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Recognition of plasmodium falciparum proteins by mannan-binding lectin, a component of the human innate immune system
Jens Klabunde1, Anne-Catrin Uhlemann, Anne E Tebo
1Department of Parasitology, Institute for Tropical Medicine, University of Tübingen, Germany.
Abstract:
The mannan-binding lectin (MBL) is a serum protein, which is involved in the immune defence against viruses, bacteria and parasites. Children who have mutations in the MBL gene that lead to a MBL deficiency are more susceptible to infectious diseases and are more likely to suffer from severe malaria. In this report we investigate the interaction between MBL and the proteins of red blood cells infected with the parasite Plasmodium falciparum. Protein extracts were separated on MBL-sepharose columns. After the elution of bound material, the proteins were detected either by Western blot with human antibodies, or radioactive labelling with 35S-methionine or 3H-glucosamine. MBL recognises proteins of P. falciparum-infected erythrocytes that are immunogenic in humans, parasite-derived and glycosylated. Whether the proteins identified in the different assays are identical remains to be explored. MBL added to in vitro cultures of P. falciparum, however, does not inhibit parasite growth. The positive effect of MBL in the blood of malaria patients could be caused by detoxification of parasite products.
Insights
Mannan-binding lectin (MBL) binds to proteins on Plasmodium falciparum-infected red blood cells, potentially aiding malaria defense by detoxifying parasite products. MBL deficiency increases susceptibility to severe malaria in children.
Area of Science:
- Immunology
- Infectious Diseases
- Parasitology
Background:
- Mannan-binding lectin (MBL) is a crucial serum protein for innate immune defense against pathogens.
- MBL deficiency, caused by MBL gene mutations, elevates susceptibility to infections and severe malaria.
- Plasmodium falciparum is the parasite responsible for the most virulent form of malaria.
Purpose of the Study:
- To investigate the interaction between MBL and proteins of red blood cells infected with Plasmodium falciparum.
- To identify MBL-binding proteins on infected erythrocytes and understand their role in malaria pathogenesis.
Main Methods:
- Separation of protein extracts from infected erythrocytes using MBL-sepharose columns.
- Detection of bound proteins via Western blot and radioactive labeling (35S-methionine, 3H-glucosamine).
Main Results:
- MBL recognizes immunogenic, parasite-derived, and glycosylated proteins on P. falciparum-infected erythrocytes.
- The precise identity of MBL-recognized proteins across different assays requires further investigation.
- MBL did not inhibit P. falciparum growth in vitro.
Conclusions:
- MBL interacts with specific parasite-derived proteins on infected red blood cells.
- The protective role of MBL in malaria may involve the detoxification of parasite products rather than direct parasite inhibition.