Plasmodium falciparum (human malaria)-induced modifications in human erythrocyte band 3 protein

Parasitology ◽  
1991 ◽  
Vol 102 (3) ◽  
pp. 335-340 ◽  
Author(s):  
I. Crandall ◽  
I. W. Sherman
Keyword(s):  
Amino Acids ◽  
Monoclonal Antibody ◽  
Plasmodium Falciparum ◽  
Geographical Origin ◽  
Band 3 ◽  
Band 3 Protein ◽  
Salt Solutions ◽  
Ionic Detergents ◽  
Results Of Treatment ◽  
Membrane Spanning

A monoclonal antibody, 1C4, was produced which recognizes a 65 kDa protein that is localized to the plasma membrane of human erythrocytes infected with Plasmodium falciparum. By immunofluorescence the antigen was visualized as dots on the surface of the infected cell. The 65 kDa protein was present in 4 strains of diverse geographical origin, and in erythrocytes infected with a knobless strain. The 65 kDa protein was insoluble in non-ionic detergents, but was partly soluble in SDS and some high (1 M) śalt solutions. The 65 kDa protein is recognized by antibodies specific for the cytoplasmic domain and the N-terminal side of the membrane-spanning region of human band 3, but was not recognized by an antibody specific to the C-terminal side of the membrane-spanning region. The results of treatment of the 65 kDa protein with trypsin and chymotrypsin are consistent with the 65 kDa protein being a truncated and covalently modified band 3 molecule which consists of the first 540 amino acids of human band 3.

scholarly journals Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter

1988 ◽  
Vol 8 (3) ◽  
pp. 1327-1335
Author(s):  
J V Cox ◽  
E Lazarides
Keyword(s):  
Amino Acids ◽  
Transmembrane Domain ◽  
Cytoplasmic Domain ◽  
Band 3 ◽  
Transporter Protein ◽  
Isolation And Characterization ◽  
Anion Transporter ◽  
Primary Structures ◽  
Membrane Spanning

Isolation and characterization of the chicken erythroid anion transporter (band 3) cDNA clone, pCHB3-1, revealed that the chicken erythroid band 3 polypeptide is 844 amino acids in length with a predicted mass of 109,000 daltons. This polypeptide is composed of a hydrophilic N-terminal cytoplasmic domain and a hydrophobic C-terminal transmembrane domain. The approximately 90 N-terminal amino acids of the human and murine erythroid band 3 polypeptides are absent in the predicted sequence of the chicken erythroid band 3 polypeptide. The absence of this very acidic N-terminal region is consistent with the lack of binding of glyceraldehyde-3-phosphate dehydrogenase to chicken erythroid band 3, as well as the relatively basic isoelectric point observed for this molecule. The remainder of the cytoplasmic domain shows little similarity to the cytoplasmic domain of the murine and human erythroid band 3, with the exception of the putative ankyrin-binding site, which is highly conserved. In contrast, the transmembrane domain of the chicken band 3 polypeptide is very similar to that of the murine erythroid and human nonerythroid band 3 polypeptides. The transmembrane domain contains 10 hydrophobic regions that could potentially traverse the membrane 12 to 14 times. In addition, a variant of chicken erythroid band 3, pCHB3-2, was cloned in which one of the hydrophobic regions of pCHB3-1 is lacking. The transcript complementary to pCHB3-2 accumulated in chicken erythroid cells in a similar manner as the transcript complementary to pCHB3-1 during embryonic development. This is the first example of a transporter protein or ion channel with alternative primary structures in its membrane-spanning segments.

Antibodies to synthetic peptides based on band 3 motifs react specifically with Plasmodium falciparum (humanmalaria)-infected erythrocytes and block cytoadherence

Parasitology ◽  
1994 ◽  
Vol 108 (4) ◽  
pp. 389-396 ◽  
Author(s):  
I. Crandall ◽  
I. W. Sherman
Keyword(s):  
Amino Acids ◽  
Plasmodium Falciparum ◽  
Synthetic Peptides ◽  
Protein Band ◽  
Significant Degree ◽  
Band 3 ◽  
Anion Transport ◽  
Amelanotic Melanoma ◽  
Murine Mabs ◽  
Antibodies To Synthetic Peptides

SUMMARYRabbit polyclonal and mouse monoclonal antibodies (Mabs) prepared against synthetic peptides patterned on exofacialloops 3 (amino acids 546–555) and 7 (821–834) of the human anion transport protein band 3 inhibited the cytoadherence of Plasmodium falciparum-infected erythrocytes to C32 amelanotic melanoma cells. Mabs directed against exofacial loop4 (amino acids 628–642) did not inhibit adherence to a significant degree. The murine Mabs recognized only P. falciparum- infected erythrocytes suggesting that the epitopes of loops 3, 4 and 7 are normally cryptic in uninfected erythrocytes.

Cytoadherence-related homologous motifs inPlasmodium falciparumantigen Pf155/RESA and erythrocyte band 3 protein

Parasitology ◽  
1995 ◽  
Vol 110 (5) ◽  
pp. 503-511 ◽  
Author(s):  
J. Iqbal ◽  
A. B. Siddique ◽  
N. Ahlborg ◽  
P. Perlmann ◽  
K. Berzins
Keyword(s):  
Plasmodium Falciparum ◽  
Cell Surface ◽  
Synthetic Peptides ◽  
Molecular Basis ◽  
Band 3 ◽  
Cell Surface Molecules ◽  
Band 3 Protein ◽  
Surface Molecules ◽  
Erythrocyte Antigen

SUMMARYCytoadherence ofPlasmodium falciparum-infected erythrocytes plays an important role in the pathogenesis of cerebral malaria. The identity of cell surface molecules on parasitized erythrocytes involved in cytoadherence is of great interest to understand the molecular basis of this mechanism. Peptide sequences derived from exofacial loops of the erythrocyte antigen band 3 from parasitized erythrocytes have previously been shown to inhibit cytoadherence. We now report that a non-repeated region of Pf155/RESA (residues 213–218) contains a hexapeptide motif being highly homologous to cytoadherence inhibitory sequences from band 3. Synthetic peptides containing the hexapeptide motif of Pf155/RESA inhibited the binding ofP.falciparum-infected erythrocytes to melanoma cellsin vitro. Furthermore, individuals residing in malaria-endemic areas have antibodies reactive with epitopes involving these motifs in band 3 and in Pf155/RESA.

scholarly journals Alternative primary structures in the transmembrane domain of the chicken erythroid anion transporter.

1988 ◽  
Vol 8 (3) ◽  
pp. 1327-1335 ◽  
Author(s):  
J V Cox ◽  
E Lazarides
Keyword(s):  
Amino Acids ◽  
Transmembrane Domain ◽  
Cytoplasmic Domain ◽  
Band 3 ◽  
Transporter Protein ◽  
Isolation And Characterization ◽  
Anion Transporter ◽  
Primary Structures ◽  
Membrane Spanning

Isolation and characterization of the chicken erythroid anion transporter (band 3) cDNA clone, pCHB3-1, revealed that the chicken erythroid band 3 polypeptide is 844 amino acids in length with a predicted mass of 109,000 daltons. This polypeptide is composed of a hydrophilic N-terminal cytoplasmic domain and a hydrophobic C-terminal transmembrane domain. The approximately 90 N-terminal amino acids of the human and murine erythroid band 3 polypeptides are absent in the predicted sequence of the chicken erythroid band 3 polypeptide. The absence of this very acidic N-terminal region is consistent with the lack of binding of glyceraldehyde-3-phosphate dehydrogenase to chicken erythroid band 3, as well as the relatively basic isoelectric point observed for this molecule. The remainder of the cytoplasmic domain shows little similarity to the cytoplasmic domain of the murine and human erythroid band 3, with the exception of the putative ankyrin-binding site, which is highly conserved. In contrast, the transmembrane domain of the chicken band 3 polypeptide is very similar to that of the murine erythroid and human nonerythroid band 3 polypeptides. The transmembrane domain contains 10 hydrophobic regions that could potentially traverse the membrane 12 to 14 times. In addition, a variant of chicken erythroid band 3, pCHB3-2, was cloned in which one of the hydrophobic regions of pCHB3-1 is lacking. The transcript complementary to pCHB3-2 accumulated in chicken erythroid cells in a similar manner as the transcript complementary to pCHB3-1 during embryonic development. This is the first example of a transporter protein or ion channel with alternative primary structures in its membrane-spanning segments.

The effects of chemical modification on the adhesion of Plasmodium falciparum-infected and uninfected erythrocytes

Parasitology ◽  
1998 ◽  
Vol 117 (6) ◽  
pp. 533-540 ◽  
Author(s):  
S. EDA ◽  
I. W. SHERMAN
Keyword(s):  
Monoclonal Antibody ◽  
Plasmodium Falciparum ◽  
Chemical Modification ◽  
Acridine Orange ◽  
Protein Band ◽  
Band 3 ◽  
Amelanotic Melanoma ◽  
Trinitrobenzene Sulfonic Acid ◽  
Infected Cells ◽  
Tyrosine Modification

Binding of Plasmodium falciparum-infected erythrocytes (PE) to endothelial cells is mediated by the erythrocyte-membrane protein, band 3-related adhesin. To determine its role, the binding of infected cells treated with various chemical modifiers was investigated. Binding was inhibited by a lysine modifier (4,4′-diisothiocyanostilbene-2,2′-di-sulfonate (DIDS)) known to specifically bind to band 3, another lysine modifier (trinitrobenzene sulfonic acid), a tyrosine modifier (sodium iodide in conjunction with lactoperoxidase, hydrogen peroxide) and oxidants (diamide, sodium periodate and ADP-chelated ferric ion), but binding was unaffected by the histidine modifier (diethylpyrocarbonate) and the arginine modifier (phenyl glyoxyl monohydrate). To artificially expose the band 3-related adhesin, uninfected erythrocytes were treated with acridine orange or loaded with calcium. These cells bound to C32 amelanotic melanoma cells, were immunostained with a monoclonal antibody that specifically binds to the band 3-related adhesin on PE, and the binding was inhibited by this monoclonal antibody. The binding of acridine orange-treated and calcium-loaded uninfected erythrocytes, could also be blocked by DIDS. In the case of acridine orange-treated erythrocytes, the patterns of the effects of the chemical modification on binding were consistent with that of PE except for tyrosine modification. These results demonstrate that the band 3-related adhesin, even in the absence of parasite-encoded proteins, contributes to PE adhesion.

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