The myriad of excreted and surface bound carbohydrate-bearing biomolecules that comprise the glycocalyx make it a complex and immense epicenter of cellular interaction. The position of the glycocalyx as the outer reach of the cell makes it a target for a multitude of pathogens infecting their host, including the persistent and ever-evolving Influenza A virus (IAV). The inherent heterogeneity and structural diversity of native glycoconjugates, as well as the lack of genetic control over glycan assembly, makes studying IAV’s multivalent sialic acid-dependent recognition of its cellular target challenging. Here, we utilize synthetic glycopolymers that mimic native biomolecules to remodel cell surfaces to better study the glycoconjugate's impact on IAV recognition. These lipidated sialylated-glycopolymers allow for effective and controlled remodeling of the glycocalyx as detected by lectin staining, and importantly, these materials are also able to restore IAV adhesion to sialic acid deficient cells. With continued characterization of this glycomaterial-based system, we aim to better decipher structural features that enhance IAV’s primary binding event to host cells.

Glycocalyx remodeling with sialylated-glycomaterials to probe the role of glycan presentation on influenza A host recognition

256th National Meeting (2018)

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