Reticulocyte-binding protein homologue 1 is required for sialic acid-dependent invasion into human erythrocytes by Plasmodium falciparum

被引:126
作者
Triglia, T [1 ]
Duraisingh, MT [1 ]
Good, RT [1 ]
Cowman, AF [1 ]
机构
[1] Walter & Eliza Hall Inst Med Res, Melbourne, Vic 3050, Australia
关键词
D O I
10.1111/j.1365-2958.2004.04388.x
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
The Apicomplexan parasite responsible for the most virulent form of malaria, Plasmodium falciparum, invades human erythrocytes through mutiple ligand-receptor interactions. Some strains of P. falciparum are sensitive to neuraminidase treatment of the host erythrocyte and these parasites have been termed sialic acid-dependent as they utilize receptors containing sialic acid. In contrast, other strains can efficiently invade neuraminidase-treated erythrocytes and hence are sialic acid-independent. The molecular interactions that allow P. falciparum to differentially utilize receptors for merozoite invasion are not understood. The P. falciparum reticulocyte-binding protein homologue (PfRh or PfRBL) family have been implicated in the invasion process but their exact role is unknown. PfRh1, a member of this protein family, appears to be expressed in all parasite lines analysed but there are marked differences in the level of expression between different strains. We have used targeted gene disruption of the PfRh1 gene in P. falciparum to show that the encoded protein is required for sialic acid-dependent invasion of human erythrocytes. The DeltaPfRh1 parasites are able to invade normally; however, they utilize a pattern of ligand-receptor interactions that are more neuraminidase-resistant. Current data suggest a strategy based on the differential function of specific PfRh proteins has evolved to allow P. falciparum parasites to utilize alternative receptors on the erythrocyte surface for evasion of receptor polymorphisms and the host immune system.
引用
收藏
页码:162 / 174
页数:13
相关论文
共 42 条
[1]   An expanding ebl family of Plasmodium falciparum [J].
Adams, JH ;
Blair, PL ;
Kaneko, O ;
Peterson, DS .
TRENDS IN PARASITOLOGY, 2001, 17 (06) :297-299
[2]   ERYTHROCYTE ENTRY BY MALARIAL PARASITES - MOVING JUNCTION BETWEEN ERYTHROCYTE AND PARASITE [J].
AIKAWA, M ;
MILLER, LH ;
JOHNSON, J ;
RABBEGE, J .
JOURNAL OF CELL BIOLOGY, 1978, 77 (01) :72-82
[3]  
ARNWELL JW, 1998, MALARIA PARASITE BIO, P93
[4]  
Baum J, 2003, GENETICS, V163, P1327
[5]   Erythrocyte invasion phenotypes of Plasmodium falciparum in the Gambia [J].
Baum, J ;
Pinder, M ;
Conway, DJ .
INFECTION AND IMMUNITY, 2003, 71 (04) :1856-1863
[6]   The major allelic dimorphisms in four Plasmodium falciparum merozoite proteins are not associated with alternative pathways of erythrocyte invasion [J].
Binks, RH ;
Conway, DJ .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1999, 103 (01) :123-127
[7]   GLYCOPHORIN-B AS AN EBA-175 INDEPENDENT PLASMODIUM-FALCIPARUM RECEPTOR OF HUMAN ERYTHROCYTES [J].
DOLAN, SA ;
PROCTOR, JL ;
ALLING, DW ;
OKUBO, Y ;
WELLEMS, TE ;
MILLER, LH .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1994, 64 (01) :55-63
[8]   Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways [J].
Duraisingh, MT ;
Maier, AG ;
Triglia, T ;
Cowman, AF .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (08) :4796-4801
[9]   Phenotypic variation of Plasmodium falciparum merozoite proteins directs receptor targeting for invasion of human erythrocytes [J].
Duraisingh, MT ;
Triglia, T ;
Ralph, SA ;
Rayner, JC ;
Barnwell, JW ;
McFadden, GI ;
Cowman, AF .
EMBO JOURNAL, 2003, 22 (05) :1047-1057
[10]   Negative selection of Plasmodium falciparum reveals targeted gene deletion by double crossover recombination [J].
Duraisingh, MT ;
Triglia, T ;
Cowman, AF .
INTERNATIONAL JOURNAL FOR PARASITOLOGY, 2002, 32 (01) :81-89