Phosphate Contaminant Detection in Water Through a Paper-based Microfluidic Device

This report describes a project aimed at developing a low-cost, portable, on-site, user-friendly system for detecting different concentrations of phosphate in drinking water. Phosphate is a natural chemical, but toxic in large concentrations; detection is therefore important to avoid drinking contaminated water. Despite this fact, no cheap, and/or nontoxic system for phosphate detection is yet on the market. The detection system utilizes a paper-based microfluidic device to automate the electrochemical detection process, which normally requires expert use of lab equipment. When combined with a portable potentiostat that works with a mobile app, the device will allow untrained users to determine if any source of drinking water contains unsafe levels of phosphate without equipment or training, and to communicate that information to a central database for further analysis. Those of any background, particularly in developing countries, will be able to maintain health and raise awareness about clean water. Microfluidic devices are useful tools for the detection of water contaminants, but there is a gap in technology for the detection of phosphate. Our phosphate detection system is a paper-based microfluidic device with an already-developed voltammetry device that automates the detection process so that any user can safely find phosphate in water. The system will provide a binary analysis about whether the water is safe to consume or not. Completion of the project provides a valuable tool to both average customers in developing countries and scientific researchers in determining the safety of drinking water

Molecular definition of multiple sites of antibody inhibition of malaria transmission-blocking vaccine antigen Pfs25.

The Plasmodium falciparum Pfs25 protein (Pfs25) is a leading malaria transmission-blocking vaccine antigen. Pfs25 vaccination is intended to elicit antibodies that inhibit parasite development when ingested by Anopheles mosquitoes during blood meals. The Pfs25 three-dimensional structure has remained elusive, hampering a molecular understanding of its function and limiting immunogen design. We report six crystal structures of Pfs25 in complex with antibodies elicited by immunization via Pfs25 virus-like particles in human immunoglobulin loci transgenic mice. Our structural findings reveal the fine specificities associated with two distinct immunogenic sites on Pfs25. Importantly, one of these sites broadly overlaps with the epitope of the well-known 4B7 mouse antibody, which can be targeted simultaneously by antibodies that target a non-overlapping site to additively increase parasite inhibition. Our molecular characterization of inhibitory antibodies informs on the natural disposition of Pfs25 on the surface of ookinetes and provides the structural blueprints to design next-generation immunogens

Molecular definition of multiple sites of antibody inhibition of malaria transmission-blocking vaccine antigen Pfs25.

The Plasmodium falciparum Pfs25 protein (Pfs25) is a leading malaria transmission-blocking vaccine antigen. Pfs25 vaccination is intended to elicit antibodies that inhibit parasite development when ingested by Anopheles mosquitoes during blood meals. The Pfs25 three-dimensional structure has remained elusive, hampering a molecular understanding of its function and limiting immunogen design. We report six crystal structures of Pfs25 in complex with antibodies elicited by immunization via Pfs25 virus-like particles in human immunoglobulin loci transgenic mice. Our structural findings reveal the fine specificities associated with two distinct immunogenic sites on Pfs25. Importantly, one of these sites broadly overlaps with the epitope of the well-known 4B7 mouse antibody, which can be targeted simultaneously by antibodies that target a non-overlapping site to additively increase parasite inhibition. Our molecular characterization of inhibitory antibodies informs on the natural disposition of Pfs25 on the surface of ookinetes and provides the structural blueprints to design next-generation immunogens