POLYLACTOSAMINES ARE NOT OBLIGATE RECEPTORS FOR INVASION OF PLASMODIUM-FALCIPARUM MALARIA AS SHOWN IN HEMPAS VARIANT-II-GAL(-) ERYTHROCYTES

被引:6
作者
DHUME, ST
ADAMSBURTON, CR
SHUMAK, KH
LAINE, RA
机构
[1] LOUISIANA STATE UNIV,LOUISIANA AGR CTR,DEPT BIOCHEM,BATON ROUGE,LA 70803
[2] UNIV TORONTO,TORONTO,ON M5S 1A8,CANADA
关键词
HEMPAS; MALARIA; PLASMODIUM FALCIPARUM; POLYLACTOSAMINE;
D O I
10.1093/glycob/4.6.903
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A HEMPAS (hereditary erythroblastic multinuclearity with positive acidified serum test) erythrocyte, atypical Variant II (referred to herein as Variant II-gal(-)), lacking long-chain polylactosamine on both glycoproteins (Band 3 and 4.5) and glycosphingolipids, was characterized by the carbohydrate profile of the erythrocyte membrane according to Fukuda et al, (Blood, 73, 1331-1339, 1989). Two laboratories previously reported that polylactosamine isolated from the erythrocyte protein Band 3 inhibited invasion of red blood cells by Plasmodium falciparum in malarial culture, suggesting a role for this carbohydrate in adhesion of the parasite, Therefore, HEMPAS erythrocyte Variant II-gal(-) presented a unique opportunity to further examine this premise, Freshly drawn blood samples (normal and HEMPAS Variant II-gal(-)) were separately incubated with P. falciparum from mannitol-synchronized cultures. The parasite was found to invade HEMPAS Variant II-gal(-) erythrocytes at a 30% lower rate through two life cycles, as shown by microscopic evaluation of invasion and by [H-3]hypoxanthine incorporation into parasite, This observation, along with the published fact that glycophorin-deficient M(k)M(k) cells are also infectable, but at a lower rate, indicates that neither sialoglycoproteins nor polylactosamines are an obligate adhesive ligand for P. falciparum, although the possibility remains that either may still contribute to adhesive events during infection.
引用
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页码:903 / 908
页数:6
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