A monoclonal antibody generated against synthetic peptides patterned on amino acids 542-555 of human band 3, designated 1F4, specifically immunostained Plasmodium falciparum-infected erythrocytes and inhibited the cytoadherence of P. 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 of P. falciparum-infected erythrocytes may result from a change in the surface topography of human band 3 protein.

Guthrie, N., Crandall, I., Marini, S., Fasciglione, G., Sherman, I. (1995). 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), 117-123.

MONOCLONAL-ANTIBODIES THAT REACT WITH HUMAN BAND-3 RESIDUES-542-555 RECOGNIZE DIFFERENT CONFORMATIONS OF THIS PROTEIN IN UNINFECTED AND PLASMODIUM-FALCIPARUM-INFECTED ERYTHROCYTES

MARINI, STEFANO;FASCIGLIONE, GIOVANNI;
1995-01-01

Abstract

A monoclonal antibody generated against synthetic peptides patterned on amino acids 542-555 of human band 3, designated 1F4, specifically immunostained Plasmodium falciparum-infected erythrocytes and inhibited the cytoadherence of P. 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 of P. falciparum-infected erythrocytes may result from a change in the surface topography of human band 3 protein.
1995
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
HUMAN BAND 3 PROTEIN; PLASMODIUM FALCIPARUM; CYTOADHERENCE; MONOCLONAL ANTIBODY; EPITOPE CONFORMATION
Guthrie, N., Crandall, I., Marini, S., Fasciglione, G., Sherman, I. (1995). 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), 117-123.
Guthrie, N; Crandall, I; Marini, S; Fasciglione, G; Sherman, I
Articolo su rivista
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/53095
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