ArticleThe Journal of biological chemistry2012
Exploring the unique N-glycome of the opportunistic human pathogen Acanthamoeba.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Comparative glycomic analysis of Mimiviridae and Marseilleviridae uncovers host-related and lineage-specific glycosylation.Journal of biochemistry · 2026Article
- Targets for the diagnosis ofmSphere · 2025Article
- New insights into the N-glycomes ofBBA advances · 2025Article
- Recombinant protein expression inFrontiers in bioengineering and biotechnology · 2025Article
- Article
- The Astounding World of Glycans from Giant Viruses.Chemical reviews · 2022Review
- Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022Review
- Expanding the Occurrence of Polysaccharides to the Viral World: The Case of Mimivirus.Angewandte Chemie (International ed. in English) · 2021Article
- Glycomics, Glycoproteomics, and Glycogenomics: An Inter-Taxa Evolutionary Perspective.Molecular & cellular proteomics : MCP · 2021Review
- Asparagine-Linked Glycans ofMolecular & cellular proteomics : MCP · 2017Article
- Analysis of Invertebrate and Protist N-Glycans.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Evolutionary diversity of social amoebae N-glycomes may support interspecific autonomy.Glycoconjugate journal · 2015Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Glycans play key roles in host-pathogen interactions; thus, knowing the N-glycomic repertoire of a pathogen can be helpful in deciphering its methods of establishing and sustaining a disease. Therefore, we sought to elucidate the glycomic potential of the facultative amoebal parasite Acanthamoeba. This is the first study of its asparagine-linked glycans, for which we applied biochemical tools and various approaches of mass spectrometry. An initial glycomic screen of eight strains from five genotypes of this human pathogen suggested, in addition to the common eukaryotic oligomannose structures, the presence of pentose and deoxyhexose residues on their N-glycans. A more detailed analysis was performed on the N-glycans of a genotype T11 strain (4RE); fractionation by HPLC and tandem mass spectrometric analyses indicated the presence of a novel mannosylfucosyl modification of the reducing terminal core as well as phosphorylation of mannose residues, methylation of hexose and various forms of pentosylation. The largest N-glycan in the 4RE strain contained two N-acetylhexosamine, thirteen hexose, one fucose, one methyl, and two pentose residues; however, in this and most other strains analyzed, glycans with compositions of Hex(8-9)HexNAc(2)Pnt(0-1) tended to dominate in terms of abundance. Although no correlation between pathogenicity and N-glycan structure can be proposed, highly unusual structures in this facultative parasite can be found which are potential virulence factors or therapeutic targets.
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Registered trials
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