Plasmodium falciparum rhoptry proteins of the 140/130/110-kDa high molecular weight complex (HMWC) are secreted into the erythrocyte membrane during merozoite invasion. Epitopes of membrane-associated HMWC proteins can be detected using rhoptry-specific antibodies by immunofluorescence assays. Phospholipase treatment of ring-infected intact human erythrocytes, membrane ghosts, and inside-out vesicles results in the release of the HMWC as demonstrated by immunoblotting. We characterized the membrane-associating properties of the 110-kDa protein in more detail. PLA from three different sources; bee venom, Naja naja venom, and porcine pancreas, were examined and all were equally effective in releasing the 1l0-kDa protein. Furthermore, PLA ac...
Detergent resistant membranes (DRMs) of Plasmodium falciparum merozoites contain a large number of g...
The successful invasion of Plasmodium falciparum depends on the recognition of host cell receptors b...
The profound changes in the morphology, antigenicity, and functional properties of the host erythroc...
During Plasmodium faciparum merozoite invasion into human and mouse erythrocytes, a 110-kDa rhoptry ...
We report on the characterization of monoclonal antibodies against Plasmodium falciparum schizonts, ...
The rhoptry is an organelle of the malarial merozoite which has been suggested to play a role in par...
PubMedID: 3309942We describe antigens of Plasmodium falciparum recognised by murine monoclonal antib...
We studied the effects of membrane modulation on the interaction of Plasmodium falciparum rhoptry pr...
The identification of sequences involved in binding to erythrocytes is an important step for underst...
ABSTRACT. To investigate in more detail the structure of the high molecular weight rhoptry protein c...
During blood-stage infection by Plasmodium falciparum, merozoites invade RBCs. Currently there is li...
Rhoptry proteins of Plasmodium falciparum merozoites, of 140, 130, and 110 kDa, identified by co-pre...
The identification of proteins present on the surface of Plasmodium falciparum-infected red blood ce...
Abstract Background Plasmodium falciparum merozoites expose at their surface a large protein complex...
Thesis (Ph. D.)--University of Hawaii at Manoa, 1992.Includes bibliographical references (leaves 126...
Detergent resistant membranes (DRMs) of Plasmodium falciparum merozoites contain a large number of g...
The successful invasion of Plasmodium falciparum depends on the recognition of host cell receptors b...
The profound changes in the morphology, antigenicity, and functional properties of the host erythroc...
During Plasmodium faciparum merozoite invasion into human and mouse erythrocytes, a 110-kDa rhoptry ...
We report on the characterization of monoclonal antibodies against Plasmodium falciparum schizonts, ...
The rhoptry is an organelle of the malarial merozoite which has been suggested to play a role in par...
PubMedID: 3309942We describe antigens of Plasmodium falciparum recognised by murine monoclonal antib...
We studied the effects of membrane modulation on the interaction of Plasmodium falciparum rhoptry pr...
The identification of sequences involved in binding to erythrocytes is an important step for underst...
ABSTRACT. To investigate in more detail the structure of the high molecular weight rhoptry protein c...
During blood-stage infection by Plasmodium falciparum, merozoites invade RBCs. Currently there is li...
Rhoptry proteins of Plasmodium falciparum merozoites, of 140, 130, and 110 kDa, identified by co-pre...
The identification of proteins present on the surface of Plasmodium falciparum-infected red blood ce...
Abstract Background Plasmodium falciparum merozoites expose at their surface a large protein complex...
Thesis (Ph. D.)--University of Hawaii at Manoa, 1992.Includes bibliographical references (leaves 126...
Detergent resistant membranes (DRMs) of Plasmodium falciparum merozoites contain a large number of g...
The successful invasion of Plasmodium falciparum depends on the recognition of host cell receptors b...
The profound changes in the morphology, antigenicity, and functional properties of the host erythroc...