The spore coat of a fucosylation mutant in Dictyostelium discoideum

Gonzalez-Yanes, Beatriz; Mandell, Robert B.; Girard, Michel; Henry, S.; Aparicio, Oscar M.; Gritzali, Mikelina; Brown, Ross; Erdos, Gregory W.; West, Christopher M.

doi:10.1016/0012-1606(89)90060-2

Cited by 37 publications

(50 citation statements)

References 25 publications

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“…The two new mutations described here, mod-352 and mod-353, define this new pathway of 0-linked glycosylation, and do not prevent type I1 (modB-dependent) glycosylation. Antibody recognition studies (Western blots) using strains HU2470 (mod-352), HU247 1 (mod-353) and a further mutant, HL250 (Gonzalez-Yanes et al, 1989), indicate that the MUD62 glycoantigen is similar to that recognized by mAb 83.5 of West and co-workers (C. M. West, personal communication). This glycoantigen is named GA-X, and is reported to be an 0-linked GlcN Ac-containing oligosaccharide (Gonzalez-Yanes et al, 1989).…”

Section: Discussionmentioning

confidence: 86%

“…Antibody recognition studies (Western blots) using strains HU2470 (mod-352), HU247 1 (mod-353) and a further mutant, HL250 (Gonzalez-Yanes et al, 1989), indicate that the MUD62 glycoantigen is similar to that recognized by mAb 83.5 of West and co-workers (C. M. West, personal communication). This glycoantigen is named GA-X, and is reported to be an 0-linked GlcN Ac-containing oligosaccharide (Gonzalez-Yanes et al, 1989). mAb 83.5 recognizes a fucose epitope on GA-X, which is present on spore coat proteins designated by Gonzalez-Yanes et al (1989) as SP75, SPSO and SP96.…”

Section: Discussionmentioning

confidence: 86%

“…This glycoantigen is named GA-X, and is reported to be an 0-linked GlcN Ac-containing oligosaccharide (Gonzalez-Yanes et al, 1989). mAb 83.5 recognizes a fucose epitope on GA-X, which is present on spore coat proteins designated by Gonzalez-Yanes et al (1989) as SP75, SPSO and SP96. This epitope is confined in aggregates and slugs to prespore vesicles in prespore cells (West & Erdos, 1988;Gonzalez-Yanes et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…mAb 83.5 recognizes a fucose epitope on GA-X, which is present on spore coat proteins designated by Gonzalez-Yanes et al (1989) as SP75, SPSO and SP96. This epitope is confined in aggregates and slugs to prespore vesicles in prespore cells (West & Erdos, 1988;Gonzalez-Yanes et al, 1989). MUD62 recognizes major glycoproteins with apparent molecular mass of 75, 80 and 96 kDa (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Immunodominant carbohydrate determinants in the multicellular stages of Dictyostelium discoideum

Champion

Callaghan

et al. 1991

Journal of General Microbiology

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Two families of glycoprotein are defined in DictyosteZium discoideum by the presence of different glycoconjugates, both of which are highly immunogenic in mice. The previously described monoclonal antibodies MUD50 and MUD62 recognize the glycoconjugates and identify the respective glycoprotein families. Both types of glycosylation occur on vegetative and developmentally regulated glycoproteins. The immunodominant components of both families are reportedly 0-linked sugars, but Western blots do not identify any glycoprotein that has both 0-glycans, suggesting that there are two independently processed types of 0-linked glycosylation in D. discoideum.The synthesis of the two 0-glycan families is affected by glycosylation-defective mutations. Strains with a mutation at the modB locus lack one of these glycosylation types (that recognized by MUDSO) and this mutation alters the size of two minor glycoproteins in the second family. Two new mutants, HU2470 (mod-352) and HU2471 (mod-353), lack the epitope recognized by MUD62. The two mutations map to different chromosomes. The mod-353 mutation also affects the size of PsA, a cell surface glycoprotein carrying the modB-dependent 0-glycan.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Immunodominant carbohydrate determinants in the multicellular stages of Dictyostelium discoideum

Champion

Callaghan

et al. 1991

Journal of General Microbiology

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“…Strains carrying a modC or a modE mutation lack another epitope, GA-XII, which is recognized by mAbs MUD3 and MUD141. Lack of fucosylation is sufficient to affect the spore coat permeability, leading to premature loss of viability (17). Strains carrying these mutations expose a new carbohydrate epitope, competed by N-acetylglucosamine and recognized by mAb MUD166 (16).…”

mentioning

confidence: 99%

Multiple O-Glycoforms on the Spore Coat Protein SP96 in Dictyostelium discoideum

Mreyen¹,

Champion²,

Srinivasan³

et al. 2000

Journal of Biological Chemistry

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A decreased level of fucosylation on certain spore coat proteins of Dictyostelium discoideum alters the permeability of the spore coat. Here the post-translational modifications of a major spore coat protein, SP96, are studied in a wild type strain (X22) and a fucosylationdefective mutant (HU2470). A novel phosphoglycan structure on SP96 of the wild type strain, consisting of Fuc(␣1-3)GlcNAc-␣-1-P-Ser , was identified by electrospray ionization mass spectrometry and NMR. It was shown using monosaccharide and gas chromatography mass spectrometry analysis that SP96 in the mutant

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Isolation of glycosylation mutants inDictyostelium discoideum using flow cytometry

et al. 1996

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The spore coat of a fucosylation mutant in Dictyostelium discoideum

Cited by 37 publications

References 25 publications

Immunodominant carbohydrate determinants in the multicellular stages of Dictyostelium discoideum

Immunodominant carbohydrate determinants in the multicellular stages of Dictyostelium discoideum

Multiple O-Glycoforms on the Spore Coat Protein SP96 in Dictyostelium discoideum

Isolation of glycosylation mutants inDictyostelium discoideum using flow cytometry

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