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Wright (a + b-) human erythrocytes and Plasmodium falciparum malaria
Blut
|February 1, 1985
Summary
Erythrocytes with a rare glycophorin A variant are susceptible to Plasmodium falciparum invasion, contradicting previous findings. The Wrb epitope on glycophorin A does not appear to be a distinct receptor site for parasite invasion.
Area of Science:
- Malariology
- Immunology
- Hematology
Background:
- Glycophorin A is implicated as a receptor for Plasmodium falciparum invasion.
- Previous studies suggested that certain erythrocyte variants, like Wr(a + b-), are refractory to parasite invasion.
- The Wrb epitope on glycophorin A has been proposed as a specific binding site.
Purpose of the Study:
- To investigate the susceptibility of Wr(a + b-) erythrocytes to Plasmodium falciparum invasion.
- To determine if the Wrb epitope on glycophorin A is essential for parasite invasion.
- To re-evaluate the role of glycophorin A in Plasmodium falciparum erythrocyte invasion.
Main Methods:
- Testing the invasion of nine Plasmodium falciparum isolates into Wr(a + b-) erythrocytes.
- Assessing the inhibitory effect of anti-Wrb serum on parasite invasion of O Rh- erythrocytes.
Main Results:
- Wr(a + b-) erythrocytes were fully susceptible to invasion by all tested Plasmodium falciparum isolates.
- The serum of donor M. Fr. containing anti-Wrb antibodies did not inhibit parasite invasion.
- These findings contradict previous reports of erythrocyte refractoriness.
Conclusions:
- Glycophorin A remains a likely receptor for Plasmodium falciparum, but the Wrb epitope is not a distinct receptor site.
- The refractoriness of Wr(a + b-) erythrocytes to Plasmodium falciparum invasion is not confirmed.
- This study refines our understanding of the molecular interactions during malaria parasite invasion.