Characterization of surface proteins and glycoproteins on red blood cells from mice infected with haemosporidia:Plasmodium bergheiinfections of BALB/c mice

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Abstract
The surface proteins and glycoproteins of red cells from P. berghei-infected blood were radioisotope labeled and compared with those of normal mouse erythrocytes using the following protein labeling probes: lactoperoxidase-catalyzed radioiodination of tyrosyl residues, periodate oxidation and NaB3H4 reduction of sialic acid and oxidation of galactosyl/N-acetylgalactosaminyl residues by galactose oxidase with subsequent NaB3H4 reduction. During P. berghei infection, new tyrosyl-labeled proteins with apparent MW (Mr) of 60,000, 54,000, 40,000 and 27,500 appeared on the surface of most, if not all, red cells in the blood. Purified multinucleate cells (mostly reticulocytes) differed only in that they also had a surface protein with Mr of 83,000. This molecule may be specific to mouse reticulocytes rather than derived from parasites. In contrast to the relatively minor changes detected with radioiodination, striking changes in glycoprotein radioisotope labeling resulted from infection. All of the red cells in infection blood of greater than 20% parasitemia lost their periodate-sensitive glycoprotein sialic acid. With some samples there was little change in glycoprotein labeling by the galactose oxidase method, provided neuraminidase was added. Modification of the exocyclic hydroxyls of sialic acid could account for this. Other blood samples exhibited a dramatic loss of galactose oxidase-dependent labeling. These observations may relate to the excessive red cell destruction of uninfected and infected cells which has been inferred in many hemosporidial infections, including malaria.

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