Identification of heat shock cognate protein 70 gene (<i>Alhsc</i>70) of <i>Apolygus lucorum</i> and its expression in response to different temperature and pesticide stresses

Sun, Yuhan; Zhao, Jing; Sheng, Yang; Xiao, Yingfang; Zhang, Yongjun; Bai, Liang; Tan, Yongan; Xiao, Liubin; Xu, Guangchun

doi:10.1111/1744-7917.12193

Cited by 51 publications

(35 citation statements)

References 33 publications

(47 reference statements)

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“…Some studies suggest that HSC70 is expressed constitutively and thus, not stress-inducible [62]. Others report that HSC70 is involved in thermoregulation, as well as protein synthesis, folding, transport, and degradation [63]. Our results for HSC70 indicated that its expression is also sensitive to low temperature.…”

Section: Discussionsupporting

confidence: 51%

Transcriptomic analysis to uncover genes affecting cold resistance in the Chinese honey bee (Apis cerana cerana)

Niu

Zhao

et al. 2017

PLoS ONE

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The biological activity and geographical distribution of honey bees is strongly temperature-dependent, due to their ectothermic physiology. In China, the endemic Apis cerana cerana exhibits stronger cold hardiness than Western honey bees, making the former species important pollinators of winter-flowering plants. Although studies have examined behavioral and physiological mechanisms underlying cold resistance in bees, data are scarce regarding the exact molecular mechanisms. Here, we investigated gene expression in A. c. cerana under two temperature treatments, using transcriptomic analysis to identify differentially expressed genes (DEGs) and relevant biological processes, respectively. Across the temperature treatments, 501 DEGs were identified. A gene ontology analysis showed that DEGs were enriched in pathways related to sugar and amino acid biosynthesis and metabolism, as well as calcium ion channel activity. Additionally, heat shock proteins, zinc finger proteins, and serine/threonine-protein kinases were differentially expressed between the two treatments. The results of this study provide a general digital expression profile of thermoregulation genes responding to cold hardiness in A. c. cerana. Our data should prove valuable for future research on cold tolerance mechanisms in insects, and may be beneficial in breeding efforts to improve bee hardiness.

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Section: Discussionsupporting

confidence: 51%

Transcriptomic analysis to uncover genes affecting cold resistance in the Chinese honey bee (Apis cerana cerana)

Niu

Zhao

et al. 2017

PLoS ONE

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“…Hsp70 is activated under stress conditions such as heat, virus infection, and oxidative stress (6,(10)(11)(12)(13)(14)(15)(16)(17)(18)(19). Whereas Hsc70 is generally expressed constitutively, it can also be induced by environmental stresses such as thermal and pesticide stress, as well as virus infection (10,(20)(21)(22)(23). It has also been found that Hsp70 and Hsc70 may complement each other in a synergistic manner to preserve cellular integrity during metabolic challenges (24).…”

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confidence: 99%

Cucumber Necrosis Virus Recruits Cellular Heat Shock Protein 70 Homologs at Several Stages of Infection

Alam

Rochon

2016

J Virol

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RNA viruses often depend on host factors for multiplication inside cells due to the constraints of their small genome size and limited coding capacity. One such factor that has been exploited by several plant and animal viruses is heat shock protein 70 (HSP70) family homologs which have been shown to play roles for different viruses in viral RNA replication, viral assembly, disassembly, and cell-to-cell movement. Using next generation sequence analysis, we reveal that several isoforms of Hsp70 and Hsc70 transcripts are induced to very high levels during cucumber necrosis virus (CNV) infection of Nicotiana benthamiana and that HSP70 proteins are also induced by at least 10-fold. We show that HSP70 family protein homologs are co-opted by CNV at several stages of infection. We have found that overexpression of Hsp70 or Hsc70 leads to enhanced CNV genomic RNA, coat protein (CP), and virion accumulation, whereas downregulation leads to a corresponding decrease. Hsc70-2 was found to increase solubility of CNV CP in vitro and to increase accumulation of CNV CP independently of viral RNA replication during coagroinfiltration in N. benthamiana. In addition, virus particle assembly into virus-like particles in CP agroinfiltrated plants was increased in the presence of Hsc70-2. HSP70 was found to increase the targeting of CNV CP to chloroplasts during infection, reinforcing the role of HSP70 in chloroplast targeting of host proteins. Hence, our findings have led to the discovery of a highly induced host factor that has been co-opted to play multiple roles during several stages of the CNV infection cycle. IMPORTANCEBecause of the small size of its RNA genome, CNV is dependent on interaction with host cellular components to successfully complete its multiplication cycle. We have found that CNV induces HSP70 family homologs to a high level during infection, possibly as a result of the host response to the high levels of CNV proteins that accumulate during infection. Moreover, we have found that CNV co-opts HSP70 family homologs to facilitate several aspects of the infection process such as viral RNA, coat protein and virus accumulation. Chloroplast targeting of the CNV CP is also facilitated, which may aid in CNV suppression of host defense responses. Several viruses have been shown to induce HSP70 during infection and others to utilize HSP70 for specific aspects of infection such as replication, assembly, and disassembly. We speculate that HSP70 may play multiple roles in the infection processes of many viruses. C ucumber necrosis virus (CNV) is a positive-strand RNA virus in the genus Tombusvirus, family Tombusviridae (1). The CNV genome is monopartite and consists of ϳ4.7 kb of positive polarity single-stranded RNA. The genome contains five open reading frames (ORFs) which encode five different proteins: the auxiliary replicase factor (p33), the RNA-dependent RNA polymerase (RdRp) (p92), the coat protein (CP; p41), the movement protein (p21), and the silencing suppressor (p20) (Fig. 1A). The UAG stop codon of the p...

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“…; Sun et al . ). Our results, obtained with H. vitessoides , indicated that HSP60 transcripts increased dramatically in larvae and pupae that were heat‐stressed at 40°C and were upregulated in adults that were heat‐stressed at 35°C and 40°C.…”

Section: Discussionmentioning

confidence: 97%

Induced expression of three heat shock proteins mediated by thermal stress in Heortia vitessoides (Lepidoptera: Crambidae)

Cheng

Wang

Lyu

et al. 2018

Entomological Research

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To gain an insight into the function of heat shock proteins (HSPs) in insects during thermal stress, three HSP cDNAs were identified in the transcriptome of adult Heortia vitessoides, one of the most destructive defoliating pests in Aquilaria sinensis (Loureiro) Sprenger forests. The open reading frames of HvHsp60, HvHsp70, and HvHsp90 were 1,719, 2,070, and 2,151 bp in length, respectively, and encoded proteins with molecular weights of 61.05, 75.02, and 82.23 kDa, respectively. Sequence analysis revealed that all three HSPs were highly conserved in structure. Regarding the stage‐specific expression profiles, HvHsp60, HvHsp70, and HvHsp90 mRNAs were detected in all developmental stages. Regarding the tissue‐specific expression profiles, the expression levels of the three HSP genes were different in various larval and adult tissues. Moreover, the expression patterns of heat‐stressed larvae, pupae, and adults indicated that HvHsp60, HvHsp70, and HvHsp90 were heat‐inducible. In particular, HvHsp60 transcripts increased dramatically in larvae and pupae that were heat‐stressed at 40°C and were upregulated in adults that were heat‐stressed at 35°C and 40°C. The expression of HvHsp70 significantly increased in all of the three different developmental stages at 35°C, 40°C, and 45°C. The expression of HvHsp90 obviously increased at 30°C, 35°C, and 40°C in larvae and could be induced at 35°C in pupae and adults. The results suggest that HSP60, HSP70, and HSP90 play a major role in protecting H. vitessoides against high‐temperature stress.

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Identification of heat shock cognate protein 70 gene (Alhsc70) of Apolygus lucorum and its expression in response to different temperature and pesticide stresses

Cited by 51 publications

References 33 publications

Transcriptomic analysis to uncover genes affecting cold resistance in the Chinese honey bee (Apis cerana cerana)

Transcriptomic analysis to uncover genes affecting cold resistance in the Chinese honey bee (Apis cerana cerana)

Cucumber Necrosis Virus Recruits Cellular Heat Shock Protein 70 Homologs at Several Stages of Infection

Induced expression of three heat shock proteins mediated by thermal stress in Heortia vitessoides (Lepidoptera: Crambidae)

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