A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus

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A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus. / Krause, K.; Brophy, Peter M.; Walter, R. D.; Boettcher, K.; Liebau, E.; Sommer, A.; Fischer, P.

In: Biochemical Journal, Vol. 353, 2001, p. 445-452.

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Harvard

Krause, K, Brophy, PM, Walter, RD, Boettcher, K, Liebau, E, Sommer, A & Fischer, P 2001, 'A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus' Biochemical Journal, vol. 353, pp. 445-452.

APA

Krause, K., Brophy, P. M., Walter, R. D., Boettcher, K., Liebau, E., Sommer, A., & Fischer, P. (2001). A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus. Biochemical Journal, 353, 445-452.

Vancouver

Krause K, Brophy PM, Walter RD, Boettcher K, Liebau E, Sommer A et al. A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus. Biochemical Journal. 2001;353:445-452.

Author

Krause, K. ; Brophy, Peter M. ; Walter, R. D. ; Boettcher, K. ; Liebau, E. ; Sommer, A. ; Fischer, P. / A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus. In: Biochemical Journal. 2001 ; Vol. 353. pp. 445-452.

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@article{0f342c1dabf646f88120f4fabee39c62,
title = "A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus",
abstract = "Glyoxal, methylglyoxal and other physiological a-oxoaldehydes are formed by the lipid peroxidation, glycation and degradation of glycolytic intermediates. They are detoxified enzymically by the glyoxalase system. To investigate the physiological function of glyoxalase I in parasitic organisms, the cDNA for glyoxalase I from the filarial nematode Onchocerca volvulus (designated Ov-GloI) has been cloned and characterized. The isolated cDNA contains an open reading frame of 579bp encoding a protein with a calculated molecular mass of 21930Da. Owing to the high degree of sequence identity (60{\%}) with human glyoxalase I, for which the X-ray structure is available, it has been possible to build a three-dimensional model of Ov-GloI. The modelled core of Ov-GloI is conserved compared with the human glyoxalase I; however, there are critical differences in the residues lining the hydrophobic substrate-binding pocket of Ov-GloI. A 22kDa protein was obtained by heterologous expression in Escherichia coli. A homogeneous enzyme preparation was obtained by affinity purification and functional characterization of the recombinant enzyme included the determination of kinetic constants for methylglyoxal and phenylglyoxal as well as inhibition studies. Gel filtration demonstrated a dimeric structure. To assess the role of Ov-GloI as a potential vaccine candidate or serodiagnostic tool, the serological reactivity of the recombinant Ov-GloI was analysed with sera from microfilaria carriers and specific IgG1 antibodies were detected. The effects of oxidative insult, namely plumbagin and xanthine/xanthine oxidase, on the gene transcript level of Ov-GloI were investigated. By using a semi-quantitative PCR ELISA it was shown that Ov-GloI is expressed at elevated levels under conditions of oxidative stress.",
keywords = "glutathione, oxidative stress, parasite",
author = "K. Krause and Brophy, {Peter M.} and Walter, {R. D.} and K. Boettcher and E. Liebau and A. Sommer and P. Fischer",
note = "Sommer, A., Fischer, P., Krause, K., Boettcher, K., Brophy, P. M., Walter, R. D., Liebau, E. (2001). A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus.  Biochemical Journal, 353, 445-452. Sponsorship: Deutsche Forschungsgemeinschaft (DFG project Li 791/1-4).",
year = "2001",
language = "English",
volume = "353",
pages = "445--452",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus

AU - Krause, K.

AU - Brophy, Peter M.

AU - Walter, R. D.

AU - Boettcher, K.

AU - Liebau, E.

AU - Sommer, A.

AU - Fischer, P.

N1 - Sommer, A., Fischer, P., Krause, K., Boettcher, K., Brophy, P. M., Walter, R. D., Liebau, E. (2001). A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus.  Biochemical Journal, 353, 445-452. Sponsorship: Deutsche Forschungsgemeinschaft (DFG project Li 791/1-4).

PY - 2001

Y1 - 2001

N2 - Glyoxal, methylglyoxal and other physiological a-oxoaldehydes are formed by the lipid peroxidation, glycation and degradation of glycolytic intermediates. They are detoxified enzymically by the glyoxalase system. To investigate the physiological function of glyoxalase I in parasitic organisms, the cDNA for glyoxalase I from the filarial nematode Onchocerca volvulus (designated Ov-GloI) has been cloned and characterized. The isolated cDNA contains an open reading frame of 579bp encoding a protein with a calculated molecular mass of 21930Da. Owing to the high degree of sequence identity (60%) with human glyoxalase I, for which the X-ray structure is available, it has been possible to build a three-dimensional model of Ov-GloI. The modelled core of Ov-GloI is conserved compared with the human glyoxalase I; however, there are critical differences in the residues lining the hydrophobic substrate-binding pocket of Ov-GloI. A 22kDa protein was obtained by heterologous expression in Escherichia coli. A homogeneous enzyme preparation was obtained by affinity purification and functional characterization of the recombinant enzyme included the determination of kinetic constants for methylglyoxal and phenylglyoxal as well as inhibition studies. Gel filtration demonstrated a dimeric structure. To assess the role of Ov-GloI as a potential vaccine candidate or serodiagnostic tool, the serological reactivity of the recombinant Ov-GloI was analysed with sera from microfilaria carriers and specific IgG1 antibodies were detected. The effects of oxidative insult, namely plumbagin and xanthine/xanthine oxidase, on the gene transcript level of Ov-GloI were investigated. By using a semi-quantitative PCR ELISA it was shown that Ov-GloI is expressed at elevated levels under conditions of oxidative stress.

AB - Glyoxal, methylglyoxal and other physiological a-oxoaldehydes are formed by the lipid peroxidation, glycation and degradation of glycolytic intermediates. They are detoxified enzymically by the glyoxalase system. To investigate the physiological function of glyoxalase I in parasitic organisms, the cDNA for glyoxalase I from the filarial nematode Onchocerca volvulus (designated Ov-GloI) has been cloned and characterized. The isolated cDNA contains an open reading frame of 579bp encoding a protein with a calculated molecular mass of 21930Da. Owing to the high degree of sequence identity (60%) with human glyoxalase I, for which the X-ray structure is available, it has been possible to build a three-dimensional model of Ov-GloI. The modelled core of Ov-GloI is conserved compared with the human glyoxalase I; however, there are critical differences in the residues lining the hydrophobic substrate-binding pocket of Ov-GloI. A 22kDa protein was obtained by heterologous expression in Escherichia coli. A homogeneous enzyme preparation was obtained by affinity purification and functional characterization of the recombinant enzyme included the determination of kinetic constants for methylglyoxal and phenylglyoxal as well as inhibition studies. Gel filtration demonstrated a dimeric structure. To assess the role of Ov-GloI as a potential vaccine candidate or serodiagnostic tool, the serological reactivity of the recombinant Ov-GloI was analysed with sera from microfilaria carriers and specific IgG1 antibodies were detected. The effects of oxidative insult, namely plumbagin and xanthine/xanthine oxidase, on the gene transcript level of Ov-GloI were investigated. By using a semi-quantitative PCR ELISA it was shown that Ov-GloI is expressed at elevated levels under conditions of oxidative stress.

KW - glutathione

KW - oxidative stress

KW - parasite

M3 - Article

VL - 353

SP - 445

EP - 452

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

ER -

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