Journal
JOURNAL OF CELL SCIENCE
Volume 118, Issue 5, Pages 1091-1098Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.01662
Keywords
hemoglobin C; malaria; band 3 clustering; quantum dots; power spectrum; autocorrelation; membrane modification
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The molecular stability of hemoglobin is critical for normal erythrocyte functions, including oxygen transport. Hemoglobin C (HbC) is a mutant hemoglobin that has increased oxidative susceptibility due to an amino acid substitution (beta 6: Glu to Lys). The growth of Plasmodium falciparuin is abnormal in homozygous CC erythrocytes in vitro, and CC individuals show innate protection against severe P falciparuin malaria. We investigated one possible mechanism of innate protection using a quantum dot technique to compare the distribution of host membrane band 3 molecules in genotypically normal (AA) to CC erythrocytes. The high photostability of quantum dots facilitated the construction of 3D cell images and the quantification of fluorescent signal intensity. Power spectra and 1D autocorrelation analyses showed band 3 clusters on the surface of infected AA and CC erythrocytes. These clusters became larger as the parasites matured and were more abundant in CC erythrocytes. Further, average cluster size (500 nm) in uninfected (native) CC erythrocytes was comparable with that of parasitized AA erythrocytes but was significantly larger (1 mu m) in parasitized CC erythrocytes. Increased band 3 clustering may enhance recognition sites for autoantibodies, which could contribute to the protective effect of hemoglobin C against malaria.
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