Characterization of a silkworm thioredoxin peroxidase that is induced by external temperature stimulus and viral infection

Lee, Kwang-Sik; Kim, Seong Ryul; Park, Nam Sook; Kim, Iksoo; Kang, Pil Dong; Sohn, Bong Hee; Choi, Kwang Ho; Kang, Seok Woo; Je, Yeon Ho; Lee, Sang Mong; Sohn, Hung Dae; Jin, Byung Rae

doi:10.1016/j.ibmb.2004.09.008

Cited by 134 publications

(83 citation statements)

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“…The majority of work has focused on the roles of pathogen and parasite Prxs in protection against host defenses. In contrast, a smaller number of studies have demonstrated that Prxs of eukaryotic hosts can be induced in response to viral, bacterial, and fungal infections [36][37][38]. Here, we investigated whether the 2-Cys Prx AsPrx-4783 can protect A. stephensi cells against ROS-and RNOS-associated cell damage and death that are consistent with conditions known to exist during malaria parasite infection of A. stephensi.…”

Section: Discussionmentioning

confidence: 84%

A mosquito 2-Cys peroxiredoxin protects against nitrosative and oxidative stresses associated with malaria parasite infection

Peterson

Luckhart

2006

Free Radical Biology and Medicine

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Malaria parasite infection in anopheline mosquitoes induces nitrosative and oxidative stresses that limit parasite development, but also damage mosquito tissues in proximity to the response. Based on these observations, we proposed that cellular defenses in the mosquito may be induced to minimize self-damage. Specifically, we hypothesized that peroxiredoxins (Prxs), enzymes known to detoxify reactive oxygen species (ROS) and reactive nitrogen oxide species (RNOS), protect mosquito cells. We identified an Anopheles stephensi 2-Cys Prx ortholog of Drosophila melanogaster Prx-4783, which protects fly cells against oxidative stresses. To assess function, AsPrx-4783 was overexpressed in D. melanogaster (S2) and in A. stephensi (MSQ43) cells and silenced in MSQ43 cells with RNA interference before treatment with various ROS and RNOS. Our data revealed that AsPrx-4783 and DmPrx-4783 differ in host cell protection and that AsPrx-4783 protects A. stephensi cells against stresses that are relevant to malaria parasite infection in vivo, namely nitric oxide (NO), hydrogen peroxide, nitroxyl, and peroxynitrite. Further, AsPrx-4783 expression is induced in the mosquito midgut by parasite infection at times associated with peak nitrosative and oxidative stresses. Hence, whereas the NO-mediated defense response is toxic to both host and parasite, AsPrx-4783 may shift the balance in favor of the mosquito. KeywordsMalaria; Mosquito; Peroxiredoxin; Plasmodium; Anopheles; Nitric oxide; Nitrosative stress; Free radicals It has long been recognized that reactive oxygen species (ROS) and, more recently, reactive nitrogen oxide species (RNOS) function to defend hosts against pathogens [1]. Although ROS and RNOS are cytotoxic to pathogens and parasites, they also induce oxidative and nitrosative stresses in the host and can damage host tissues [1]. Host protection against oxidative and nitrosative stress, therefore, is vital for homeostasis and hence survival. Gene products that confer protection against ROS are well known. In contrast, gene products that confer protection against RNOS have been identified, but are less well studied. The peroxiredoxins (Prxs) are a recently discovered family of antioxidant peroxidases that can reduce hydrogen peroxide and alkyl hydroperoxides to water and the corresponding alcohols, respectively, and can protect cells from widely divergent organisms against a variety of nitrosative stress challenges [2][3][4][5][6].Prxs do not show sequence homology to other known antioxidant enzymes. Crystal structures of PrxI, II, V, and VI have revealed that Prxs are novel members of the thioredoxin fold * Corresponding author. Fax: +1 530 752 8692. E-mail address: sluckhart@ucdavis.edu (S. Luckhart). NIH Public Access NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript superfamily [7,8]. Unlike most peroxidases-which contain a heme ring at their active site (e.g., cytochrome c peroxidase) or a redox-sensitive moiety like selenocysteine (glutathione peroxidase; GPx), vanadium (algal bro...

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Section: Discussionmentioning

confidence: 84%

A mosquito 2-Cys peroxiredoxin protects against nitrosative and oxidative stresses associated with malaria parasite infection

Peterson

Luckhart

2006

Free Radical Biology and Medicine

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“…The antioxidant activity of Prx is due to a reduction of hydroperoxide, with thioredoxin as an immediate hydrogen donor (Rodriguez et al, 2000). Perturbation in the expression of detoxification proteins has been found in insect subjected to an immune challenge, exposed to a temperature stress or to viral infections (de Morais Guedes et al, 2005;Lee et al, 2005). Using 2D gel analysis, Nguyen et al(2008) reported an increase in such types of proteins in the aphid Macrosiphum euphorbiae challenged by the parasitoids Aphidius nigripes or A. ervi.…”

Section: Detoxification Proteinsmentioning

confidence: 99%

Proteome changes in the plasma of Papilio xuthus (Lepidoptera: Papilionidae): effect of parasitization by the endoparasitic wasp Pteromalus puparum (Hymenoptera: Pteromalidae)

Zhu

Yè

Fang

et al. 2009

J. Zhejiang Univ. Sci. B

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Abstract:Although the biochemical dissection of parasitoid-host interactions is becoming well characterized, the molecular knowledge concerning them is minimal. In order to understand the molecular bases of the host immune response to parasitoid attack, we explored the response of Papilio xuthus parasitized by the endoparasitic wasp Pteromalus puparum using proteomic approach. By examining the differential expression of plasma proteins in the parasitized and unparasitized host pupae by two-dimensional (2D) electrophoresis, 16 proteins were found to vary in relation to parasitization compared with unparasitized control samples. All of them were submitted to identification by mass spectrometry coupled with a database search. The modulated proteins were found to fall into the following functional groups: humoral or cellular immunity, detoxification, energy metabolism, and others. This study contributes insights into the molecular mechanism of the relationships between parasitoids and their host insects.

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“…It is reported that temperature stress is a key mediator of the formation of ROS (Hariari et al, 1989;Rauen et al, 1999). In previous studies, insect enzymes, Gryllotalpa orientalis SOD1 (Kim et al, 2005b), Bombyx mori TPx (Lee et al, 2005) and G. orientalis Prx (Kim et al, 2005a), were up-regulated by bolt cold and heat stress. In this study, Bitxl induction by temperature stress, a mediator of ROS, suggests that Bitxl may play an important role as an antioxidant protein, by reducing the high level of intracellular hydrogen peroxide induced by extracellular stimuli such as low or high temperatures.…”

Section: Discussionmentioning

confidence: 92%

“…It is likely that the up-regulation of Bitxl is related to its role in protecting against oxidative damage caused by LPS stimulation. In another insect, the antioxidant protein, B. mori TPx, was significantly induced during viral infection (Lee et al, 2005). Furthermore, B. ignitus SOD1 was upregulated by LPS stimulation (Choi et al, in prep.).…”

Section: Discussionmentioning

confidence: 99%

A bumblebee thioredoxin-like protein gene that is up-regulated by a temperature stimulus and lipopolysaccharide injection

Choi¹,

Lee²,

Yoon³

et al. 2006

Eur. J. Entomol.

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Abstract.A thioredoxin-like protein (txl) gene was cloned from the bumblebee, Bombus ignitus. The B. ignitus txl (Bitxl) gene spans 1777 bp and consists of three introns and four exons coding for 285 amino acid residues with a conserved active site (CGPC). The deduced amino acid sequence of the Bitxl cDNA was 65% similar to the Drosophila melanogaster txl. Northern blot analysis revealed the presence of Bitxl transcripts in all tissues examined. When H2O2 was injected into the body cavity of B. ignitus workers, Bitxl mRNA expression was up-regulated in the fat body tissue. In addition, the expression levels of Bitxl mRNA in the fat body greatly increased when B. ignitus workers were exposed to low (4°C) or high (37°C) temperatures, or injected with lipopolysaccharide (LPS), which suggests that the Bitxl possibly protects against oxidative stress caused by extreme temperatures and bacterial infection.

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Characterization of a silkworm thioredoxin peroxidase that is induced by external temperature stimulus and viral infection

Cited by 134 publications

References 28 publications

A mosquito 2-Cys peroxiredoxin protects against nitrosative and oxidative stresses associated with malaria parasite infection

A mosquito 2-Cys peroxiredoxin protects against nitrosative and oxidative stresses associated with malaria parasite infection

Proteome changes in the plasma of Papilio xuthus (Lepidoptera: Papilionidae): effect of parasitization by the endoparasitic wasp Pteromalus puparum (Hymenoptera: Pteromalidae)

A bumblebee thioredoxin-like protein gene that is up-regulated by a temperature stimulus and lipopolysaccharide injection

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