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Stage-specific proteins of the avian malaria Plasmodium lophurae

Published online by Cambridge University Press:  06 April 2009

I. W. Sherman  and
Linda Tanigoshi
I. W. Sherman
Affiliation:
Department of Biology, University of California, Riverside CA 92521
Linda Tanigoshi
Affiliation:
Department of Biology, University of California, Riverside CA 92521
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Summary

The proteins in the soluble and membrane fractions of Plasmodium lophurae, separated by SDS-PAGE and stained with Coomassie blue, were distinct from one another and different from the soluble and membrane proteins of the host cell, the duckling erythrocyte. Pulse-labelling of malaria-infected red cells containing schizonts or trophozoites with [14C]isoleucine, followed by parasite isolation, SDS-PAGE and autoradiography, showed a pattern of incorporation into soluble proteins identical to the banding pattern of gels stained with Coomassie blue. On autoradiograms, the banding patterns of the membrane proteins of trophozoites and schizonts labelled with [14C]isoleucine were similar. No qualitative differences in the soluble proteins of trophozoites and schizonts were apparent when isoleucine was used as the radiotracer; however, the banding pattern of membrane and soluble proteins labelled with [14C]isoleucine were distinct from each other. The banding pattern of soluble proteins, after staining with Coomassie blue, was distinctly different from the array of bands seen after autoradiography of parasites derived from infected cells pulse-labelled with [14C]histidine. Only small amounts of contaminating haemoglobin in the soluble protein fraction of parasites were labelled with histidine; the membrane fraction, on the other hand, had high incorporation into a single 43 kDalton band, the histidine-rich protein. No band differences, either in the membrane or soluble fractions, were observed in autoradiograms after pulse-labelling trophozoites and schizonts with [14C]histidine. The most consistent and distinct differences in protein synthesis were seen in P. lophurae pulse-labelled with [14C]proline. Autoradiograms of both soluble and membrane fractions showed the presence of bands unique to the trophozoite and schizont–stage-specific proteins.

Type
Research Article
Information
Parasitology , Volume 86 , Issue 2 , April 1983 , pp. 211 - 220
Copyright
Copyright © Cambridge University Press 1983

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