A novel expression vector for the secretion of abaecin in Bacillus subtilis
Braz. j. microbiol
;
48(4): 809-814, Oct.-Dec. 2017. graf
Article
in English
| LILACS
| ID: biblio-889176
ABSTRACT
ABSTRACT This study aimed to describe a Bacillus subtilis expression system based on genetically modified B. subtilis. Abaecin, an antimicrobial peptide obtained from Apis mellifera, can enhance the effect of pore-forming peptides from other species on the inhibition of bacterial growth. For the exogenous expression, the abaecin gene was fused with a tobacco etch virus protease cleavage site, a promoter Pglv, and a mature beta-glucanase signal peptide. Also, a B. subtilis expression system was constructed. The recombinant abaecin gene was expressed and purified as a recombinant protein in the culture supernatant. The purified abaecin did not inhibit the growth of Escherichia coli strain K88. Cecropin A and hymenoptaecin exhibited potent bactericidal activities at concentrations of 1 and 1.5 µM. Combinatorial assays revealed that cecropin A and hymenoptaecin had sublethal concentrations of 0.3 and 0.5 µM. This potentiating functional interaction represents a promising therapeutic strategy. It provides an opportunity to address the rising threat of multidrug-resistant pathogens that are recalcitrant to conventional antibiotics.
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Bacillus subtilis
/
Insect Proteins
/
Antimicrobial Cationic Peptides
/
Genetic Vectors
Language:
English
Journal:
Braz. j. microbiol
Journal subject:
Microbiology
Year:
2017
Type:
Article
Affiliation country:
China
Institution/Affiliation country:
College of Basic Medicine/CN
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