Partially glucose-capped oligosaccharides are found on the hemoglobins of the deep-sea tube worm Riftia pachyptila

Zal, Franck; Küster, Bernhard; Brian, N Green; Harvey, David J.; Lallier, François H.

doi:10.1093/glycob/8.7.663

Cited by 16 publications

(10 citation statements)

References 21 publications

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“…The treatment of this Vg with GNA indicated the presence of N-glycosylation of the high mannose type (Fig. 2); this finding is consistent with the common glycosylation of arthropod glycoproteins, such as the hemocyanin of Astacus leptodactylus [30], the hemoglobins of the deep-sea tube worm Riftia pachyptila [31], the larval serum protein of Drosophila melanogaster [32], and the storage glycoprotein, arylphorin, of lepidopteran insects [20,33]. As was to be expected, no interaction was found with either of the sialic-acid-specific lectins, SNA and MAA.…”

Section: Discussionsupporting

confidence: 79%

N-glycan moieties of the crustacean egg yolk protein and their glycosylation sites

et al. 2009

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Vitellogenin (Vg) is the precursor of the egg yolk glycoprotein of crustaceans. In the prawn Macrobrachium rosenbergii, Vg is synthesized in the hepatopancreas, secreted to the hemolymph, and taken up by means of receptor-mediated endocytosis into the oocytes. The importance of glycosylation of Vg lies in its putative role in the folding, processing and transport of this protein to the egg yolk and in the fact that the N-glycan moieties could provide a source of carbohydrate during embryogenesis. The present study describes, for the first time, the structure of the glycan moieties and their sites of attachment to the Vg of M. rosenbergii. Bioinformatics analysis revealed seven putative N-glycosylation sites in M. rosenbergii Vg; two of these glycosylation sites are conserved throughout the Vgs of decapod crustaceans from the Pleocyemata suborder (N 159 and N 660). The glycosylation of six putative sites of M. rosenbergii Vg (N 151, N 159, N ,168 N ,614 N 660 and N 2300) was confirmed; three of the confirmed glycosylation sites are localized around the N-terminally conserved N-glycosylation site N 159. From a theoretical three-dimensional structure, these three N-glycosylated sites N 151, N 159, and N 168 were localized on the surface of the Vg consensus sequence. In addition, an uncommon high mannose N-linked oligosaccharide structure with a glucose cap (Glc1Man9GlcNAc2) was characterized in the secreted Vg. These findings thus make a significant contribution to the structural elucidating of the crustacean Vg glycan moieties, which may shed light on their role in protein folding and transport and in recognition between Vg and its target organ, the oocyte.

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Section: Discussionsupporting

confidence: 79%

N-glycan moieties of the crustacean egg yolk protein and their glycosylation sites

et al. 2009

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“…The bacteria oxidize hydrogen sulfide, thereby producing the energy required to fix carbon from CO 2 , providing sugars and amino acids (predominantly as glutamate) that nourish the worm (55,84). The worm contributes to the symbiosis by collecting hydrogen sul- (3,46,(149)(150)(151)(152)(153). The bacterium is a member of the ␥-Proteobacteria, as identified by 16S rRNA gene sequence (47).…”

Section: Symbiosismentioning

confidence: 99%

Metagenomics: Application of Genomics to Uncultured Microorganisms

Handelsman

2004

Microbiol Mol Biol Rev

2,023

1,038

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Metagenomics (also referred to as environmental and community genomics) is the genomic analysis of microorganisms by direct extraction and cloning of DNA from an assemblage of microorganisms. The development of metagenomics stemmed from the ineluctable evidence that as-yet-uncultured microorganisms represent the vast majority of organisms in most environments on earth. This evidence was derived from analyses of 16S rRNA gene sequences amplified directly from the environment, an approach that avoided the bias imposed by culturing and led to the discovery of vast new lineages of microbial life. Although the portrait of the microbial world was revolutionized by analysis of 16S rRNA genes, such studies yielded only a phylogenetic description of community membership, providing little insight into the genetics, physiology, and biochemistry of the members. Metagenomics provides a second tier of technical innovation that facilitates study of the physiology and ecology of environmental microorganisms. Novel genes and gene products discovered through metagenomics include the first bacteriorhodopsin of bacterial origin; novel small molecules with antimicrobial activity; and new members of families of known proteins, such as an Na+(Li+)/H+ antiporter, RecA, DNA polymerase, and antibiotic resistance determinants. Reassembly of multiple genomes has provided insight into energy and nutrient cycling within the community, genome structure, gene function, population genetics and microheterogeneity, and lateral gene transfer among members of an uncultured community. The application of metagenomic sequence information will facilitate the design of better culturing strategies to link genomic analysis with pure culture studies

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“…N-Linked glycans enzymatically liberated from the SIPC were found to be high mannose-type, ranging from M2 to M9. Previous studies have reported the presence of similar oligosaccharide structures on the proteins isolated from other aquatic organisms such as haemocyanin from the crayfish Astacus leptodactylus (Tseneklidou-Stoeter et al, 1995) and haemoglobins from the hydrothermal vent tube worm Riftia pachyptila (Zal et al, 1998).…”

Section: Discussionmentioning

confidence: 93%

Structural characterisation of theN-glycan moiety of the barnacle settlement-inducing protein complex (SIPC)

Pagett

Abrahams

Bones

et al. 2012

Journal of Experimental Biology

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Partially glucose-capped oligosaccharides are found on the hemoglobins of the deep-sea tube worm Riftia pachyptila

Cited by 16 publications

References 21 publications

N-glycan moieties of the crustacean egg yolk protein and their glycosylation sites

N-glycan moieties of the crustacean egg yolk protein and their glycosylation sites

Metagenomics: Application of Genomics to Uncultured Microorganisms

Structural characterisation of theN-glycan moiety of the barnacle settlement-inducing protein complex (SIPC)

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