A plant-based heat shock protein inducing compound modulates host–pathogen interactions between Artemia franciscana and Vibrio campbellii

Aquaculture ◽  
2014 ◽  
Vol 430 ◽  
pp. 120-127 ◽  
Author(s):  
Yufeng Niu ◽  
Parisa Norouzitallab ◽  
Kartik Baruah ◽  
Shuanglin Dong ◽  
Peter Bossier
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Artemia Franciscana ◽  
Host Pathogen Interactions ◽  
Host Pathogen ◽  
Vibrio Campbellii

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

Heat-shock proteins in host-pathogen interactions: implications for cystic fibrosis

1995 ◽  
Vol 3 (10) ◽  
pp. 392-396 ◽  
Author(s):  
Barbara S Polla ◽  
Ewa Mariéthoz ◽  
Dominique Hubert ◽  
Constance Barazzone
Keyword(s):  
Cystic Fibrosis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Host Pathogen Interactions ◽  
Host Pathogen ◽  
Shock Proteins

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
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