{"refrec":{"BRefID":210907,"RR":"<b>Baruah, K.; Ranjan, J.; Sorgeloos, P.; Bossier, P.</b> (2010). Efficacy of heterologous and homologous heat shock protein 70s as protective agents to <i>Artemia franciscana</i> challenged with <i>Vibrio campbellii</i>. <i>Fish Shellfish Immunol. 29(5)</i>: 733-739. <a href=\"http://dx.doi.org/10.1016/j.fsi.2010.07.011\" target=\"_blank\">dx.doi.org/10.1016/j.fsi.2010.07.011</a>","BEntID":202829,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Fish Shellfish Immunol. 29(5)</i>: 733-739. <a href=\"https://dx.doi.org/10.1016/j.fsi.2010.07.011\" target=\"_blank\">https://dx.doi.org/10.1016/j.fsi.2010.07.011</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Baruah, K.; Ranjan, J.; Sorgeloos, P.; Bossier, P.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Baruah, K. <i>et al.</i>","Englishabstract":"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, <i>Artemia</i> Hsp70 and <i>Escherichia coli</i> Hsp70 equivalent DnaK (each overproduced in <i>E.coli</i>), for their ability to protect <i>Artemia</i> against <i>Vibrio</i> challenge. Results showed that <i>Artemia</i> fed with <i>E. coli</i> producing <i>Artemia</i> Hsp70 or DnaK proteins, as assessed by immune-probing in western blots, survived better in a <i>Vibrio</i> challenge assay. The observed effects could be due to enhancement of the <i>Artemia</i> 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.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Efficacy of heterologous and homologous heat shock protein 70s as protective agents to <i>Artemia franciscana</i> challenged with <i>Vibrio campbellii</i>","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":"Heat shock protein (Hsp) 70; DnaK; Phenoloxidase; Artemia franciscana;","OtherDescriptors":null,"Notes":null,"AnaPub":2010,"MonPub":null,"DateUpdate":"2012-05-30","DateCreate":"2011-12-22","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000282470400004","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.fsi.2010.07.011"},"refs":null,"anarec":{"AnaID":210907,"PubliDate":2010,"Pagination":"733-739","XtraPublOfAnaID":null,"ISBN":null,"Volume":"29","Issue":"5","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":45027,"SerRR":"Fish & Shellfish Immunology. 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