EBA-175 binds its receptor sialic acids on glycophorin A when invading erythrocytes. The receptor-binding region (RII) contains two cysteine-rich domains with similar cysteine motifs (F1 and F2). Functional relationships between F1 and F2 domains and characterization of EBA-175 were studied using specific monoclonal antibodies (mAbs) against these domains..The role of the F1 and F2 domains in erythrocyte invasion and binding was elucidated with mAbs. These mAbs interfere with native EBA-175 binding to erythrocyte in a synergistic fashion. The stage specific expression of EBA-175 showed that the primary focus of activity was the merozoite stage. A recombinant RII protein vaccine consisting of both F1 and F2 domains that could induce synergi...
<div><p>Disrupting erythrocyte invasion by <i>Plasmodium falciparum</i> is an attractive approach to...
<p>Monoclonal antibody sensograms show binding to immobilized EBA-175 RII with the concentrations of...
Plasmodium falciparum causes the most virulent form of malaria and remains a major worldwide health ...
EBA-175 binds its receptor sialic acids on glycophorin A when invading erythrocytes. The receptor-b...
A 175-kilodalton erythrocyte binding protein, EBA-175, of the parasite Plasmodium falciparum mediate...
Erythrocyte binding antigen 175 (EBA-175) is a P. falciparum protein that binds the major glycoprote...
The malaria parasite, Plasmodium falciparum, and related parasites use a variety of proteins with Du...
SummaryErythrocyte binding antigen 175 (EBA-175) is a P. falciparum protein that binds the major gly...
Malaria parasites make specific receptor-ligand interactions to invade erythrocytes. A 175 kDa Plasm...
Malaria parasites make specific receptor-ligand interactions to invade erythrocytes. A 175 kDa Plasm...
<div><p>The malaria parasite, <em>Plasmodium falciparum</em>, and related parasites use a variety of...
<p>Effects of mAbs on immunoprecipitation of [<sup>35</sup>S]-labeled parasite culture supernatant c...
SummaryErythrocyte binding antigen 175 (EBA-175) is a P. falciparum protein that binds the major gly...
Plasmodium falciparum utilizes multiple ligand-receptor interactions for invasion. The invasion liga...
<p>(A) Western blot of post-invasion culture supernatants from W2mef and W2mef175-Cterm parasites pr...
<div><p>Disrupting erythrocyte invasion by <i>Plasmodium falciparum</i> is an attractive approach to...
<p>Monoclonal antibody sensograms show binding to immobilized EBA-175 RII with the concentrations of...
Plasmodium falciparum causes the most virulent form of malaria and remains a major worldwide health ...
EBA-175 binds its receptor sialic acids on glycophorin A when invading erythrocytes. The receptor-b...
A 175-kilodalton erythrocyte binding protein, EBA-175, of the parasite Plasmodium falciparum mediate...
Erythrocyte binding antigen 175 (EBA-175) is a P. falciparum protein that binds the major glycoprote...
The malaria parasite, Plasmodium falciparum, and related parasites use a variety of proteins with Du...
SummaryErythrocyte binding antigen 175 (EBA-175) is a P. falciparum protein that binds the major gly...
Malaria parasites make specific receptor-ligand interactions to invade erythrocytes. A 175 kDa Plasm...
Malaria parasites make specific receptor-ligand interactions to invade erythrocytes. A 175 kDa Plasm...
<div><p>The malaria parasite, <em>Plasmodium falciparum</em>, and related parasites use a variety of...
<p>Effects of mAbs on immunoprecipitation of [<sup>35</sup>S]-labeled parasite culture supernatant c...
SummaryErythrocyte binding antigen 175 (EBA-175) is a P. falciparum protein that binds the major gly...
Plasmodium falciparum utilizes multiple ligand-receptor interactions for invasion. The invasion liga...
<p>(A) Western blot of post-invasion culture supernatants from W2mef and W2mef175-Cterm parasites pr...
<div><p>Disrupting erythrocyte invasion by <i>Plasmodium falciparum</i> is an attractive approach to...
<p>Monoclonal antibody sensograms show binding to immobilized EBA-175 RII with the concentrations of...
Plasmodium falciparum causes the most virulent form of malaria and remains a major worldwide health ...