Functional evaluation of Heat Shock Proteins 70 (HSP70/HSC70) on Rhodnius prolixus (Hemiptera, Reduviidae) physiological responses associated with feeding and starvation

Paim, Rafaela M.M.; Araújo, Ricardo Nascimento; Leis, Miguel; Sant’Anna, Maurício Roberto Viana; Gontijo, Nelder Figueiredo; Lazzari, Cláudio R.; Pereira, Marcos H.

doi:10.1016/j.ibmb.2016.07.011

Cited by 48 publications

(70 citation statements)

References 51 publications

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“…In that respect, Hsp70 is the most widely studied HSP as a response to heat and many other stresses [ 24 , 28 ]. Interestingly, it was reported that a Hsp70 knockdown in R. prolixus results into a significant alteration in the physiological responses to a blood meal [ 29 ]. In this case, the insects die prematurely after blood feeding after showing an alteration in the blood digestion process and a reduction in energy metabolism and immune response [ 29 ].…”

Section: Resultsmentioning

confidence: 99%

High-Throughput Identification of the Rhodnius prolixus Midgut Proteome Unravels a Sophisticated Hematophagic Machinery

et al. 2020

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Chagas disease is one of the most common parasitic infections in Latin America, which is transmitted by hematophagous triatomine bugs, of which Rhodnius prolixus is the vector prototype for the study of this disease. The protozoan parasite Trypanosoma cruzi, the etiologic agent of this disease, is transmitted by the vector to humans through the bite wound or mucosa. The passage of the parasite through the digestive tract of its vector constitutes a key step in its developmental cycle. Herewith, by a using high-throughput proteomic tool in order to characterize the midgut proteome of R. prolixus, we describe a set of functional groups of proteins, as well as the biological processes in which they are involved. This is the first proteomic analysis showing an elaborated hematophagy machinery involved in the digestion of blood, among which, several families of proteases have been characterized. The evaluation of the activity of cathepsin D proteases in the anterior part of the digestive tract of the insect suggested the existence of a proteolytic activity within this compartment, suggesting that digestion occurs early in this compartment. Moreover, several heat shock proteins, blood clotting inhibitors, and a powerful antioxidant enzyme machinery against reactive oxygen species (ROS) and cell detoxification have been identified. Highlighting the complexity and importance of the digestive physiology of insects could be a starting point for the selection of new targets for innovative control strategies of Chagas disease.

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Section: Resultsmentioning

confidence: 99%

High-Throughput Identification of the Rhodnius prolixus Midgut Proteome Unravels a Sophisticated Hematophagic Machinery

et al. 2020

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“…1 legend. www.nature.com/scientificreports www.nature.com/scientificreports/ of SfHsp19.74, SfHsp20. 15,SfHsp24.35,SfHsp26.61, and SfHsp29.00 increased by 5-to 34-fold. In other mixed tissues, only four SfHsp genes were induced by heat-shock (SfHsp70A/B at 344-fold, SfHsp20.15 at 16-fold, SfHsp20.71 at 40-fold, and SfHsp21.37 at 42-fold).…”

Section: Figurementioning

confidence: 94%

“…Based on their molecular mass and function, insect Hsp can be divided into four major families, small heat-shock proteins, Hsp60, Hsp70, and Hsp 90 2 . Expression of Hsp from a wide range of insect species have been reported to be induced and modulated by abiotic stressors, including extreme temperature 3-5 , ultraviolet radiation 6,7 , pesticides 8,9 , heavy metals 10,11 , desiccation 12-14 , starvation 15,16 , and anoxia/hypoxia 17-19 , as well as several biotic insults, including parasites 20,21 , pathogens 22,23 , and high population density 24 . In recent years, the availability of both transcriptome and genome data greatly contributed to the identification of an increasing number of Hsp genes from diverse insect species and promoted their functional studies 5,9,[25][26][27] .…”

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confidence: 99%

Identification and functional analysis of promoters of heat-shock genes from the fall armyworm, Spodoptera frugiperda

Chen

Tan

Palli

2020

Sci Rep

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The functional information on heat-shock proteins (Hsp) and heat-shock promoters from an important agricultural insect pest, Spodoptera frugiperda, is still lacking. We conducted a genomewide identification of Hsp genes and identified a total of 21 genes belonging to four major insect Hsp families (small heat-shock proteins, Hsp60, Hsp70, and Hsp90) in S. frugiperda. Expression of most of S. frugiperda (SfHsp) genes could be detected in Sf9 cells, embryos and larval tissues of S. frugiperda. The heat-inducible activity of heat-shock promoters from several SfHsp genes was tested in Sf9 cells and embryos. The promoter of SfHsp70D showed the high constitutive activity in cell line and embryos, while the activity of SfHsp20.15 and SfHsp20.71 promoters was most dramatically induced in Sf9 cells and embryos. In embryos, the heat-induced activity of SfHsp20.71 and SfHsp70D promoters outperformed commercially used ie1 and ie2 promoters. The heat-induced activity of SfHsp70D and SfHsp19.07 promoters were more robust than ie2 promoter in Sf9 cells. These SfHsp promoters with high basal activity or with heat-induced activity from low basal activity, could be used in S. frugiperda or other lepidopteran insects for many applications including transgenesis and genome editing.Heat-shock proteins (Hsp) are abundant and ubiquitously expressed in insects playing important roles in enhancing abiotic and biotic stress tolerance, as well as regulating normal development 1,2 . Based on their molecular mass and function, insect Hsp can be divided into four major families, small heat-shock proteins, Hsp60, Hsp70, and Hsp 90 2 . Expression of Hsp from a wide range of insect species have been reported to be induced and modulated by abiotic stressors, including extreme temperature 3-5 , ultraviolet radiation 6,7 , pesticides 8,9 , heavy metals 10,11 , desiccation 12-14 , starvation 15,16 , and anoxia/hypoxia 17-19 , as well as several biotic insults, including parasites 20,21 , pathogens 22,23 , and high population density 24 . In recent years, the availability of both transcriptome and genome data greatly contributed to the identification of an increasing number of Hsp genes from diverse insect species and promoted their functional studies 5,9,[25][26][27] . However, information of Hsp genes from a destructive insect pest, Spodoptera frugiperda, is still limited 23,28 .The stress-inducible expression of Hsp gene is conferred by binding of heat-shock factor (HSF) to heat-shock elements (HSEs), which consists of arrays of the 5-bp unit NGAAN arranged as inverted repeats in the promoter region 29 . Since exposure to high temperature is likely the simpler way to achieve inducible expression of insect Hsp genes, the promoters of insect Hsp genes are good candidates to drive the expression of foreign genes by heat-shock. Analysis of heat-shock promoters is still limited to a few model insect species. Promoters of Hsp26, Hsp68, Hsp70, and Hsp82, from Drosophila melanogaster have been used to drive the heat-shock induced expression of transposase...

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“…The ability to adapt to temperature fluctuations is critical for insect survival, and the induction of Hsp70s generally coincides with increased thermotolerance. The characterization of Hsp70 and Hsc70 homologues has been described for insects assigned to diverse orders (Rybczynski and Gilbert, 2000;Rinehart et al, 2007;Tungjitwitayakul et al, 2008;Gkouvitsas et al, 2010;Huang and Kang, 2010;Moribe et al, 2010;Sonoda et al, 2010;Cheng et al, 2016;Paim et al, 2016). Furthermore, advances in genome sequencing has resulted in the identification of novel insect Hsp70s.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional regulation of heat shock protein 70 genes by class I histone deacetylases in the red flour beetle, Tribolium castaneum

Chen

Jiang

et al. 2019

Insect Molecular Biology

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The regulatory function of histone acetylation in the expression of genes encoding heat shock proteins (Hsps) has been documented in Drosophila melanogaster; however, knowledge of the role of acetylation in modulating Hsps in other insect pests is limited. In this study, two full‐length cDNAs encoding inducible Hsp70 (designated TcHsp70) and heat shock cognate 70 (TcHsc70) were isolated and characterized in the red flour beetle, Tribolium castaneum. TcHsp70 and TcHsc70 cDNAs were 2256 and 2132 bp and encoded 1941‐ and 1893‐bp open reading frames, respectively. The deduced TcHsp70 and TcHsc70 proteins contained 646 and 630 amino acids, respectively, and contained sequences typical of the Hsp70 family, including the EEVD motif for cytoplasmic localization. Expression patterns after heat shock indicated that TcHsp70 was strongly heat‐inducible, whereas the expression level of TcHsc70 remained unchanged under heat shock. RNA interference‐mediated knock‐down of three genes encoding class I histone deacetylases differentially influenced both basal and heat shock inducible expression of TcHsp70 and TcHsc70, suggesting the involvement of histone acetylation in epigenetic regulation of Hsp70 transcription in T. castaneum.

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Functional evaluation of Heat Shock Proteins 70 (HSP70/HSC70) on Rhodnius prolixus (Hemiptera, Reduviidae) physiological responses associated with feeding and starvation

Cited by 48 publications

References 51 publications

High-Throughput Identification of the Rhodnius prolixus Midgut Proteome Unravels a Sophisticated Hematophagic Machinery

High-Throughput Identification of the Rhodnius prolixus Midgut Proteome Unravels a Sophisticated Hematophagic Machinery

Identification and functional analysis of promoters of heat-shock genes from the fall armyworm, Spodoptera frugiperda

Transcriptional regulation of heat shock protein 70 genes by class I histone deacetylases in the red flour beetle, Tribolium castaneum

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