Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities.

Ahn, Bokyung; Moss, Bernard

doi:10.1073/pnas.89.15.7060

Cited by 65 publications

(47 citation statements)

References 41 publications

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“…A4L encodes an immunodominant late protein associated with the virion core and necessary for viral morphogenesis (84). OV-SA00 and OV-IA82 080 encode products that are 84 and 80 amino acids longer than the BPSV 080 product, respectively, due in part to the lack of four Cys-(Pro-Ala) 3 motifs separated by additional Pro/Ala-rich sequences in BPSV 080. Similar Pro/Ala-rich repeats are present in the molluscum contagiosum virus (MOCV) orthologue MC107L but not in A4L.…”

Section: Resultsmentioning

confidence: 99%

Genomes of the Parapoxviruses Orf Virus and Bovine Papular Stomatitis Virus

Delhon

Tulman

Afonso

et al. 2004

J Virol

249

274

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Section: Resultsmentioning

confidence: 99%

Genomes of the Parapoxviruses Orf Virus and Bovine Papular Stomatitis Virus

Delhon

Tulman

Afonso

et al. 2004

J Virol

249

274

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“…Very recently, human glutaredoxin has been shown to regulate the activity of HIV-1 protease and to be packaged into HIV viral particles (Davis et al, 1997). Interestingly, vaccinia virus also packages its virally encoded glutaredoxin into its viral particles (Ahn & Moss, 1992), suggesting a possible functional role for glutaredoxins in viral pathogenesis.…”

Section: Introductionmentioning

confidence: 99%

“…They are essential for the glutathione-dependent reduction of ribonucleotides by ribonucleotide reductase (Holmgren, 1976(Holmgren, , 1979Luthman et al, 1979;Luthman & Holmgren, 1982). They have also been shown to play a role in the reduction of sulfate (Russel et al, 1990;Tsang, 1981), arsenate (Gladysheva et al, 1994;Wells et al, 1990), and ascorbate (Ahn & Moss, 1992;Gravina & Mieyal, 1993). They preferentially reduce glutathione-containing mixed disul®des (Gravina & Mieyal, 1993;Jung & Thomsa, 1996) due to the glutathione binding site present on the protein (Bushweller et al, 1994) .…”

Section: Introductionmentioning

confidence: 99%

“…Glutaredoxins have now been identi®ed in numerous species including Escherichia coli, bacteriophage T4, vaccinia virus, yeast, rabbit, pig, and human (Ahn & Moss, 1992;Gan & Wells, 1987a;Gan et al, 1990;Ho È o È g et al, 1983;Hopper et al, 1989;Johnson et al, 1991;Klintrot et al, 1984;Minakuchi et al, 1994;Padilla et al, 1995). This important family of protein disul®de reductants has been shown to play numerous important roles in the cell.…”

Section: Introductionmentioning

confidence: 99%

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The NMR solution structure of human glutaredoxin in the fully reduced form

Sun

Berardi

Bushweller

1998

Journal of Molecular Biology

100

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The determination of the nuclear magnetic resonance (NMR) solution structure of fully reduced human glutaredoxin is described. A total of 1159 useful nuclear Overhauser effect (NOE) upper distance constraints and 187 dihedral angle constraints were obtained as the input for the structure calculations for which the torsion angle dynamics program DYANA has been utilized followed by energy minimization in water with the AMBER force ®eld as implemented in the program OPAL. The resulting 20 conformers have an average root-mean-square deviation value relative to the mean coordinates of 0.54 A Ê for all the backbone atoms N, C a and C H , and of 1.01 A Ê for all heavy atoms. Human glutaredoxin consists of a four-stranded mixed b-sheet composed of residues 15 to 19, 43 to 47, 72 to 75 and 78 to 81, and ®ve a-helices composed of residues 4 to 9, 24 to 34, 54 to 65, 83 to 91, and 94 to 100. Comparisons with the structures of Escherichia coli glutaredoxin-1, pig liver glutaredoxin and human thioredoxin were made. Electrostatic calculations on the human glutaredoxin structure and that of related proteins provide an understanding of the variation of pK a values for the nucleophilic cysteine in the active site observed among these proteins. In addition, the high-resolution NMR solution structure of human glutaredoxin has been used to model the binding site for glutathione and for ribonucleotide reductase B1 by molecular dynamics simulations.

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“…Although ERV1/ALR proteins lack the characteristic thioredoxin fold of many other redox proteins, several members of the family have been shown to be flavin adenine dinucleotide-linked sulfhydryl oxidases (6,11,12), suggesting a related mechanism of electron transfer for E10R. Vaccinia virus G4L and O2L glutaredoxins, with predicted thioredoxin folds, have both thiol transferase and dehydroascorbate reductase activities in vitro (1,7). O2L is nonessential for vaccinia virus replication and is thought to serve as a ribonucleotide reductase (15), though it may have additional functions consistent with its late promoter.…”

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confidence: 99%

Vaccinia Virus G4L Glutaredoxin Is an Essential Intermediate of a Cytoplasmic Disulfide Bond Pathway Required for Virion Assembly

White

Senkevich

Moss

2002

J Virol

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Our previous studies provided evidence that E10R, a vaccinia virus protein belonging to the ERV1/ALR family, has a redox function and is required for virion assembly. Repression of E10R prevented the formation of intramolecular disulfide bonds of the G4L glutaredoxin, the L1R membrane protein, and the structurally related F9L protein. Here, we demonstrate an oxidation pathway (E10R SS 3 G4L SS 3 L1R SS , F9L SS ) in which G4L occupies an intermediate position. By reacting free thiols with 4-acetamido-4-malemideylstilbene-2,2-disulfonic acid, alkylated and nonalkylated disulfide-bonded forms of G4L could be resolved from each other by polyacrylamide gel electrophoresis. The cysteines of intracellular G4L were in both disulfide and reduced forms, whereas those of E10R, L1R, and F9L and virion-associated G4L were mostly disulfide bonded. Repression of G4L expression prevented the formation of disulfide bonds in both L1R and F9L but not E10R. Both cysteines of G4L were required for L1R and F9L disulfide bond formation or for trans-complementation of virus infectivity when G4L expression was repressed. No role in the E10R-G4L redox pathway was found for O2L, a nonessential glutaredoxin encoded by vaccinia virus. We suggest that cytoplasmic G4L is a redox shuttle between membrane-associated E10R and L1R or F9L.

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Glutaredoxin homolog encoded by vaccinia virus is a virion-associated enzyme with thioltransferase and dehydroascorbate reductase activities.

Abstract: Glutaredoxins (GRXs), also known as thioltransferases, use glutathione as a cofactor for reduction of disulfides in prokaryotes and eukaryotes. We demonstrate that the vaccinia virus 02L open reading frame encodes a fumctional

Cited by 65 publications

References 41 publications

Genomes of the Parapoxviruses Orf Virus and Bovine Papular Stomatitis Virus

Genomes of the Parapoxviruses Orf Virus and Bovine Papular Stomatitis Virus

The NMR solution structure of human glutaredoxin in the fully reduced form

Vaccinia Virus G4L Glutaredoxin Is an Essential Intermediate of a Cytoplasmic Disulfide Bond Pathway Required for Virion Assembly

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