Membrane Transport Structure Function and Biogenesis: Structural and functional studies of interaction between plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and erythrocyte spectrin
摘要：
in infected erythrocytes (6). It interacts with erythrocyte skeletal proteins such as spectrin, actin and ankyrin (7, 8) and also with erythrocyte membrane-associated parasite protein, PfEMP1(9). PfEMP1 mediates the adhesion of parasitized erythrocytes to the vascular endothelium (10), a process strongly implicated in the pathology of cerebral malaria (11). Absence of the KAHRP protein at the erythrocyte membrane leads to a weakening of the interaction between PfEMP1 and the vascular endothelium at physiologic shear stresses (6). This decreased avidity of the interaction in the absence of KAHRP can mitigate the severity of vascular obstruction and hence complications of cerebral malaria. In contrast, little is known regarding the functional implication of KAHRP-skeletal protein interactions.
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