase activity assay. To examine the role of the size distribution, we produced different size distributions by size filtering, and demonstrated that different size distributions exhibit varying sensitivities to cholesterol composition in the target membrane, which can stabilize the formation of receptor nanoclusters. To study the influence of neuraminidase inhibition on SeV binding, we utilized several previously identified neuraminidase inhibitors, including N-Acetyl-2,3-didehydro-2-deoxyneuraminic acid (DANA) and suramin. We discuss the implication of these results on the relationship between the receptor binding site and the neuraminidase site as well as the role neuraminidase plays in SeV mobility and binding.

Influence of neuraminidase inhibition and viral size distribution on Sendai virus binding to supported lipid bilayers

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