Isolation and Functional Characterization of a New Shrimp Ovarian Peritrophin with Antimicrobial Activity from <Emphasis Type="Italic">Fenneropenaeus merguiensis</Emphasis> |
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Authors: | Wiriya Loongyai Jean-Christophe Avarre Martine Cerutti Esther Lubzens Wilaiwan Chotigeat |
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Institution: | (1) Center for Genomics and Bioinformatics Research, Faculty of Science, Prince of Songkla University, Hatyai, Songkla, 90112, Thailand;(2) Laboratoire des Symbioses Tropicales et Méditerranéenes Campus International de Baillarguet, 34398 Montpellier, Cedex 5, France;(3) CNRS Station de Pathologie Comparée Baculovirus et Therapie, 30380 Saint Christol Les Ales, France;(4) Israel Oceanographic and Limnological Research, Tel-Shikmona, P.O. Box 8030, Haifa, 31080, Israel |
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Abstract: | Shrimp ovarian peritrophin (SOP), a major protein in jelly layer (JL) and cortical rods (CRs), is proposed to play a role
in the protection of spawned eggs. The full sequence of SOP cDNA from Fenneropenaeus merguiensis (Fm-SOP) shares approximately 50% identity with other SOP sequences and contains several putative chitin-binding or peritrophin-A
domains. Interestingly, Fm-SOP contains a putative 61-amino acid propeptide located at the N-terminal end, downstream of a
19-amino acid signal peptide, which is unique among penaeid SOP sequences described so far. This 61-amino-acid sequence constitutes
a putative chitin-binding domain with six conserved cysteines, and is cleaved at a dibasic recognition site for a furin (subtilisin-like
endoprotease). Expression analyses indicated that Fm-SOP mRNA is abundant in early vitellogenic ovaries and scarce in late-vitellogenic ovaries. Conversely, Fm-SOP protein is the
most abundant at the end of vitellogenesis. To investigate its biological function, a recombinant Fm-SOP was expressed to
generate a glycosylated protein in Spodoptera frugiperda Sf9 cells (rSOP-Sf9) and a nonglycosylated protein (rSOP-Ec) in Escherichia coli. rSOP-Sf9 and rSOP-Ec were found to bind to chitin, similarly to the native protein extracted from F. merguiensis ovaries. Most interestingly, rSOP-Ec displayed a chitinase activity and efficiently inhibited the growth of Vibrio harveyi and Staphylococcus aureus, with minimum inhibitory concentrations of 2.4 and 15.7 μM, respectively. This first report shows that a major component
of CR and JL is biologically active against known pathogens and predicts a significant role of JL in the protection of the
spawned eggs against pathogens.
The nucleotide sequence reported in this article has been submitted to the GeneBank™/EBI accession number AY775291 for Fm-SOP. |
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Keywords: | antimicrobial Fenneropenaeus merguiensis ovary peritrophin |
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