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Broad Spectrum Anti-Bacterial Activity of a Recombinant Phosphatase-Like Protein (rPLP), Isolated from the Shrimp Penaeus monodon
|Title:||Broad Spectrum Anti-Bacterial Activity of a Recombinant Phosphatase-Like Protein (rPLP), Isolated from the Shrimp Penaeus monodon|
cloning and expression
|LC Subject Headings:||Fish culture--Israel.|
|Abstract:||Antimicrobial peptides play a significant role in the innate immune response of crustaceans. The gene coding for a phosphatase-like protein (PLP) from the black tiger shrimp, Penaeus monodon was cloned using pQE-30-UA expression vector and expressed in Escherichia coli M15 host cells. The recombinant protein purified by nickel-nitrilotriacetic acid affinity chromatography, gave a single distinct band of approximately 25 kDa by 15% sodium dodecyl sulfate polyacrylamide gel electrophoresis. The anti-bacterial activity of the recombinant phosphatase-like protein (rPLP) was characterized in vitro. Solid phase agar based assay revealed its inhibitory effect against several gram positive and gram negative bacteria. The minimal inhibitory concentration of the rPLP against Vibrio harveyi, by micro dilution method, was 1 μg/ml. This protein offers promise for use in hatcheries to control luminous vibriosis.|
|Appears in Collections:||Volume 67, 2015|
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