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Characterization of a UDP-N-acetylglucosamine biosynthetic pathway encoded by the giant DNA virus Mimivirus.
Glycobiology. 2014 Jan; 24(1):51-61.G

Abstract

Mimivirus is a giant DNA virus belonging to the Megaviridae family and infecting unicellular Eukaryotes of the genus Acanthamoeba. The viral particles are characterized by heavily glycosylated surface fibers. Several experiments suggest that Mimivirus and other related viruses encode an autonomous glycosylation system, forming viral glycoproteins independently of their host. In this study, we have characterized three Mimivirus proteins involved in the de novo uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) production: a glutamine-fructose-6-phosphate transaminase (CDS L619), a glucosamine-6-phosphate N-acetyltransferase (CDS L316) and a UDP-GlcNAc pyrophosphorylase (CDS R689). Sequence and enzymatic analyses have revealed some unique features of the viral pathway. While it follows the eukaryotic-like strategy, it also shares some properties of the prokaryotic pathway. Phylogenetic analyses revealed that the Megaviridae enzymes cluster in monophyletic groups, indicating that they share common ancestors, but did not support the hypothesis of recent acquisitions from one of the known hosts. Rather, viral clades branched at deep nodes in phylogenetic trees, forming independent clades outside sequenced cellular organisms. The intermediate properties between the eukaryotic and prokaryotic pathways, the phylogenetic analyses and the fact that these enzymes are shared between most of the known members of the Megaviridae family altogether suggest that the viral pathway has an ancient origin, resulting from lateral transfers of cellular genes early in the Megaviridae evolution, or from vertical inheritance from a more complex cellular ancestor (reductive evolution hypothesis). The identification of a virus-encoded UDP-GlcNAc pathway reinforces the concept that GlcNAc is a ubiquitous sugar representing a universal and fundamental process in all organisms.

Authors+Show Affiliations

Department of Experimental Medicine, Center of Excellence for Biomedical Research, University of Genova, Viale Benedetto XV, 1 Genova 16132, Italy.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

24107487

Citation

Piacente, Francesco, et al. "Characterization of a UDP-N-acetylglucosamine Biosynthetic Pathway Encoded By the Giant DNA Virus Mimivirus." Glycobiology, vol. 24, no. 1, 2014, pp. 51-61.
Piacente F, Bernardi C, Marin M, et al. Characterization of a UDP-N-acetylglucosamine biosynthetic pathway encoded by the giant DNA virus Mimivirus. Glycobiology. 2014;24(1):51-61.
Piacente, F., Bernardi, C., Marin, M., Blanc, G., Abergel, C., & Tonetti, M. G. (2014). Characterization of a UDP-N-acetylglucosamine biosynthetic pathway encoded by the giant DNA virus Mimivirus. Glycobiology, 24(1), 51-61. https://doi.org/10.1093/glycob/cwt089
Piacente F, et al. Characterization of a UDP-N-acetylglucosamine Biosynthetic Pathway Encoded By the Giant DNA Virus Mimivirus. Glycobiology. 2014;24(1):51-61. PubMed PMID: 24107487.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of a UDP-N-acetylglucosamine biosynthetic pathway encoded by the giant DNA virus Mimivirus. AU - Piacente,Francesco, AU - Bernardi,Cinzia, AU - Marin,Margherita, AU - Blanc,Guillaume, AU - Abergel,Chantal, AU - Tonetti,Michela G, Y1 - 2013/10/09/ PY - 2013/10/11/entrez PY - 2013/10/11/pubmed PY - 2014/7/22/medline KW - Mimivirus KW - UDP-N-acetylglucosamine KW - UDP-N-acetylglucosamine pyrophosphorylase KW - glucosamine-6P acetyltransferase KW - glutamine-fructose-6P transaminase SP - 51 EP - 61 JF - Glycobiology JO - Glycobiology VL - 24 IS - 1 N2 - Mimivirus is a giant DNA virus belonging to the Megaviridae family and infecting unicellular Eukaryotes of the genus Acanthamoeba. The viral particles are characterized by heavily glycosylated surface fibers. Several experiments suggest that Mimivirus and other related viruses encode an autonomous glycosylation system, forming viral glycoproteins independently of their host. In this study, we have characterized three Mimivirus proteins involved in the de novo uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) production: a glutamine-fructose-6-phosphate transaminase (CDS L619), a glucosamine-6-phosphate N-acetyltransferase (CDS L316) and a UDP-GlcNAc pyrophosphorylase (CDS R689). Sequence and enzymatic analyses have revealed some unique features of the viral pathway. While it follows the eukaryotic-like strategy, it also shares some properties of the prokaryotic pathway. Phylogenetic analyses revealed that the Megaviridae enzymes cluster in monophyletic groups, indicating that they share common ancestors, but did not support the hypothesis of recent acquisitions from one of the known hosts. Rather, viral clades branched at deep nodes in phylogenetic trees, forming independent clades outside sequenced cellular organisms. The intermediate properties between the eukaryotic and prokaryotic pathways, the phylogenetic analyses and the fact that these enzymes are shared between most of the known members of the Megaviridae family altogether suggest that the viral pathway has an ancient origin, resulting from lateral transfers of cellular genes early in the Megaviridae evolution, or from vertical inheritance from a more complex cellular ancestor (reductive evolution hypothesis). The identification of a virus-encoded UDP-GlcNAc pathway reinforces the concept that GlcNAc is a ubiquitous sugar representing a universal and fundamental process in all organisms. SN - 1460-2423 UR - https://www.unboundmedicine.com/medline/citation/24107487/Characterization_of_a_UDP_N_acetylglucosamine_biosynthetic_pathway_encoded_by_the_giant_DNA_virus_Mimivirus_ L2 - https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cwt089 DB - PRIME DP - Unbound Medicine ER -