Expression & Purification of Recombinant Plasmodium falciparum Erythrocyte-binding Ligands

Plasmodium falciparum, the most virulent malarial parasite, is capable of invading all known human blood types. Erythrocyte invasion depends on specific parasite ligand and erythrocyte receptor interactions. These interactions are mediated by Region II of the P. falciparum erythrocyte binding ligands. Although invasion does not seem dependent upon a singular ligand, their individual contributions to the invasion process are yet to be explained. In this study, Region II of P. falciparum binding ligands BAEBL and JESEBL were transiently expressed as hexahistidyl recombinant proteins in COS-1 cells. Purification by column chromatography yielded 0.52 mg of BAEBL and 0.433 mg of JESEBL. The production and purification of these recombinant hexahistidyl proteins can allow for future binding affinity and kinetic analysis that may eventually define the contributive roles of each ligand during erythrocyte invasion.

Name thesis:degree_name

Master of Science

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Biology

Year dc:date.available

2010

Author dc:creator

• Cofie, Seward Joann

Contributors dc:contributor

• D. C. Ghislaine Mayer

• Erythrocyte-binding Ligands
• Plasmodium falciparum
• recombinant
• hexahistidyl
• Biology
• Life Sciences

Statement dc:rights

• © The Author

Identifier

https://scholarscompass.vcu.edu/etd/90

OAI identifier oai:identifier

oai:scholarscompass.vcu.edu:etd-1089