Submicrometer pore-based characterization and quantification of antibody-virus interactions.

This paper describes the use of a submicrometer pore-based resistive-pulse sensor to 1) detect a specific virus or a virusspecific antibody in solution, 2) probe the ability of an antibody to immunoprecipitate the virus, 3) determine the number of antibodies bound to individual virus particles, and 4) monitor the assembly of nanoparticles onto templates (here antibodies onto viruses) in situ. The assay is label-free, examines viruses in their native, assembled state, and requires no immobilization or modification of the virus or antibody. It functions by detecting the difference in the peak amplitudes of resistive pulses that occur when viruses with and without antibody bound pass through a submicrometer pore. This technique made it possible to monitor quantitatively the time-course of the binding of an antibody to a nonpathogenic virus, the icosahedrical Paramecium bursaria chlorella virus (PBCV-1) with a diameter of 190 nm. [1] We found that the maximum number of antibodies that were able to bind to PBCV-1 was 4200 450. Due to its small footprint and its simple detection scheme, submicrometer pore-based sensing of antibody–virus interactions may enable portable or high-throughput immunoassays for diagnostics and biodefense. The ability to determine the number of antibodies

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