Thermotolerance and HSP70 expression in the Mediterranean fruit fly Ceratitis capitata

Kalosaka, Katerina; Soumaka, Elisavet; Politis, Nikos; Mintzas, Anastassios C.

doi:10.1016/j.jinsphys.2009.02.002

Cited by 55 publications

(42 citation statements)

References 50 publications

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“…RHH has been observed in a number of Drosophila species (Chen et al, 1991;Loeschcke et al, 1997;reviewed in Hoffmann et al, 2003) and recently also in C. capitata (Kalosaka et al, 2009), but to our knowledge, such high temperature responses have not been documented in C. rosa. The physiological mechanisms underlying RHH involves the production of heat-shock proteins (HSPs) which can act as molecular chaperones by preventing accumulation of structurally damaged proteins (reviewed in Sørensen et al, 2003;Hoffmann et al, 2003).…”

Section: Discussionmentioning

confidence: 74%

Phenotypic plasticity of thermal tolerance contributes to the invasion potential of Mediterranean fruit flies (Ceratitis capitata)

Nyamukondiwa

Kleynhans

Terblanche

2010

Ecological Entomology

101

108

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Abstract. 1. The invasion success of Ceratitis capitata probably stems from physiological, morphological, and behavioural adaptations that enable them to survive in different habitats. However, it is generally poorly understood if variation in acute thermal tolerance and its phenotypic plasticity might be important in facilitating survival of C. capitata upon introduction to novel environments.2. Here, by comparison of widely distributed C. capitata with a narrowly distributed congener, C. rosa, we show that both species have similar levels of survival to acute high and low temperature exposures under common rearing conditions. However, these species differ dramatically in the time-course of plastic responses to acute low temperature treatments.3. The range of temperatures that induce rapid cold hardening (RCH) are similar for both species. However, C. capitata has two distinct advantages over C. rosa. First, at 5• C C. capitata develops RCH significantly faster than C. rosa. Second, C.capitata maintains a RCH response longer than C. rosa (8 vs. 0.5 h). 4. A simple population survival model, based on the estimated time-course of RCH responses determined for both species, was undertaken to simulate time to extinction for both species introduced into a similar thermally variable environment. The model showed that time to extinction is greater for C. capitata than for C. rosa, especially in habitats where temperatures frequently drop below 10• C.5. Thus, variation in RCH responses may translate into significant variation in survival upon introduction to novel thermal habitats for C. capitata, particularly in cooler and more thermally variable geographic regions, and may contribute to their ongoing invasion success relative to other, more geographically constrained Ceratitis species.

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Section: Discussionmentioning

confidence: 74%

Phenotypic plasticity of thermal tolerance contributes to the invasion potential of Mediterranean fruit flies (Ceratitis capitata)

Nyamukondiwa

Kleynhans

Terblanche

2010

Ecological Entomology

101

108

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“…These results indicated that increased Se-Hsp70 expression under thermal stress is due to an increase of the Se-hsp70 RNA. Positive relationship between Hsp70 protein expression and hsp70 gene expression always occurs at other insect species (Kalosaka et al 2009). …”

Section: Discussionmentioning

confidence: 99%

Cloning of the heat shock protein 90 and 70 genes from the beet armyworm, Spodoptera exigua, and expression characteristics in relation to thermal stress and development

Jiang

Zhai

Wang

et al. 2012

Cell Stress and Chaperones

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Two full-length cDNAs of heat shock protein (HSP) genes (Se-hsp90 and Se-hsp70) were cloned from the beet armyworm, Spodoptera exigua, and their expression was investigated in relation to cold shock, heat shock, and development. The open reading frames of Se-hsp90 and Sehsp70 are 2,154 and 2,004 bp in length, encoding polypeptides of 717 and 667 amino acids with a molecular mass of 82.6 and 72.5 kDa, respectively. Both genes showed high similarity to their counterparts in other species. Transcriptional expression profiles revealed that both genes were significantly up-regulated under thermal stress. However, the temperature at which expression level became significantly higher than that of controls varied between genes. Intensity of response to temperature was more intense for Se-hsp70 than for Se-hsp90, regardless of temperature or developmental stage. However, intensities of response to temperature of either Se-hsp90 or Se-hsp70 varied with developmental stage. The basal expression of both genes was highest in young larvae and decreased with age. Translational expression of Se-Hsp70 was observed by using Western blot, the expression profiles of Se-Hsp70 protein were in high agreement with those of Se-hsp70 RNA under heat or cold stress in larvae and pupae. However, it does not completely accord with that of Sehsp70 RNA expression during development without thermal stress. These results indicated that, in addition to heat shock responses, both Se-hsp90 and Se-hsp70 might be involved in development.

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“…Alternatively, the heat shock temperatures used may have failed to induce this stress response in tadpoles from the 28°C treatment, which may explain why protein abundance in this group did not reflect their increased CTmax. While Hsp70 expression may in some cases be correlated with upper thermal limits (Kalosaka et al, 2009;Fangue et al, 2011), abundance of this protein does not always predict plasticity of this trait (Healy and Schulte, 2011;Dahlgaard et al, 1998), highlighting the difficulty in understanding the mechanistic basis of complex physiological traits. Furthermore, the independent effects of temperature and UVR on the abundance of Hsp72 illustrate that understanding the effects of single stressors on mechanistic traits may not explain complex pathways at After a heat shock at 34°C, tadpoles exposed to UVR (grey bars) had higher Hsp72 density than tadpoles not exposed to UVR (white bars; F 1, 32.62 = 6.05, p = 0.019) but this was not affected by temperature treatment (F 2, 32.62 = 3.05, p = 0.06).…”

Section: Discussionmentioning

confidence: 99%

“…Upper thermal limits are often correlated with the expression of heat shock proteins (Hsps) (Gong and Golic, 2006;Kalosaka et al, 2009). Hsps function as molecular chaperones, which prevent damage when cells experience environmental stress by refolding and precluding the aggregation of non-native proteins (Feder and Hofmann, 1999b).…”

Section: Introductionmentioning

confidence: 99%

Plasticity of protective mechanisms only partially explains interactive effects of temperature and UVR on upper thermal limits

Kern

Cramp

Seebacher

et al. 2015

Comparative Biochemistry and Physiology Part A: Molecular &

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Thermotolerance and HSP70 expression in the Mediterranean fruit fly Ceratitis capitata

Cited by 55 publications

References 50 publications

Phenotypic plasticity of thermal tolerance contributes to the invasion potential of Mediterranean fruit flies (Ceratitis capitata)

Phenotypic plasticity of thermal tolerance contributes to the invasion potential of Mediterranean fruit flies (Ceratitis capitata)

Cloning of the heat shock protein 90 and 70 genes from the beet armyworm, Spodoptera exigua, and expression characteristics in relation to thermal stress and development

Plasticity of protective mechanisms only partially explains interactive effects of temperature and UVR on upper thermal limits

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