MONOCLONAL-ANTIBODIES THAT REACT WITH HUMAN BAND-3 RESIDUES-542-555 RECOGNIZE DIFFERENT CONFORMATIONS OF THIS PROTEIN IN UNINFECTED AND PLASMODIUM-FALCIPARUM-INFECTED ERYTHROCYTES
N. Guthrie et al., MONOCLONAL-ANTIBODIES THAT REACT WITH HUMAN BAND-3 RESIDUES-542-555 RECOGNIZE DIFFERENT CONFORMATIONS OF THIS PROTEIN IN UNINFECTED AND PLASMODIUM-FALCIPARUM-INFECTED ERYTHROCYTES, Molecular and cellular biochemistry, 144(2), 1995, pp. 117-123
A monoclonal antibody generated against synthetic peptides patterned o
n amino acids 542-555 of human band 3, designated 1F4, specifically im
munostained Plasmodium falciparum-infected erythrocytes and inhibited
the cytoadherence of P. falciparum-infected erythrocytes to C32 amelan
otic melanoma cells. 1F4 did not recognize intact band 3 protein on im
munoblots, however it was reactive towards proteolytic fragments of ba
nd 3. The binding region of another murine monoclonal antibody previou
sly reported to recognize the membrane spanning domain of human band 3
, designated B6, was found to also recognize residues 542-555, however
its properties differed from 1F4. Mab B6 recognized both infected and
uninfected red cells, and reacted only with intact band 3 on immunobl
ots. Mab B6 was without effect on cytoadherence. These results demonst
rate that monoclonal antibodies reactive against a common peptide sequ
ence may bind to different conformations of the peptide sequence and s
uggest that the adherent competency of P. falciparum-infected erythroc
ytes may result from a change in the surface topography of human band
3 protein.