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Human neutrophil peptide 3 could be functionally expressed in Rhodobacter sphaeroides

100%

Nie X., Zhang L., Hu Z., Liu Y., Zhao Z.

2015

vol. 62

issue 2

259-263

Human neutrophil peptides (HNPs) possess high antimicrobial activities against a broad spectrum of microorganisms. Rhodobacter sphaeroides is the best-characterized photosynthetic bacterium and exhibits potential as a novel expression system. Up to date, no literature has been reported regarding expression of HNP3 in Rb. sphaeroides. In the present study, the HNP3 gene fragment was amplified by SOE PCR and ligated into photosynthetic bacteria light-harvesting complex 2 (LH2) expression vector leading to HNP3 fusion protein expression vector. The HNP3 fusion protein was successfully expressed as rapidly evaluated by the LH2 characteristic peaks at ~800 nm and ~850 nm before purification and SDS/PAGE. Subsequently, the HNP3 fusion protein was purified by one-step affinity chromatography, and could be rapidly detected by the color and the spectral absorption at ~800 nm and ~850 nm before SDS/PAGE. Antimicrobial activity assay suggested that the HNP3 fusion protein exhibited high antimicrobial activity towards E. coli. The present study may supply an insight into employing the novel Rb. sphaeroides expression system, exhibiting dramatic advantages over currently used commercial expression system, to heterologously express human neutrophil peptides.

High-grade mutant OmpF induces decreased bacterial survival rate

86%

Zhao Z.-p., Liu T.-t., Zhang L., Luo M., Nie X., Li Z.-x., Pan Y.

2014

vol. 61

issue 2

369-373

OmpF plays very important roles in the influx of antibiotics and bacterial survival in the presence of antibiotics. However, high-grade mutant OmpF and its function in decreasing bacterial survival rate have not been reported to date. In the present study, we cloned a high-grade mutant OmpF (mOmpF) and sequence analysis suggested that over 45 percent of the DNA sequence was significantly mutated, leading to dramatic changes in over 55 percent of the amino acid sequence. mOmpF protein was successfully expressed. When grown in the presence of antibiotic, the bacterial survival rate decreased and the antibiotic inhibition zone became larger with the increase of the mOmpF. It was concluded that concentration of high-grade mutant mOmpF dramatically influenced the bacterial survival rate. The study presented here may provide insights into better understanding of the relationships between structure and function of OmpF.

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2 Acta Biochimica Polonica

1 2015

1 2014

2 Nie X.

2 Zhang L.

1 Hu Z.

1 Li Z.-x.

1 Liu T.-t.

1 Liu Y.

1 Luo M.

1 Pan Y.

1 Zhao Z.

1 Zhao Z.-p.

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Human neutrophil peptide 3 could be functionally expressed in Rhodobacter sphaeroides

High-grade mutant OmpF induces decreased bacterial survival rate