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Identification of Plasmodium knowlesi erythrocyte binding proteins
L H Miller1, D Hudson, J D Haynes
1Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.
Molecular and Biochemical Parasitology
|December 1, 1988
Summary
Researchers identified Plasmodium knowlesi proteins binding to monkey and human red blood cells. A 155 kDa protein specifically binds to Old World monkey erythrocytes, distinct from the 135 kDa protein.
Area of Science:
- Malariology
- Parasitology
- Molecular Biology
Background:
- Plasmodium knowlesi, a malaria parasite of Old World monkeys, infects human Duffy blood group positive erythrocytes.
- Previous research identified a 135 kDa P. knowlesi protein binding to Duffy-positive human erythrocytes.
Purpose of the Study:
- To identify P. knowlesi proteins that bind specifically to New World monkey erythrocytes susceptible to invasion.
- To differentiate binding specificities of P. knowlesi erythrocyte-binding proteins.
Main Methods:
- Utilized New World monkey erythrocytes as reagents to screen P. knowlesi culture supernatants.
- Analyzed protein binding to erythrocytes from various monkey species, including Cebus apella (refractory).
- Characterized the binding properties of 135 kDa and 155 kDa P. knowlesi proteins.
Main Results:
- The 135 kDa protein binds to all tested New World monkey erythrocytes, including C. apella.
- A 155 kDa protein binds to all New World monkey erythrocytes except C. apella.
- The 155 kDa protein binds to Old World monkey erythrocytes but not human Duffy-positive erythrocytes.
Conclusions:
- Identified distinct Plasmodium knowlesi erythrocyte-binding proteins with varying specificities.
- The 155 kDa protein shows specific binding to the natural host erythrocytes (Old World monkeys).
- These findings represent initial steps in identifying receptor-specific parasite proteins for P. knowlesi.