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

Fish & Shellfish Immunology
Kartik BaruahPeter Bossier

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 prot...Continue Reading

Citations

Jun 23, 2015·Journal of Fish Diseases·L H PhuocP Bossier
Apr 24, 2014·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Parisa NorouzitallabPeter Bossier
Mar 3, 2020·Frontiers in Immunology·Eamy Nursaliza YaacobDaisy Vanrompay
Sep 29, 2020·Developmental and Comparative Immunology·Wisarut JunprungAnchalee Tassanakajon
Nov 13, 2019·International Journal of Biological Macromolecules·Ramachandran SrinivasanKodiveri Muthukaliannan Gothandam

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