Zygote giant cell differentiation in <i>Dictyostelium discoideum</i>: biochemical markers of specific stages of sexual development

Browning, Darren D.; Lewis, Keith E.; O’Day, Danton H.

doi:10.1139/o92-166

Cited by 9 publications

(6 citation statements)

References 29 publications

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“…This hypothesis is consistent with the thick glycocalyx present at the cell surface of the amoebae, poor conservation of the gp130-polypeptide sequence in related species as reported here, and evidence for extensive N-glycosylation differences among different social amoebae . Previous studies of D. discoideum have implicated glycoproteins and oligosaccharide moieties in cell adhesion, − phagocytosis and sexual development. − Classical methods and a recent mass spectrometry-based study describe major features of the D. discoideum N-glycome, but it is not known which are presented at the cell surface. Here we apply a mass spectrometry-based approach to analyze the N-glycans on a secreted recombinant version of gp130.…”

Section: Introductionsupporting

confidence: 85%

Glycopeptidome of a Heavily N-Glycosylated Cell Surface Glycoprotein of Dictyostelium Implicated in Cell Adhesion

et al. 2010

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Genetic analysis has implicated the cell surface glycoprotein gp130 in cell interactions of the social amoeba Dictyostelium, and information about the utilization of the 18 N-glycosylation sequons present in gp130 is needed to identify critical molecular determinants of its activity. Various glycomics strategies, including mass spectrometry of native and derivatized glycans, monosaccharide analysis, exoglycosidase digestion, and antibody binding, were applied to characterize a nonanchored version secreted from Dictyostelium. s-gp130 is modified by a predominant Man(8)GlcNAc(4) species containing bisecting and intersecting GlcNAc residues and additional high-mannose N-glycans substituted with sulfate, methyl-phosphate, and/or core alpha 3-fucose. Site mapping confirmed the occupancy of 15 sequons, some variably, and glycopeptide analysis confirmed 14 sites and revealed extensive heterogeneity at most sites. Glycopeptide glycoforms ranged from Man(6) to Man(9), GlcNAc(0-2) (peripheral), Fuc(0-2) (including core alpha 3 and peripheral), (SO(4))(0-1), and (MePO(4))(0-1), which represented elements of virtually the entire known cellular N-glycome as inferred from prior metabolic labeling and mass spectrometry studies. gp130, and a family of 14 related predicted glycoproteins whose polypeptide sequences are rapidly diverging in the Dictyostelium lineage, may contribute a functionally important shroud of high-mannose N-glycans at the interface of the amoebae with each other, their predators and prey, and the soil environment.

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Section: Introductionsupporting

confidence: 85%

Glycopeptidome of a Heavily N-Glycosylated Cell Surface Glycoprotein of Dictyostelium Implicated in Cell Adhesion

et al. 2010

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“…Browning et al recently identified gpl30, a WGA-binding glycoprotein that was detected in association with the sexual development of D. discoideum (30,31). Although this protein and DdFRP3 are similar in that both have WGA-binding sugar chains and the same molecular mass, we do not consider them to be identical, for the following reasons.…”

Section: Discussionmentioning

confidence: 91%

“…First, their expression levels are different; the former is detected while the latter is not detected by the lectin staining. Second, their expression period is different; GP138B is expressed in vegetative cells (13), while the gpl30 identified by Browning et al is expressed after cell fusion (30,31).…”

Section: Discussionmentioning

confidence: 99%

Isoforms of gp138, a Cell-Fusion Related Protein in Dictyostelium discoideum

Aiba

Fang

Yamaguchi

et al. 1997

Journal of Biochemistry

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Sexual development of Dictyostelium discoideum is a unique and useful system for the study of sexual phenomena. We have been studying molecular mechanisms of sexual cell fusion in D. discoideum and have identified several relevant cell-surface proteins. One of the proteins, gp138, was identified as a target molecule for fusion-blocking antibodies, and two genes for gp138, GP138A and GP138B, were cloned. The participation of gp138 in the sexual cell fusion was confirmed by antisense RNA mutagenesis, but it is unclear which of the genes encodes gp138. Moreover, the presence of a third gene for gp138 was indicated by gene disruption. In the present study, we generated strains of D. discoideum overexpressing either GP138A or GP138B to investigate the products of these genes. The transformants overexpressing GP138A and GP138B overproduced glycoproteins with molecular masses of 135 and 130 kDa, respectively. Although their molecular masses were different from that of gp138, the results of peptide mapping and amino acid sequencing showed that they are related to proteins, suggesting that the proteins encoded by GP138A and GP138B are isoforms of gp138 protein.

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“…Further, an analysis using Western blotting has shown that a glucosylated receptor appearing at the onset of phagocytosis, has a molecular weight of about 126 kDa (gp 126). A WGA-binding glycoprotein appearing at about the same time had a molecular weight of 130 kDa (gp130) and may be the same receptor [8]. It is interesting to speculate whether the gp126 receptor implicated in nonspecific phagocytosis in vegetative amoebae is the same as that found during sexual phagocytosis [8,42).…”

Section: Discussionmentioning

confidence: 99%

“…A WGA-binding glycoprotein appearing at about the same time had a molecular weight of 130 kDa (gp130) and may be the same receptor [8]. It is interesting to speculate whether the gp126 receptor implicated in nonspecific phagocytosis in vegetative amoebae is the same as that found during sexual phagocytosis [8,42). However, there are indications that this may not be the case.…”

Section: Discussionmentioning

confidence: 99%

Phagocytosis in Dictyostelium: Nibbling, Eating and Cannibalism

Lewis

O’Day

1996

J Eukaryotic Microbiology

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Phagocytosis is a highly conserved biological process that serves numerous functions in a wide variety of organisms. Over the past few decades Dictyostelium has proven to be an excellent organism for investigations in cell biology and this is certainly no less the case for a study of phagocytosis. This review examines three distinct phagocytic activities which have been characterized in Dictyostelium. The first, "vegetative phagocytosis," represents the classical eukaryotic microbial uptake of food particles (bacteria). The second, a predatory form of phagocytosis, arises when one species such as Dictyostelium caveatum attacks another species of slime mold, engulfing small pieces of the target prey. This has been termed "cell nibbling." The third phagocytic process is "sexual cannibalistic phagocytosis." In this situation a zygote giant cell, having arisen from the fusion of gametic amoebae, attracts unfused nonzygotic amoebae of the same species and engulfs them as a food source. While cell nibbling has not been actively studied, vegetative and sexual cannibalistic phagocytosis have received varying amounts of attention leading to the idea that some of the elements (e.g., glycoprotein receptors and a Gas subunit) involved in certain of these phagocytic events may be the same. On the other hand, some unique events (e.g., filopodial induction in prey by D. caveatum) are also worthy of further investigation. Among other things, the presence of selfnonself recognition, the existence of opsonin-like substances and the presence of signal transduction elements (e.g., an A2-like receptor that negatively modulates sexual phagocytosis) once considered to be extant only in higher organisms suggest that much can be learned about phagocytosis in general by further studies in the classic, eukaryotic microbe Dictyostelium discoideum and related species.

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Zygote giant cell differentiation in Dictyostelium discoideum: biochemical markers of specific stages of sexual development

Cited by 9 publications

References 29 publications

Glycopeptidome of a Heavily N-Glycosylated Cell Surface Glycoprotein of Dictyostelium Implicated in Cell Adhesion

Glycopeptidome of a Heavily N-Glycosylated Cell Surface Glycoprotein of Dictyostelium Implicated in Cell Adhesion

Isoforms of gp138, a Cell-Fusion Related Protein in Dictyostelium discoideum

Phagocytosis in Dictyostelium: Nibbling, Eating and Cannibalism

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