ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structure of N-linked oligosaccharides attached to chlorovirus PBCV-1 major capsid protein reveals unusual class of complex N-glycans.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 53 citations in OpenAlex.
- Article
- Carbohydrate-mediated interactions between chloroviruses and the immune system.Communications biology · 2024Article
- Virologs, viral mimicry, and virocell metabolism: the expanding scale of cellular functions encoded in the complex genomes of giant viruses.FEMS microbiology reviews · 2023Article
- The Astounding World of Glycans from Giant Viruses.Chemical reviews · 2022Review
- Rhamnose-Containing Compounds: Biosynthesis and Applications.Molecules (Basel, Switzerland) · 2022Review
- Giant viruses of themicroLife · 2022Article
- Strong selection and high mutation supply characterize experimental Chlorovirus evolution.Virus evolution · 2022Article
- Dissecting Lipopolysaccharide Composition and Structure by GC-MS and MALDI Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Expanding the Occurrence of Polysaccharides to the Viral World: The Case of Mimivirus.Angewandte Chemie (International ed. in English) · 2021Article
- Production of perdeuterated fucose from glyco-engineered bacteria.Glycobiology · 2021Article
- Article
- Chlorovirus PBCV-1 protein A064R has three of the transferase activities necessary to synthesize its capsid protein N-linked glycans.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships.Mass spectrometry reviews · 2020Review
- Toward Automatic and Comprehensive Glycan Characterization by Online PGC-LC-EED MS/MS.Analytical chemistry · 2020Article
- Chloroviruses.Viruses · 2019Review
- Nucleocytoplasmic O-glycosylation in protists.Current opinion in structural biology · 2019Review
- TheThe Journal of biological chemistry · 2019Article
- Structure of the chlorovirus PBCV-1 major capsid glycoprotein determined by combining crystallographic and carbohydrate molecular modeling approaches.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The rare sugarThe Journal of biological chemistry · 2017Article
- Chloroviruses Have a Sweet Tooth.Viruses · 2017Review
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
The major capsid protein Vp54 from the prototype chlorovirus Paramecium bursaria chlorella virus 1 (PBCV-1) contains four Asn-linked glycans. The structure of the four N-linked oligosaccharides and the type of substitution at each glycosylation site was determined by chemical, spectroscopic, and spectrometric analyses. Vp54 glycosylation is unusual in many ways, including: (i) unlike most viruses, PBCV-1 encodes most, if not all, of the machinery to glycosylate its major capsid protein; (ii) the glycans are attached to the protein by a β-glucose linkage; (iii) the Asn-linked glycans are not located in a typical N-X-(T/S) consensus site; and (iv) the process probably occurs in the cytoplasm. The four glycoforms share a common core structure, and the differences are related to the nonstoichiometric presence of two monosaccharides. The most abundant glycoform consists of nine neutral monosaccharide residues, organized in a highly branched fashion. Among the most distinctive features of the glycoforms are (i) a dimethylated rhamnose as the capping residue of the main chain, (ii) a hyperbranched fucose unit, and (iii) two rhamnose residues with opposite absolute configurations. These glycoforms differ from what has been reported so far in the three domains of life. Considering that chloroviruses and other members of the family Phycodnaviridae may have a long evolutionary history, we suggest that the chlorovirus glycosylation pathway is ancient, possibly existing before the development of the endoplasmic reticulum and Golgi pathway, and involves still unexplored mechanisms.
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