biostudies-literatureUnknown10Rui E<h4>Background</h4>In vitro cell-free systems for protein expression with extracts from prokaryotic (Escherichia coli) or eukaryotic (wheat germ) cells coupled to solid matrices have offered a valid approach for antigen discovery in malaria research. However, no comparative analysis of both systems is presently available nor the usage of suspension array technologies, which offer nearly solution phase kinetics.<h4>Methods</h4>Five Plasmodium vivax antigens representing leading vaccine candidates were expressed in the E. coli and wheat germ cell-free systems at a 50 μl scale. Products were affinity purified in a single-step and coupled to luminex beads to measure antibody reactivity of human immune sera.<h4>Results</h4>Both systems readily produced detectable proteins; proteins produced in Malaria journal192https://www.ebi.ac.uk/biostudies/studies/S-EPMC3224337biostudies-literaturePlasmodium vivax: comparison of immunogenicity among proteins expressed in the cell-free systems of Escherichia coli and wheat germ by suspension array assays.PMC3224337Rui ESanz STsuboi TFernandez-Becerra CLacerda MVdel Portillo HATakeo SfalsePlasmodium vivax: comparison of immunogenicity among proteins expressed in the cell-free systems of Escherichia coli and wheat germ by suspension array assays.<h4>Background</h4>In vitro cell-free systems for protein expression with extracts from prokaryotic (Escherichia coli) or eukaryotic (wheat germ) cells coupled to solid matrices have offered a valid approach for antigen discovery in malaria research. However, no comparative analysis of both systems is presently available nor the usage of suspension array technologies, which offer nearly solution phase kinetics.<h4>Methods</h4>Five Plasmodium vivax antigens representing leading vaccine candidates were expressed in the E. coli and wheat germ cell-free systems at a 50 μl scale. Products were affinity purified in a single-step and coupled to luminex beads to measure antibody reactivity of human immune sera.<h4>Results</h4>Both systems readily produced detectable proteins; proteins produced in 2011-01-01T00:00:00Z2011 Jul2026-04-07T19:38:25.447Z2025-07-01T03:05:46.861ZS-EPMC32243372175634910.1186/1475-2875-10-192