ArticleGlycoconjugate journal2011
Glycan structures of the structural subunit (HtH1) of Haliotis tuberculata hemocyanin.
Article in Glycoconjugate journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Mollusc N-glycosylation: Structures, Functions and Perspectives.Biomolecules · 2021Review
- De Novo Structural Determination of the Oligosaccharide Structure of Hemocyanins from Molluscs.Biomolecules · 2020Review
- Article
- Hemocyanins Stimulate Innate Immunity by Inducing Different Temporal Patterns of Proinflammatory Cytokine Expression in Macrophages.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Abalone Hemocyanin Blocks the Entry of Herpes Simplex Virus 1 into Cells: a Potential New Antiviral Strategy.Antimicrobial agents and chemotherapy · 2016Article
- Copper active sites in biology.Chemical reviews · 2014Review
- Hemocytes and plasma of the eastern oyster (Crassostrea virginica) display a diverse repertoire of sulfated and blood group A-modified N-glycans.The Journal of biological chemistry · 2013Article
- Positions of the glycans in molluscan hemocyanin, determined by fluorescence spectroscopy.Journal of fluorescence · 2013Article
- A lectin from the mussel Mytilus galloprovincialis has a highly novel primary structure and induces glycan-mediated cytotoxicity of globotriaosylceramide-expressing lymphoma cells.The Journal of biological chemistry · 2012Article
- Method for analysis of different oligosacchiride structures.Journal of fluorescence · 2012Article
- Complicated N-linked glycans in simple organisms.Biological chemistry · 2012Review
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oligosaccharide structures of the structural subunit HtH1 of Haliotis tuberculata hemocyanin (HtH) were studied by mass spectral sequence analysis of the glycans. The proposed structures are based on MALDI-TOF-MS data before and after treatment with the specific exoglycosidases β1-3,4,6-galactosidase and α1-6(>2,3,4) fucosidase followed by sequence analysis via electrospray ionization MS/MS-spectra. In total, 15 glycans were identified as a highly heterogeneous group of structures. As in most molluscan hemocyanins, the glycans of HtH1 contain a terminal MeHex, but more interestingly, a novel structural motif was observed: MeHex[Fuc(α1-3)-]GlcNAc, including thus MeHex and (α1-3)-Fuc residues being linked to an internal GlcNAc residue. While the functional unit (FU) c (HtH1-c) is completely lacking any potential glycosylation site, FU-h possesses a second exposed sugar attachment site between beta-strands 8 and 9 within the beta sandwich domain compared to the other FUs. The glycosylation pattern/sites show a high degree of conservation. In FU-h two prominent potential glycosylation sites can be detected. The finding that HtH1 is not able to form multidecameric structures in vivo could be explained by the presence of the exposed glycan on the surface of FU-h.
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