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In Vitro Assay of Plasmodium-Infected Red Blood Cell Killing by Cytotoxic Lymphocytes
Published on: August 17, 2022
B-cell activity in children with malaria.
Jackson C Korir1, Japhet K Magambo, Joseph K Mwatha
1Walter Reed Project/Kenya Medical Research Institute, Kisumu, Kenya.
Malaria Journal
|March 13, 2012
Summary
Severe malaria anaemia involves increased B-cell proliferation and complement deposition, leading to the loss of B-cell CD21. This membrane-bound CD21 loss, crucial in malaria pathophysiology, is not due to classical enzymatic cleavage.
Area of Science:
- Immunology
- Hematology
- Infectious Diseases
Background:
- Red blood cell (RBC) complement regulatory proteins (CR1 and CD55) deficiency is linked to malarial anemia.
- This study investigates the role of B cell CD21, which shares functional similarities with RBC CR1, in malaria.
Purpose of the Study:
- To explore the involvement of B cell CD21 in the pathophysiology of severe malaria anemia (SMA).
- To compare B cell characteristics, including CD21 expression and complement deposition, between children with SMA and uncomplicated malaria (UM).
Main Methods:
- Case-control study in Kenya involving children with SMA and UM.
- Flow cytometry assessed B cell numbers (CD20+), CD21 expression, and C3dg deposition.
- ELISA measured soluble CD21 (sCD21) levels.
- Paired t tests were used for statistical analysis.
Main Results:
- Children with SMA exhibited higher lymphocyte counts and a greater number/percentage of activated B cells (CD20+).
- SMA patients showed significantly lower median fluorescence intensity of membrane-bound CD21 and increased C3dg deposition on B cells.
- Soluble CD21 levels were unexpectedly lower in SMA patients, suggesting CD21 shedding without release into circulation.
Conclusions:
- B cell involvement, characterized by increased proliferation, complement deposition, and loss of membrane-bound CD21, is implicated in severe malaria pathophysiology.
- The observed loss of CD21 on B cells in SMA is likely mediated by complement and does not follow classical enzymatic cleavage pathways.

