Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge

2013 ◽  
Vol 34 (1) ◽  
pp. 183-191 ◽  
Author(s):  
Kartik Baruah ◽  
Parisa Norouzitallab ◽  
Li Shihao ◽  
Patrick Sorgeloos ◽  
Peter Bossier
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Artemia Franciscana ◽  
Vibrio Campbellii

Priming the prophenoloxidase system of Artemia franciscana by heat shock proteins protects against Vibrio campbellii challenge

2011 ◽  
Vol 31 (1) ◽  
pp. 134-141 ◽  
Author(s):  
Kartik Baruah ◽  
Jayant Ranjan ◽  
Patrick Sorgeloos ◽  
Thomas H. MacRae ◽  
Peter Bossier
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Artemia Franciscana ◽  
Prophenoloxidase System ◽  
Shock Proteins ◽  
Vibrio Campbellii

scholarly journals Knockdown of the small heat-shock protein p26 by RNA interference modifies the diapause proteome of Artemia franciscana

2019 ◽  
Vol 97 (4) ◽  
pp. 471-479
Author(s):  
Hajer Salem Malitan ◽  
Alejandro M. Cohen ◽  
Thomas H. MacRae
Keyword(s):  
Rna Interference ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Tolerance ◽  
Small Heat Shock Protein ◽  
Isotopic Labeling ◽  
Artemia Franciscana ◽  
Signal Transducers ◽  
Translation Factors

Embryos of the crustacean Artemia franciscana may arrest as gastrulae, forming cysts that enter diapause, which is a state of reduced metabolism and enhanced stress tolerance. Diapausing cysts survive physiological stresses for years due, in part, to molecular chaperones. p26, a small heat-shock protein, is an abundant diapause-specific molecular chaperone in cysts, and it affects embryo development and stress tolerance. p26 is therefore thought to influence many proteins in cysts, and this study was undertaken to determine how the loss of p26 by RNA interference (RNAi) affects the diapause proteome of A. franciscana. The proteome was analyzed by shot-gun proteomics coupled to differential isotopic labeling and tandem mass spectrometry. Proteins in the diapause proteome included metabolic enzymes, antioxidants, binding proteins, structural proteins, transporters, translation factors, receptors, and signal transducers. Proteins within the diapause proteome either disappeared or were reduced in amount when p26 was knocked down, or conversely, proteins appeared or increased in amount. Those proteins that disappeared may be p26 substrates, whereas the synthesis of those proteins that appeared or increased may be regulated by p26. This study provides the first global characterization of the diapause proteome of A. franciscana and demonstrates that the sHsp p26 influences proteome composition.

Knockdown of heat shock protein 70 (Hsp70) by RNAi reduces the tolerance of Artemia franciscana nauplii to heat and bacterial infection

2017 ◽  
Vol 487 ◽  
pp. 106-112 ◽  
Author(s):  
Mat Taib Mimi Iryani ◽  
Thomas H. MacRae ◽  
Sheethal Panchakshari ◽  
Jiabo Tan ◽  
Peter Bossier ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Bacterial Infection ◽  
Heat Shock Protein 70 ◽  
Artemia Franciscana

ArHsp21, a developmentally regulated small heat-shock protein synthesized in diapausing embryos of Artemia franciscana

2008 ◽  
Vol 411 (3) ◽  
pp. 605-611 ◽  
Author(s):  
Zhijun Qiu ◽  
Thomas H. MacRae
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Citrate Synthase ◽  
Sequence Similarity ◽  
Single Gene ◽  
Small Heat Shock Protein ◽  
Subtractive Hybridization ◽  
Artemia Franciscana ◽  
Induced Aggregation

Embryos of the crustacean, Artemia franciscana, undergo alternative developmental pathways, producing either larvae or encysted embryos (cysts). The cysts enter diapause, characterized by exceptionally high resistance to environmental stress, a condition thought to involve the sHSP (small heat-shock protein), p26. Subtractive hybridization has revealed another sHSP, termed ArHsp21, in diapause-destined Artemia embryos. ArHsp21 shares sequence similarity with p26 and sHSPs from other organisms, especially in the α-crystallin domain. ArHsp21 is the product of a single gene and its synthesis occurred exclusively in diapause-destined embryos. Specifically, ArHsp21 mRNA appeared 2 days post-fertilization, followed 1 day later by the protein, and then increased until embryo release at day 5. No ArHsp21 protein was detected in embryos developing directly into larvae, although there was a small amount of mRNA at 3 days post-fertilization. The protein was degraded during post-diapause development and had disappeared completely from second instar larvae. ArHsp21 formed large oligomers in encysted embryos and transformed bacteria. When purified from bacteria, ArHsp21 functioned as a molecular chaperone in vitro, preventing heat-induced aggregation of citrate synthase and reduction-driven denaturation of insulin. Sequence characteristics, synthesis patterns and functional properties demonstrate clearly that ArHsp21 is an sHSP able to chaperone other proteins and contribute to stress tolerance during diapause. As such, ArHsp21 would augment p26 chaperone activity and it may also possess novel activities that benefit Artemia embryos exposed to stress.

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