Lactate dehydrogenase and the diagnosis of malaria

Parasitol Today. 1998 Sep;14(9):376-7. doi: 10.1016/s0169-4758(98)01284-8.

Abstract

Over the past five years, several methods have been developed that exploit the differences between Plasmodium lactate dehydrogenase (pLDH) and the human LDH isoforms for the purposes of measuring pLDH in blood and in in vitro cultures. These methods have been incorporated into an easy screening method for the identification and quantitation of parasite growth in in vitro cultures using a Malstattrade mark reagent. In addition, another quantitative microplate method, the immunocapture pLDH (IcpLDH) assay, has been developed that utilizes monoclonal antibodies (mAbs) to capture the pLDH and then to measure the captured enzyme by its ability to reduce 3 acetyl pyridine adenine dinucleotide (APAD). In addition, a rapid immunochromatographic method, the OptiMAL® assay, has been formatted to capture pLDH as an antigen, and then to signal the presence of this captured antigen (enzyme) with a colloid conjugated antibody. The microplate IcpLDH assay, and the dipstick OptiMAL® assays, are both being used for the diagnosis and monitoring of malaria infections, as described here by Michael Makler, Rob Piper and Wil Milhous.