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Studies on Cloning, Sequence Analysis of Piscidin-like Gene from Two Species of Marine Fish and Phylogenetic Relationship of Piscidins Family

Author: ChenYong
Tutor: SuYongQuan
School: Xiamen University
Course: Marine biology
Keywords: Piscidin Antimicrobial peptides Red grouper Large yellow croaker
CLC: Q78
Type: Master's thesis
Year: 2008
Downloads: 180
Quote: 1
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Abstract


Antimicrobial peptides (antimicrobial peptides, AMPs) are a class of the natural small peptides with broad-spectrum anti-microbial activity is important in the innate immune system of non-specific immune factors. The term of Piscidin originally derived from hybridization markings perch (Silphaduang etc. the hybrid stripedbass, a peptide antibiotic isolated Morone.chrysops × M.saxatils) mast cells, subsequent research found that from of antimicrobial peptides pleurocidin of the flatfish the the hybrid the markings bass of moronecidin, European seabass (Dicentrarchus labrax) dicentracin coioides (Epinepheluscoioides) epinecidin-1, etc., have very similar amino acid sequence and piscidin its polypeptide structure and function for the α-helix , positively charged, amphoteric, affinity and polypeptides, can be collectively referred to as piscidin. Of this thesis to the important waters economic farmed fish - red spotted grouper (Epinephelus akaara) and large yellow croaker (Pseudosciaena crocea) for the cloned the two fish piscidin class antimicrobial peptide genes and analysis of its amino acid sequence composition and secondary structure characteristics, the multiple sequence alignment with piscidin other family members, and to establish the phylogenetic tree, the research results are as follows: 1, by RT-PCR, 3'RACE, 5'RACE and sequencing, molecular biology techniques antimicrobial peptide sequence amplified piscidin-like, from the red grouper head kidney and spleen, and sequence analysis and protein property prediction, the results show the deficit point the grouper piscidin for positively charged amphiphilic α-helix. structure, the end of the mature peptide carbon having the strong cation tetrapeptides RRRH structure, consistent with the end of the coioides mature peptide carbon, this structure is conducive to improve the binding ability of the bacterial membrane, with the other antimicrobial peptides piscidins family sequence similarity 59% -79% 45% -75%, consistency, its amino acid sequence and secondary structure in line with the characteristics of the family piscidin antimicrobial peptides, indicating that the red spotted grouper head kidney and spleen tissue cloning piscidin-like antimicrobial peptide the gene is piscidin gene variants, new members belonging to piscidins family. 2 by RT-PCR, 3'RACE, 5'RACE and sequencing and other molecular biology techniques, from the head kidney and spleen of large yellow croaker amplified piscidin-like antimicrobial peptide sequence, and the sequence analysis and protein property prediction results large yellow croaker piscidin the mature peptide is positively charged amphiphilic α-helix structure, end of the mature peptide carbon the grouper class RRRH structure positive charge than the red spotted grouper piscidin advantage domains carbon end other antimicrobial peptides of the the perch XQQ module, piscidins family sequence similarity of 50-77%, consistency of 41-70% of its amino acid sequence and secondary structure conforms to the characteristics of the family of piscidin antimicrobial peptides, indicating that the clones obtained from the large yellow croaker piscidin -like antimicrobial peptides the gene is piscidin gene variants and new members belonging to piscidins family. 3 the CLUSTALW software piscidin family of antimicrobial peptides for multiple sequence alignment, verify that a high degree of unity has a high degree of sequence homology, indicating that the structure and function of organisms. MEGA 4.0 software to draw the phylogenetic tree of the antimicrobial peptide family and other fish of the Piscidin antimicrobial peptide family, antimicrobial peptide gene validation of genes belonging to clone from red grouper and large yellow croaker fish piscidin, and the piscidin family of antimicrobial peptides genetic self-contained clusters differentiated from each other, and fish hepcidin antimicrobial peptide family.

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