Thermal resistance, developmental rate and heat shock proteins in Artemia franciscana, from San Francisco Bay and southern Vietnam

Clegg, James S.; Jackson, Susan A.; Hòa, Nguyễn Văn; Sorgeloos, Patrick

doi:10.1016/s0022-0981(00)00239-2

Cited by 70 publications

(64 citation statements)

References 36 publications

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“…In line with these observations, induced Hsp synthesis confers secondary hyperthermic stress tolerance on Artemia (Clegg et al 2000a;Frankenberg et al 2000). In other work, a nonlethal heat shock promoted Hsp70 expression and crossprotected Artemia larvae against Vibrio challenge (Sung et al 2007).…”

Section: Introductionsupporting

confidence: 55%

“…Protein extraction was performed essentially as described previously (Clegg et al 2000a;Sung et al 2007). Artemia larvae were collected on 50-μm sieves and rinsed with icecold distilled water.…”

Section: Protein Extraction Sds Polyacrylamide Gel Electrophoresis Amentioning

confidence: 99%

“…Ten microliters samples representing 1.0mg (wet weight) of animals were applied to each lane of a 10% SDS polyacrylamide gel (Frankenberg et al 2000;Clegg et al 2000a) before electrophoresis. Two gels were run simultaneously, and one was stained with Coomassie Biosafe (BioRad Laboratories, USA).…”

Section: Protein Extraction Sds Polyacrylamide Gel Electrophoresis Amentioning

confidence: 99%

“…After recovery from an initial stress, 50 larvae were transferred in triplicate into separate Falcon tubes containing 30ml of seawater, exposed to heat shock at 42°C for 30min (Clegg et al 2000a), and then transferred to 28°C. Induced thermotolerance was determined 12h after heating by counting actively swimming larvae.…”

Section: Determination Of Induced Thermotolerance In Artemia Larvaementioning

confidence: 99%

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Exposure of gnotobiotic Artemia franciscana larvae to abiotic stress promotes heat shock protein 70 synthesis and enhances resistance to pathogenic Vibrio campbellii

Sung

Pineda

MacRae

et al. 2008

Cell Stress and Chaperones

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Larvae of the brine shrimp Artemia franciscana serve as important feed in fish and shellfish larviculture; however, they are subject to bacterial diseases that devastate entire populations and consequently hinder their use in aquaculture. Exposure to abiotic stress was shown previously to shield Artemia larvae against infection by pathogenic Vibrio, with the results suggesting a mechanistic role for heat shock protein 70. In the current report, combined hypothermic/hyperthermic shock followed by recovery at ambient temperature induced Hsp70 synthesis in Artemia larvae. Thermotolerance was also increased as was protection against infection by Vibrio campbellii, the latter indicated by reduced mortality and lower bacterial load in challenge tests. Resistance to Vibrio improved in the face of declining body mass as demonstrated by measurement of ash-free dry weight. Hypothermic stress only and acute osmotic insult did not promote Hsp70 expression and thermotolerance in Artemia larvae nor was resistance to Vibrio challenge augmented. The data support a causal link between Hsp70 accumulation induced by abiotic stress and enhanced resistance to infection by V. campbellii, perhaps via stimulation of the Artemia immune system. This possibility is now under investigation, and the work may reveal fundamental properties of crustacean immunity. Additionally, the findings are important in aquaculture where development of procedures to prevent bacterial infection of feed stock such as Artemia larvae is a priority.

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Section: Introductionsupporting

confidence: 55%

Section: Protein Extraction Sds Polyacrylamide Gel Electrophoresis Amentioning

confidence: 99%

Section: Protein Extraction Sds Polyacrylamide Gel Electrophoresis Amentioning

confidence: 99%

Section: Determination Of Induced Thermotolerance In Artemia Larvaementioning

confidence: 99%

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Exposure of gnotobiotic Artemia franciscana larvae to abiotic stress promotes heat shock protein 70 synthesis and enhances resistance to pathogenic Vibrio campbellii

Sung

Pineda

MacRae

et al. 2008

Cell Stress and Chaperones

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“…Bacteria were homogenized by rapid agitation with 0.1 mm diameter glass beads in cold buffer K (150 mM sorbitol, 70 mM potassium gluconate, 5 mM MgCl 2 , 5 mM NaH 2 PO 4 , 40 mM HEPES, pH 7.4) [21] containing protease inhibitor cocktail (Catalogue #P8465; SigmaeAldrich, Inc.) at the highest recommended level. Subsequent to centrifugation at 2200 Â g for 1 min at 4 C, supernatant protein concentrations were determined by the Bradford method [22] using bovine serum albumin as standard.…”

Section: Protein Extraction Detection and Analysismentioning

confidence: 99%

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Baruah

Ranjan

Sorgeloos

et al. 2010

Fish & Shellfish Immunology

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a b s t r a c tThe Hsp70 class of heat shock proteins (Hsps) has been implicated at multiple points in the immune response of both vertebrates and invertebrates. This class of chaperones is highly conserved in both sequence and structure, from prokaryotes to higher eukaryotes. In view of their high degree of homology, it was assumed that these Hsp70 proteins derived either from the prokaryotes or eukaryotes would have similar functions, especially in relation to their protective ability in a challenge assay. To verify this, we compared two evolutionary diverse Hsp70s, Artemia Hsp70 and Escherichia coli Hsp70 equivalent DnaK (each overproduced in E.coli), for their ability to protect Artemia against Vibrio challenge. Results showed that Artemia fed with E. coli producing Artemia Hsp70 or DnaK proteins, as assessed by immune-probing in western blots, survived better in a Vibrio challenge assay. The observed effects could be due to enhancement of the Artemia immune system as phenoloxidase activity was found to be increased by these proteins. These two Hsp70 proteins exhibit a high degree of homology, particularly in the peptidebinding domain (the putative innate immunity-activating portion) with 59.6% identity, indicating that the observed protective capacity of homologous or heterologous Hsp70 proteins might reside within this peptide-binding domain.

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Comparing the acute response to cadmium toxicity of nauplii from different populations of Artemia

Sarabia

Ramo

Varó

et al. 2002

Enviro Toxic and Chemistry

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The lethal responses to cadmium of instar II nauplii from eight populations of Artemia belonging to the species Artemia franciscana, Artemia salina, Artemia persimilis, and Artemia parthenogenetica have been compared. Generalized linear models were used to fit mortality. The model indicates that there is a relationship between species, type of population, and mortality rate. The two populations of A. franciscana were the most sensitive to cadmium toxicity (median lethal concentration, LC50, of 93.3-142 mg/L), while the population of A. persimilis was the most resistant (LC50 of 284 mg/L). Differences in the phenotypic variability in each population were assessed through the slope of the mortality curve, with A. persimilis exhibiting the highest diversity. This study suggests that habitat peculiarities and historical origin of the populations may have a significant influence on their response to cadmium toxicity.

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Thermal resistance, developmental rate and heat shock proteins in Artemia franciscana, from San Francisco Bay and southern Vietnam

Cited by 70 publications

References 36 publications

Exposure of gnotobiotic Artemia franciscana larvae to abiotic stress promotes heat shock protein 70 synthesis and enhances resistance to pathogenic Vibrio campbellii

Exposure of gnotobiotic Artemia franciscana larvae to abiotic stress promotes heat shock protein 70 synthesis and enhances resistance to pathogenic Vibrio campbellii

Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii

Comparing the acute response to cadmium toxicity of nauplii from different populations of Artemia

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