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Molecular cloning, genomic organization and antibacterial activity of a second isoform of antilipopolysaccharide factor (ALF) from the mud crab, Scylla paramamosain
Genetic makeup and bacteria-fighting ability of a second form of an antibacterial protein from mud crab
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Abstract
The ALFSp2 protein, a novel antimicrobial peptide from the mud crab, has a molecular mass of 10.79 kDa.
- ALFSp2 consists of 94 amino acids and is derived from a 348 bp cDNA sequence.
- The amino acid sequence of ALFSp2 shows a similarity of 74% to Eriocheir sinensis ALF.
- In healthy mud crabs, ALFSp2 is most abundant in hemocytes and gill tissues.
- The gene for ALFSp2 is organized into three exons and two introns, with multiple potential transcription factor binding sites upstream.
- The synthesized 24 amino acid LPS-binding domain of ALFSp2 exhibits antimicrobial activity against both Gram-positive and Gram-negative bacteria.
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