{"refrec":{"BRefID":238402,"RR":"<b>Baruah, K.; Norouzitallab, P.; Li, S.H.; Sorgeloos, P.; Bossier, P.</b> (2013). Feeding truncated heat shock protein 70s protect <i>Artemia franciscana</i> against virulent <i>Vibrio campbellii</i> challenge. <i>Fish Shellfish Immunol. 34(1)</i>: 183-191. <a href=\"http://dx.doi.org/10.1016/j.fsi.2012.10.025\" target=\"_blank\">dx.doi.org/10.1016/j.fsi.2012.10.025</a>","BEntID":230089,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Fish Shellfish Immunol. 34(1)</i>: 183-191. <a href=\"https://dx.doi.org/10.1016/j.fsi.2012.10.025\" target=\"_blank\">https://dx.doi.org/10.1016/j.fsi.2012.10.025</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Baruah, K.; Norouzitallab, P.; Li, S.H.; Sorgeloos, P.; Bossier, P.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Baruah, K. <i>et al.</i>","Englishabstract":"The 70 kDa heat shock proteins (Hsp70s) are highly conserved in evolution, leading to striking similarities in structure and composition between eukaryotic Hsp70s and their homologs in prokaryotes. The eukaryotic Hsp70 like the DnaK (<i>Escherichia coli</i> equivalent Hsp70) protein, consist of three functionally distinct domains: an N-terminal 44-kDa ATPase portion, an 18-kDa peptide-binding domain and a C-terminal 10-kDa fragment. Previously, the amino acid sequence of eukaryotic (the brine shrimp <i>Artemia franciscana</i>) Hsp70 and DnaK proteins were shown to share a high degree of homology, particularly in the peptide-binding domain (59.6%, the putative innate immunity-activating portion) compared to the N-terminal ATPase (48.8%) and the C-terminal lid domains (19.4%). Next to this remarkable conservation, these proteins have been shown to generate protective immunity in <i>Artemia</i> against pathogenic <i>Vibrio campbellii</i>. This study, aimed to unravel the <i>Vibrio</i>-protective domain of Hsp70s <i>in vivo</i>, demonstrated that gnotobiotically cultured <i>Artemia</i> fed with recombinant C-terminal fragment (containing the conserved peptide binding domain) of <i>Artemia</i> Hsp70 or DnaK protein were well protected against subsequent <i>Vibrio</i> challenge. In addition, the prophenoloxidase (proPO) system, at both mRNA and protein activity levels, was also markedly induced by these truncated proteins, suggesting epitope(s) responsible for priming the proPO system and presumably other immune-related genes, consequently boosting <i>Artemia</i> survival upon challenge with <i>V. campbellii</i>, might be located within this conserved region of the peptide binding domain.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Feeding truncated heat shock protein 70s protect <i>Artemia franciscana</i> against virulent <i>Vibrio campbellii</i> challenge","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Truncated heat shock protein 70; Phenoloxidase; Priming; Artemiafranciscana; Vibrio campbellii","OtherDescriptors":null,"Notes":null,"AnaPub":2013,"MonPub":null,"DateUpdate":"2015-10-29","DateCreate":"2014-05-18","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000314743600022","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.fsi.2012.10.025"},"refs":null,"anarec":{"AnaID":238402,"PubliDate":2013,"Pagination":"183-191","XtraPublOfAnaID":null,"ISBN":null,"Volume":"34","Issue":"1","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":45027,"SerRR":"Fish & Shellfish Immunology. 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