The rare sugar N-acetylated viosamine is a major component of Mimivirus fibers

Piacente, Francesco; Castro, Cristina De; Jeudy, Sandra; Gaglianone, Matteo; Laugieri, Maria Elena; Notaro, Anna; Salis, Annalisa; Damonte, Gianluca; Abergel, Chantal; Tonetti, Michela

doi:10.1074/jbc.m117.783217

Cited by 17 publications

(28 citation statements)

References 41 publications

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“…It is well known that most conventional viruses utilize host cellular glycosylation pathways to modify their proteins . The fact that the Mimivirus genome, as well as those of other giant viruses, encodes enzymes involved in nucleotide‐linked sugar metabolism is, indeed, fascinating . Clearly we are at the beginning of this foray into viral glycobiology.…”

Section: Discussionmentioning

confidence: 99%

Biochemical analysis of a sugar 4,6‐dehydratase from Acanthamoeba polyphaga Mimivirus

2020

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The exciting discovery of the giant DNA Mimivirus in 2003 challenged the conventional description of viruses in a radical way, and since then, dozens of additional giant viruses have been identified. It has now been demonstrated that the Mimivirus genome encodes for the two enzymes required for the production of the unusual sugar 4-amino-4,6-dideoxy-D-glucose, namely a 4,6-dehydratase and an aminotransferase. In light of our long-standing interest in the bacterial 4,6-dehydratases and in unusual sugars in general, we conducted a combined structural and functional analysis of the Mimivirus 4,6-dehydratase referred to as R141. For this investigation, the threedimensional X-ray structure of R141 was determined to 2.05 Å resolution and refined to an R-factor of 18.3%. The overall fold of R141 places it into the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Whereas its molecular architecture is similar to that observed for the bacterial 4,6-dehydratases, there are two key regions where the polypeptide chain adopts different conformations. In particular, the conserved tyrosine that has been implicated as a catalytic acid or base in SDR superfamily members is splayed away from the active site by nearly 12 Å, thereby suggesting that a major conformational change must occur upon substrate binding. In addition to the structural analysis, the kinetic parameters for R141 using either dTDP-D-glucose or UDP-D-glucose as substrates were determined. Contrary to a previous report, R141 demonstrates nearly identical catalytic efficiency with either nucleotide-linked sugar. The data presented herein represent the first threedimensional model for a viral 4,6-dehydratase and thus expands our understanding of these fascinating enzymes. K E Y W O R D SAcanthamoeba polyphaga Mimivirus, dideoxysugar, giant viruses, UDP-D-glucose 4,6-dehydratase, UDP-D-viosamine, viral glycans, X-ray structure Abbreviations: dTDP, thymidine diphosphate; ESI, electrospray ionization; HEPES, N-2-hydroxyethylpiperazine-N 0 -2-ethanesulfonic acid; HEPPS, N-2-hydroxyethylpiperazine-N 0 -3-propanesulfonic acid; HPLC, high-performance liquid chromatography; NAD + , nicotinamide adenine dinucleotide (oxidized); NADH, nicotinamide adenine dinucleotide (reduced); NADP + , nicotinamide adenine dinucleotide phosphate (oxidized); NADPH, nicotinamide adenine dinucleotide phosphate (reduced); Ni-NTA, nickel-nitrilotriacetic acid; PCR, polymerase chain reaction; PLP, pyridoxal 5 0 -phosphate; Qui4N, 4-amino-4,6-dideoxy-D-glucose; TEV, Tobacco Etch Virus; Tris, tris-(hydroxymethyl)aminomethane; UDP, uridine diphosphate.

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Section: Discussionmentioning

confidence: 99%

Biochemical analysis of a sugar 4,6‐dehydratase from Acanthamoeba polyphaga Mimivirus

2020

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“…Whilst most known viruses typically utilise the N- and O-linked host-cell glycosylation pathways to adorn their glycoproteins with carbohydrate modifications, it is important to mention known exceptions. There are a few notable examples of viruses that encode some, if not all, of the enzymes involved in the glycosylation of their proteins and other macromolecules such as, chloroviruses and mimiviruses [[41], [42], [43], [44]].…”

Section: Introductionmentioning

confidence: 99%

Exploitation of glycosylation in enveloped virus pathobiology

Watanabe

Bowden

Wilson

et al. 2019

Biochimica et Biophysica Acta (BBA) - General Subjects

427

547

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Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies.

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“…Unlike bacteria, viruses as obligate parasites need to glycosylate their own proteins for host-cell machinery. Indeed, most viruses hijack the N - and O -linked glycosylation pathways of the host-cells to glycosylate their proteins, except for a few cases, e.g., chloroviruses and mimiviruses, capable of coding themselves some of the enzymes involved in the glycosylation event [ 8 , 9 ].…”

Section: Glycosylation In Other Organismsmentioning

confidence: 99%

Protein Glycosylation Investigated by Mass Spectrometry: An Overview

Illiano

Pinto

Melchiorre

et al. 2020

Cells

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The protein glycosylation is a post-translational modification of crucial importance for its involvement in molecular recognition, protein trafficking, regulation, and inflammation. Indeed, abnormalities in protein glycosylation are correlated with several disease states such as cancer, inflammatory diseases, and congenial disorders. The understanding of cellular mechanisms through the elucidation of glycan composition encourages researchers to find analytical solutions for their detection. Actually, the multiplicity and diversity of glycan structures bond to the proteins, the variations in polarity of the individual saccharide residues, and the poor ionization efficiencies make their detection much trickier than other kinds of biopolymers. An overview of the most prominent techniques based on mass spectrometry (MS) for protein glycosylation (glycoproteomics) studies is here presented. The tricks and pre-treatments of samples are discussed as a crucial step prodromal to the MS analysis to improve the glycan ionization efficiency. Therefore, the different instrumental MS mode is also explored for the qualitative and quantitative analysis of glycopeptides and the glycans structural composition, thus contributing to the elucidation of biological mechanisms.

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The rare sugar N-acetylated viosamine is a major component of Mimivirus fibers

Cited by 17 publications

References 41 publications

Biochemical analysis of a sugar 4,6‐dehydratase from Acanthamoeba polyphaga Mimivirus

Biochemical analysis of a sugar 4,6‐dehydratase from Acanthamoeba polyphaga Mimivirus

Exploitation of glycosylation in enveloped virus pathobiology

Protein Glycosylation Investigated by Mass Spectrometry: An Overview

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