The Role of Glycoproteins in the Life Cycle of the Cellular Slime Mold Dictyostelium discoideum

Henderson, Ellen J.

doi:10.1007/978-1-4684-7464-0_7

Cited by 12 publications

(5 citation statements)

References 165 publications

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“…The occurrence of a novel "intersecting" GlcNAc residue and a partial characterization of its sugar transferase has been described [Couso et al, 1987;Sharkey and Kornfeld, 19891. The presence of peripheral and core fucose residues on N-linked oligosaccharides has been reported, but these have not been structurally characterized to date [Henderson, 1984;Ivatt et al, 19841. During development, the structure of the N-linked oligosaccharides changes dramatically [Ivatt et al, 1984;Knecht et al, 1985;Moore et al, 1985;Judelson and Dimond, 1988bl. A set of two neutral pH a-mannosidases is expressed that is probably responsible for generating smaller, more highly trimmed sugar chains [Sharkey and Kornfeld, 19851.…”

Section: N-linked Oligosaccharides Biosynthesis and Structurementioning

confidence: 99%

Biochemical and genetic analysis of an antigenic determinant found on N‐linked oligosaccharides in Dictyostelium

1990

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Dictyostelium discoideum synthesizes many highly immunogenic carbohydrates of unknown structure and function. We have used monoclonal antibodies prepared against one of these called CA1 to investigate its structure and the consequences of its loss. CA1 is preferentially expressed on lysosomal enzymes as a specific arrangement of mannose-6-SO4 residues on N-linked oligosaccharides. Mutant strains HL241 and HL243 do not express CA1, and synthesize a truncated lipid-linked oligosaccharide (LLO) precursor that lacks the critical mannose residues needed for expression. The lesion appears to result from the loss of mannosyl transferase activity involved in LLO biosynthesis. The truncated LLO is poorly transferred to an artificial peptide acceptor in a cell-free N-glycosylation assay, and this appears to result from improper topological localization of the LLO or to a lower affinity of the LLO for the oligosaccharyl transferase. Although both mutants share these lesions, they are biochemically and genetically distinct. Only HL243 is lower in N-glycosylation in intact cells, and this is not a result of an altered structure of the LLO. There are other differences between the strains. HL241 can form fruiting bodies at a slower rate than normal while HL243 cannot aggregate. Genetic analysis of defects shows that the CA1 lesion in HL241 is recessive, while the lesion in both CA1 and in development are dominant and co-segregate in HL243 and are, therefore, likely to be in the same gene. Lysosomal enzyme targeting is normal but enzyme processing proceeds at a 2-3 fold slower rate in HL241 and HL243 compared to wild-type. Strain HL244 does not express CA1 since it completely lacks protein sulfation, but lysosomal enzyme targeting and processing proceeds at a normal rate, showing that sulfate is not essential for these processes. Alterations in oligosaccharide structure can have individualized effects on the biosynthesis of lysosomal enzymes. The results presented here illustrate how this approach can be used to study both the structure and function of carbohydrate epitopes.

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Section: N-linked Oligosaccharides Biosynthesis and Structurementioning

confidence: 99%

Biochemical and genetic analysis of an antigenic determinant found on N‐linked oligosaccharides in Dictyostelium

1990

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“…During development the pattern of glycosylation changes dramatically (39,45,46). The N-linked oligosaccharides are still derived from the lipidlinked precursor, but many of them are highly processed by the removal of a large portion of the Man residues (39).…”

Section: General Features Of Protein Glycosylation In Dictyosteliummentioning

confidence: 99%

Modifications of lysosomal enzymes in Dictyostelium discoideum

Freeze¹

1986

Mol Cell Biochem

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This paper has two purposes. The first is to review the past studies on the structure, biosynthesis, and immunological properties of a class of glycoproteins, the lysosomal enzymes, in Dictyostelium discoideum. The second purpose is to present new data on the analysis of mutant strains altered in the biosynthesis of the lipid-linked precursor of N-linked oligosaccharides, and on the characterization of new carbohydrate antigenic determinants found on multiple proteins in Dictyostelium. We will also show how a combination of genetic, biochemical and immunochemical approaches have been used to unravel a portion of the glycosylation pathway in Dictyostelium. The long-term goal of these studies is to use Dictyostelium discoideum as a model system to understand the functions of a variety of glycoconjugates in a multicellular organism. The existence of a large number of mutant strains which are altered in a variety of cellular functions, development and the posttranslational modification of multiple proteins, offers a great opportunity to explore this area.

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“…In growing D. tliscoideum cells about 50% of structures are endo-H resistant and are radio-labelled with fucose, unlike the Endo-H sensitive structures (Ivatt et al, 1981(Ivatt et al, , 1984. This has been interpreted as fucosylation on the core N-acetylglucosamine residues (Henderson, 1984). This conclusion is supported by the detection of fucose in neutral Endo-H resistant oligosaccharides, but fucosylation does not appear to account for all the Endo-H resistance as charged oligosaccharides contained little fucose (Freeze and Wolgast, 1986).…”

Section: Glycosylation Of Proteins In Dictyosteliul1l Discoidellmmentioning

confidence: 98%

Expression of Recombinant Glycoproteins in the Simple EukaryoteDictyostelium discoideum

Slade

Emslie

Williams

1997

Biotechnology and Genetic Engineering Reviews

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The Role of Glycoproteins in the Life Cycle of the Cellular Slime Mold Dictyostelium discoideum

Cited by 12 publications

References 165 publications

Biochemical and genetic analysis of an antigenic determinant found on N‐linked oligosaccharides in Dictyostelium

Biochemical and genetic analysis of an antigenic determinant found on N‐linked oligosaccharides in Dictyostelium

Modifications of lysosomal enzymes in Dictyostelium discoideum

Expression of Recombinant Glycoproteins in the Simple EukaryoteDictyostelium discoideum

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