کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2432273 1106788 2013 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک علوم آبزیان
پیش نمایش صفحه اول مقاله
Feeding truncated heat shock protein 70s protect Artemia franciscana against virulent Vibrio campbellii challenge
چکیده انگلیسی

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 (Escherichia coli 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 Artemia franciscana) 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 Artemia against pathogenic Vibrio campbellii. This study, aimed to unravel the Vibrio-protective domain of Hsp70s in vivo, demonstrated that gnotobiotically cultured Artemia fed with recombinant C-terminal fragment (containing the conserved peptide binding domain) of Artemia Hsp70 or DnaK protein were well protected against subsequent Vibrio 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 Artemia survival upon challenge with V. campbellii, might be located within this conserved region of the peptide binding domain.


► The prokaryotic (DnaK) and eukaryotic (Artemia) Hsp70s are highly conserved.
► These Hsp70s consist of 3 distinct domains: ATPase, peptide-binding (PBD) and lid.
► The amino acid sequence of these proteins is highly homologous, mainly in the PBD.
► We showed that truncated Hsp70s containing the PBD protected Artemia against Vibrio.
► The protective epitope within Hsp70s might be located within this conserved PBD.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Fish & Shellfish Immunology - Volume 34, Issue 1, January 2013, Pages 183–191
نویسندگان
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