Abstract

The effect of the cell glycocalyx on the binding of a membrane receptor, classI major histocompatibility complex (MHC) human leukocyte antigen (HLA)-A2, to an immobilized anti-HLA antibody was investigated using an acoustic sensor based on a Love wave geometry. The enzyme neuraminidase was used to remove sialic acid residues from the cell glycocalyx. Real-time measurements of the amplitude of the acoustic wave showed that treatment with neuraminidase facilitates HLA/anti-HLA-mediated cell attachment via a 3.6-fold increase of the two-dimensional (2D) binding constant of the interaction. This could be attributed to better approach of binding partners due to favorable condition of the desialylated glycocalyx. The results underline the importance of microtopological factors in membrane receptor binding and reveal the potential of the Love wave sensor and 2D binding parameters for studying cell-substrate binding events.

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