Presence of O-glycosylated glycoproteins in the Plasmodium falciparum parasite

Dayal-Drager, Renu; Hoessli, Daniel C.; Decrind, C.; Guidice, Guiseppe Del; Lambert, Paul‐Henri; Nasiruddin, .

doi:10.1016/0008-6215(91)80172-j

Cited by 21 publications

(9 citation statements)

References 11 publications

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“…Labeling of MSP-1 with galactose has also been reported [69,70] and the blast search results are further strengthening these findings. However, the human mannosaminyl transferase blast search in the genomic sequence of P. falciparum uncovered eight sequences with 18% to 40% identity and 38% to 69% similarity.…”

Section: Genetic Regulation Of Glycosylationsupporting

confidence: 67%

“…The sugar residues identified by these studies include glucosamine, mannose and galactose. The presence of galactose residues has been shown by in vitro labeling [69,70] and lectin binding studies [100]. It was further shown that galactose residues are incorporated in P. falciparum proteins that bind RCA-120 [100] and Bandeirea simplicifolia lectins, suggesting the presence of galactose residues in terminal position and linked in and anomery.…”

Section: Possible Role Of Galactose In Msp-1 and Other P Falciparum mentioning

confidence: 95%

“…The existence of both N-and O-linked carbohydrates on MSP-1 and MSP-2 has been described [67][68][69][70][71][72]. Kimura and co-workers [67] have shown that N-linked carbohydrates in P. falciparum proteins constitute 70% of the total carbohydrates present.…”

Section: Genetic Regulation Of Glycosylationmentioning

confidence: 97%

“…The addition of galactose to MSP-1 was shown in vitro [69][70][71], as well as modification by O--GlcNAc [72] at serine and threonine residues. However, the expression of galactosyltransferase and OGT in P. falciparum has not been established nor has it been demonstrated that these transferases exist in the P. falciparum or in any other plasmodial genome (http://www.plasmodb.org/).…”

Section: Erythrocytic Interactions With Plasmo-dium Falciparummentioning

confidence: 99%

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Glycosylphosphatidylinositol (GPI) Anchored Proteins of Plasmodium falciparum:Antigenic Determinants and Role of Sugar Moieties in the GPI Anchor

Nasiruddin¹,

Ahmad²,

Hoessli³

et al. 2007

COC

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GPI-anchored proteins are ubiquitously expressed on eukaryotic cell surfaces and are involved in a variety of vital functions ranging from adhesion to enzymatic catalysis. This review focuses on GPI-anchored proteins in malaria and the role of carbohydrate moieties in malarial proteins. Malaria remains a formidable threat to human beings even in the twenty-first century. Malaria vaccine development to prevent morbidity and mortality has generated comprehensive molecular information on many immunologically-relevant malarial antigens but an effective anti-malaria vaccine is still unavailable. Several malarial antigenic proteins have been considered as promising vaccine candidates. Merozoite surface protein 1 (MSP-1) and merozoite surface protein 2 (MSP-2) from the asexual stages of the malarial life cycle are prominent amongst malarial antigens. Modifications of MSPs are significantly important as the natural MSPs offer better protection against malaria compared to recombinant proteins that lack post-translational modifications. Development of viable vaccine(s) against malaria has met considerable difficulties and it is likely that the lack of post-translational modification may have been a contributory factor. The role of galactose residues in MSP-1 is reviewed in this article.

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Section: Genetic Regulation Of Glycosylationsupporting

confidence: 67%

Section: Possible Role Of Galactose In Msp-1 and Other P Falciparum mentioning

confidence: 95%

Section: Genetic Regulation Of Glycosylationmentioning

confidence: 97%

Section: Erythrocytic Interactions With Plasmo-dium Falciparummentioning

confidence: 99%

See 2 more Smart Citations

Glycosylphosphatidylinositol (GPI) Anchored Proteins of Plasmodium falciparum:Antigenic Determinants and Role of Sugar Moieties in the GPI Anchor

Nasiruddin¹,

Ahmad²,

Hoessli³

et al. 2007

COC

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“…Several proteins of erythrocytic stage P. falciparum are known to contain carbohydrates (12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23). The deduced amino acid sequences of the parasite proteins have potential N-glycosylation sites (7, 24 -26).…”

mentioning

confidence: 99%

Glycosylphosphatidylinositol Anchors Represent the Major Carbohydrate Modification in Proteins of Intraerythrocytic Stage Plasmodium falciparum

Gowda

Gupta

Davidson

1997

Journal of Biological Chemistry

135

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The nature and extent of carbohydrate modification in intraerythrocytic stage Plasmodium falciparum proteins have been controversial. This study describes the characterization of the carbohydrates in intraerythrocytic P. falciparum proteins and provides an overall picture of the nature of carbohydrate modification in the parasite proteins. P. falciparum strains were metabolically labeled with radioactive sugar precursors and ethanolamine at different developmental stages. The individual parasite proteins separated on SDS-polyacrylamide gels and whole parasite cell lysates were analyzed for the carbohydrate moieties. The results established the following: 1) glycosylphosphatidylinositol (GPI) anchors represent the major carbohydrate modification in the intraerythrocytic stage P. falciparum proteins; 2) in contrast to previous reports, O-linked carbohydrates are either absent or present only at very low levels in the parasite; and 3) P. falciparum contains low levels of N-glycosylation capability. The amount of N-linked carbohydrates in whole parasite proteins is ϳ6% compared with the GPI anchors attached to proteins based on radioactive GlcN incorporated into the proteins.The glycan cores of multiple parasite protein GPI anchors are all similar, consisting of protein-ethanolamine-phosphate-(Man␣1-2)6Man␣1-2Man␣1-6Man␣1-4GlcN. The fourth Man residues distal to GlcN of the GPI anchor glycan cores contain unidentified substituents that are susceptible to conditions of nitrous acid deamination. This unusual structural feature may contribute to the reported pathogenic properties of the P. falciparum GPI anchors.Malaria, a life-threatening disease caused by parasitic protozoa of the genus Plasmodium, is a major health problem throughout the tropical and subtropical regions of the world. Among the four species that infect humans, Plasmodium falciparum is the most virulent. New approaches such as vaccine development and novel therapeutic agents are urgently needed due to the emergence of parasite strains resistant to chloroquine and other commonly used drugs (1).Vaccines based on antigens of the blood stage parasite are under intensive study. A major focus has been on synthetic peptides or recombinant proteins of cell surface antigens (2-6). However, this approach has not been highly effective, although immunization with native cell surface proteins purified from the erythrocytic stage parasite is known to confer significant protective immunity (7-10). It is plausible that post-translational modifications play an important role in antigenicity. Accordingly, a basic understanding of such modifications may assist in the development of effective vaccines.Glycosylation is an often extensive post-translational modification of eukaryotic proteins. Carbohydrate moieties of glycoproteins perform a variety of functions including modulation of immunological properties, receptor-ligand interactions, sorting and localization of proteins, cell adhesion, and cell-cell communication (11). In addition, they contribute to protein conform...

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The biochemistry ofPlasmodium falciparum

Ginsburg

2016

Advances in Malaria Research

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Presence of O-glycosylated glycoproteins in the Plasmodium falciparum parasite

Cited by 21 publications

References 11 publications

Glycosylphosphatidylinositol (GPI) Anchored Proteins of Plasmodium falciparum:Antigenic Determinants and Role of Sugar Moieties in the GPI Anchor

Glycosylphosphatidylinositol (GPI) Anchored Proteins of Plasmodium falciparum:Antigenic Determinants and Role of Sugar Moieties in the GPI Anchor

Glycosylphosphatidylinositol Anchors Represent the Major Carbohydrate Modification in Proteins of Intraerythrocytic Stage Plasmodium falciparum

The biochemistry ofPlasmodium falciparum

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