ISSN:
1573-4919
Keywords:
human band 3 protein
;
Plasmodium falciparum
;
cytoadherence
;
monoclonal antibody
;
epitope conformation
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Abstract A monoclonal antibody generated against synthetic peptides patterned on amino acids 542–555 of human band 3, designated 1F4, specifically immunostainedPlasmodium falciparum-infected erythrocytes and inhibited the cytoadherence ofP. falciparum-infected erythrocytes to C32 amelanotic melanoma cells. 1F4 did not recognize intact band 3 protein on immunoblots, however it was reactive towards proteolytic fragments of band 3. The binding region of another murine monoclonal antibody previously 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 immunoblots. Mab B6 was without effect on cytoadherence. These results demonstrate that monoclonal antibodies reactive against a common peptide sequence may bind to different conformations of the peptide sequence and suggest that the adherent competency ofP. falciparum-infected erythrocytes may result from a change in the surface topography of human band 3 protein.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00944390
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