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Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis

Paper ID Volume ID Publish Year Pages File Format Full-Text
25510 43578 2007 10 PDF Available
Title
Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis
Abstract

Antimicrobial peptides or proteins (AMPs) are proved to be one of the most important humoral factors to resist pathogen infection. As an antimicrobial protein, crustin had been described in invertebrates as a component of the innate immune system. A crustin-like gene (CruFc) was cloned from haemocytes of Chinese shrimp Fenneropenaeus chinensis by 3′ and 5′-RACE PCR. The full-length cDNA consists of 523 with 405 bp open reading frame encoding 134 amino acids and the deduced peptide contains a putative signal peptide of 17 amino acids. The sequence also contains a whey-acidic protein (WAP) domain at the C-terminal. Transcripts of CruFc were mainly detected in haemocytes and gill by RT-PCR analysis. In addition, another full-length cDNA named CshFc was also cloned from haemocytes of Chinese shrimp and its inferred amino acid sequence lacks the WAP-type ‘four-disulfide core’ domain. The fusion proteins containing CruFc and CshFc were, respectively, produced and the antimicrobial assays revealed that the recombinant CruFc could inhibit the growth of gram-positive bacteria in vitro but the recombinant CshFc could not inhibit at the same conditions. The difference of antimicrobial activity between recombinant CruFc and CshFc provides the evidence that the four-disulfide core domain of crustin may play an important role in its biological function.

Keywords
Fenneropenaeus chinensis; Crustin-like gene; Prokaryotic expression; Function identification
First Page Preview
Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 127, Issue 4, 20 January 2007, Pages 605–614
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering