| one publication added to basket [210907] | Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii
Baruah, K.; Ranjan, J.; Sorgeloos, P.; Bossier, P. (2010). Efficacy of heterologous and homologous heat shock protein 70s as protective agents to Artemia franciscana challenged with Vibrio campbellii. Fish Shellfish Immunol. 29(5): 733-739. dx.doi.org/10.1016/j.fsi.2010.07.011 In: Fish & Shellfish Immunology. Academic Press: London; New York. ISSN 1050-4648; e-ISSN 1095-9947, more |  |
| Keyword | Artemia franciscana Kellog, 1906 [WoRMS]
| | Author keywords | Heat shock protein (Hsp) 70; DnaK; Phenoloxidase; Artemia franciscana; |
| Abstract | The 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 peptide-binding 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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