Expression patterns and structural modelling of Hsp70 and Hsp90 in a fish-borne zoonotic nematode Anisakis pegreffii

Chen, Hui-Yu; Cheng, Yi-Sheng

doi:10.1016/j.vetpar.2015.07.006

Cited by 15 publications

(12 citation statements)

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“…HSPs are a family of highly conserved proteins that play primary roles in maintaining cellular homeostasis but whose increased expression in the presence of conditions of stress such as sudden changes in temperature, injuries and infections, is responsible for the activation of a cascade of immune-molecular events that culminate in inflammatory responses [ 31 ]. In particular, in a recent study [ 32 ], the expression of an HSP 70 from A . pegreffii was increased in L4s compared with L3s, which may be linked to a response of the parasite to the heat stress that immediately follows infection [ 32 ].…”

Section: Discussionmentioning

confidence: 99%

The Anisakis Transcriptome Provides a Resource for Fundamental and Applied Studies on Allergy-Causing Parasites

Baird

Aibinu

et al. 2016

PLoS Negl Trop Dis

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BackgroundFood-borne nematodes of the genus Anisakis are responsible for a wide range of illnesses (= anisakiasis), from self-limiting gastrointestinal forms to severe systemic allergic reactions, which are often misdiagnosed and under-reported. In order to enhance and refine current diagnostic tools for anisakiasis, knowledge of the whole spectrum of parasite molecules transcribed and expressed by this parasite, including those acting as potential allergens, is necessary.Methodology/Principal FindingsIn this study, we employ high-throughput (Illumina) sequencing and bioinformatics to characterise the transcriptomes of two Anisakis species, A. simplex and A. pegreffii, and utilize this resource to compile lists of potential allergens from these parasites. A total of ~65,000,000 reads were generated from cDNA libraries for each species, and assembled into ~34,000 transcripts (= Unigenes); ~18,000 peptides were predicted from each cDNA library and classified based on homology searches, protein motifs and gene ontology and biological pathway mapping. Using comparative analyses with sequence data available in public databases, 36 (A. simplex) and 29 (A. pegreffii) putative allergens were identified, including sequences encoding ‘novel’ Anisakis allergenic proteins (i.e. cyclophilins and ABA-1 domain containing proteins).Conclusions/SignificanceThis study represents a first step towards providing the research community with a curated dataset to use as a molecular resource for future investigations of the biology of Anisakis, including molecules putatively acting as allergens, using functional genomics, proteomics and immunological tools. Ultimately, an improved knowledge of the biological functions of these molecules in the parasite, as well as of their immunogenic properties, will assist the development of comprehensive, reliable and robust diagnostic tools.

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Section: Discussionmentioning

confidence: 99%

The Anisakis Transcriptome Provides a Resource for Fundamental and Applied Studies on Allergy-Causing Parasites

Baird

Aibinu

et al. 2016

PLoS Negl Trop Dis

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“…In particular, the mRNA expression levels of some selected genes (i.e., Nas-13, EF-TsMt, SFX2, dhs) were found to be significantly higher in A. simplex (s. l.) third stage larvae, compared to the fourth stage larvae [30]. Furthermore, the expression patterns of Heat shock proteins (i.e., Hsp70 and Hsp90) appeared to be modulated in L3 versus L4 stage larvae of A. pegreffii, with higher expression profiles in L4 larvae [12]. However, the expression profiles of the genes coding immuno-related proteins in L3 larvae of Anisakis in response to the temperature were never investigated.…”

Section: Introductionmentioning

confidence: 90%

Gene expression profiles of antigenic proteins of third stage larvae of the zoonotic nematode Anisakis pegreffii in response to temperature conditions

et al. 2019

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Anisakis pegreffii, a recognised etiological agent of human anisakiasis, is a parasite of homeothermic hosts at the adult stage and of ectothermic hosts at the third larval stage. Among distinct factors, temperature appears to be crucial in affecting parasite hatching, moulting and to modulate parasite-host interaction. In the present study, we investigated the gene transcripts of proteins having an antigenic role among excretory secretory products (ESPs) (i.e., a Kunitz-type trypsin inhibitor, A.peg-1; a glycoprotein, A.peg-7; and the myoglobin, A.peg-13) after 24 h, in A. pegreffii larvae maintained in vitro, under controlled temperature conditions. Temperatures were 37 °C and 20 °C, resembling respectively homeothermic and ectothermic hosts conditions, and 7 °C, the cold stress condition post mortem of the fish host. Primers of genes coding for these ESPs to be used in quantitative real-time PCR were newly designed, and qRT-PCR conditions developed. Expression profiles of the genes A.peg-1 and A.peg-13 were significantly up-regulated at 20 °C and 37 °C, with respect to the control (larvae kept at 2 °C for 24 h). Conversely, transcript profiles of A.peg-7 did not significantly change among the chosen temperature conditions. In accordance with the observed transcript profiles, sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) revealed the presence of the three target ESPs at 37 °C, while only A.peg-13 was observed at 7 °C. The results suggest that temperature conditions do regulate the gene expression profiles of A.peg-1 and A.peg-13 in A. pegreffii larvae. However, regulation of the glycoprotein A.peg-7 is likely to be related to other factors such as the host’s immune response.

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“…Heat shock response of cells and tissues presumably is not affected directly by temperature but to the accumulation of these unfolded proteins (Richter et al, 2010). Arrigo (2000) reported that organisms respond to lethal effects of hyperthermia through protection of heat shock proteins (Hsps), a family of highly conserved proteins that are found in all organisms from prokaryotes to mammals (Hunt, Morimoto, 1985;Lindquist, 1986;Fast et al, 2002;Chen et al, 2015). Hsps are necessary for the normal functioning of the cell structures in response to environmental Thermal induction of heat shock proteins Hsp70 and Hsp90 in nemerteans refolding of damaged proteins (Glover, Lindquist, 1998;Maloyan et al, 1999;Young et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

“…Eukaryotic Hsp90 proteins have functionally conserved N-termini and C-termini connected by a middle region containing highly charged and hydrophobic regions with variable length (Pratt, Toft, 2003). Conserved sequences for Hsp70 and Hsp90 have been identified in human, mouse, rat, insects, nematodes, yeasts, plants, and virus (Hunt, Morimoto, 1985;Choi et al, 2008;Liang et al, 2013;Chen et al, 2015). The sequence identities ranged from 76.7 to 80.7% for Hsp70 and 73.8 to 77.6% for Hsp90 between human and nematodes (Chen et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Thermal induction of heat shock proteins Hsp70 and Hsp90 in tissues of the nemerteans Lineus alborostratus Takakura, 1898 and Quasitetrastemma stimpsoni (Chernyshev, 1992)

2018

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Intertidal ribbon worms in the phylum Nemertea live in environments where temperature and salinity can vary widely depending on the tidal fluctuations. Heat shock proteins (Hsps) are expressed by cells in their physiological responses to these changing abiotic factors. To understand the role of Hsps, the presence of Hsp70 and Hsp90 was determined by western blotting in two nemertean species, Lineus alborostratus and Quasitetrastemma stimpsoni after 2-and 4-h thermal stress. Additionally, their tissue distributions of these Hsps were detected by immunohistochemistry. Both Hsps were detected in the two nemertean species. In L. alborostratus, Hsp70 and Hsp90 immunoreactivities were detected in the body wall, specifically in the epidermal and cutis cells, as well as in the epithelia of the stomach and proboscis; Hsp immunoreactivities in these cells and tissues appeared higher in the thermally-stressed nemerteans compared to the controls. For both the control and thermally-stressed Q. stimpsoni, Hsp70 and Hsp90 were localized in the epidermis, while the stomach epithelium and neurons of the lateral nerve cord showed low immunoreactivities in the thermally-stressed worms. In thermally-stressed L. alborostratus, the proboscis showed a marked increase of Hsp70 and Hsp90 immunoreactivity. Active immunoreactivities were observed in the supra-epidermal granules in both ribbonworm species, especially Q. stimpsoni. Accumulation of Hsp70 and Hsp90 in the body wall and the gastric epithelium of nemerteans may indicate their importance during their physiological response to thermal stress.

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Expression patterns and structural modelling of Hsp70 and Hsp90 in a fish-borne zoonotic nematode Anisakis pegreffii

Cited by 15 publications

References 56 publications

The Anisakis Transcriptome Provides a Resource for Fundamental and Applied Studies on Allergy-Causing Parasites

The Anisakis Transcriptome Provides a Resource for Fundamental and Applied Studies on Allergy-Causing Parasites

Gene expression profiles of antigenic proteins of third stage larvae of the zoonotic nematode Anisakis pegreffii in response to temperature conditions

Thermal induction of heat shock proteins Hsp70 and Hsp90 in tissues of the nemerteans Lineus alborostratus Takakura, 1898 and Quasitetrastemma stimpsoni (Chernyshev, 1992)

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