In vitro and in vivo Activity of the Dimer of PMAP-36 Expressed in Pichia pastoris

Publisher: Karger

E-ISSN: 1660-2412|24|4|234-240

ISSN: 1464-1801

Source: Journal of Molecular Microbiology and Biotechnology, Vol.24, Iss.4, 2014-08, pp. : 234-240

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Abstract

The antimicrobial peptide PMAP-36 exists as a homodimer stabilized by an intermolecular disulfide bridge. The dimer of PMAP-36 exhibits a potent and rapid microbicidal activity against a wide spectrum of microorganisms. The gene encoding the antiparallel dimer (PMAP-36)2 was designed and codon-optimized according to bias of Pichia pastoris. The gene was then expressed in the P. pastoris strain GS115. The concentration of the recombinant product reached 106 mg/l. In vitro activity assays indicated that the recombinant peptide showed antimicrobial activities against Gram-positive and Gram-negative bacteria but did not cause hemolysis of chicken erythrocytes. Subsequently, 120 7-day-old male Arbor Acres broilers were used to evaluate the in vivo activities of the peptide. A prophylactic dose of ciprofloxacin lactate was supplemented as the control. The results showed that recombinant (PMAP-36)2 significantly increased the serum IgM content of the birds (p < 0.05). The recombinant peptide significantly increased the amounts of Bifidobacterium and decreased the amount of Escherichia coli cells in the ceca of the experimental birds (p < 0.05). The results obtained in the present study indicate that the recombinant (PMAP-36)2 has a potent in vitro and in vivo activity and can be used as an alternative to antibiotic treatment.

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