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Antibacterial properties of Acinetobacter baumannii phage Abp1 endolysin (PlyAB1).

Huang G, Shen X, Gong Y, Dong Z, Zhao X, Shen W, Wang J, Hu F, Peng Y - BMC Infect. Dis. (2014)

Bottom Line: Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs.These isolates were shown to belong to different ST clones by multilocus sequence typing.The results presented here show that PlyAB1 has potential as an antibiotic against drug-resistant A. baumannii.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Trauma, Burns and Combined Injury, Institute of Burn Research, Southwest Hospital, Third Military Medical University, Chongqing, China. haitao3140@sina.com.

ABSTRACT

Background: Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs. Endolysins from phages are attracting increasing interest as potential antimicrobial agents, especially for drug-resistant bacteria. We previously isolated and characterized Abp1, a virulent phage targeting the multidrug-resistant A. baumannii strain, AB1.

Methods: To evaluate the antimicrobial potential of endolysin from the Abp1 phage, the endolysin gene plyAB1 was cloned and over-expressed in Escherichia coli, and the lytic activity of the recombinant protein (PlyAB1) was tested by turbidity assessment and bacteria counting assays.

Results: PlyAB1 exhibits a marked lytic activity against A. baumannii AB1, as shown by a decrease in the number of live bacteria following treatment with the enzyme. Moreover, PlyAB1 displayed a highly specific lytic effect against all of the 48 hospital-derived pandrug-resistant A. baumannii isolates that were tested. These isolates were shown to belong to different ST clones by multilocus sequence typing.

Conclusions: The results presented here show that PlyAB1 has potential as an antibiotic against drug-resistant A. baumannii.

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Related in: MedlinePlus

Cloning and over-expression of PlyAB1. (A) Cloning of plyAB1 into pET28a: 1) recombinant plasmid pET28a-plyAB1, 2) pET28a-plyAB1 digested with BamHI and Xhol, 3) PCR amplification of plyAB1. (B) The purified PlyAB1 protein after Ni+ affinity chromatography and filtration.
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Fig2: Cloning and over-expression of PlyAB1. (A) Cloning of plyAB1 into pET28a: 1) recombinant plasmid pET28a-plyAB1, 2) pET28a-plyAB1 digested with BamHI and Xhol, 3) PCR amplification of plyAB1. (B) The purified PlyAB1 protein after Ni+ affinity chromatography and filtration.

Mentions: The plyAB1 gene was successfully amplified from Abp1 genomic DNA using the P1/P2 primer pair, and was then cloned into the BamHI/Xhol sites of the pET28a expression vector. The recombinant plasmid generated (pET28a-plyAB1) was confirmed by enzyme digestion (FigureĀ 2A) and DNA sequencing.Figure 2


Antibacterial properties of Acinetobacter baumannii phage Abp1 endolysin (PlyAB1).

Huang G, Shen X, Gong Y, Dong Z, Zhao X, Shen W, Wang J, Hu F, Peng Y - BMC Infect. Dis. (2014)

Cloning and over-expression of PlyAB1. (A) Cloning of plyAB1 into pET28a: 1) recombinant plasmid pET28a-plyAB1, 2) pET28a-plyAB1 digested with BamHI and Xhol, 3) PCR amplification of plyAB1. (B) The purified PlyAB1 protein after Ni+ affinity chromatography and filtration.
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4274762&req=5

Fig2: Cloning and over-expression of PlyAB1. (A) Cloning of plyAB1 into pET28a: 1) recombinant plasmid pET28a-plyAB1, 2) pET28a-plyAB1 digested with BamHI and Xhol, 3) PCR amplification of plyAB1. (B) The purified PlyAB1 protein after Ni+ affinity chromatography and filtration.
Mentions: The plyAB1 gene was successfully amplified from Abp1 genomic DNA using the P1/P2 primer pair, and was then cloned into the BamHI/Xhol sites of the pET28a expression vector. The recombinant plasmid generated (pET28a-plyAB1) was confirmed by enzyme digestion (FigureĀ 2A) and DNA sequencing.Figure 2

Bottom Line: Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs.These isolates were shown to belong to different ST clones by multilocus sequence typing.The results presented here show that PlyAB1 has potential as an antibiotic against drug-resistant A. baumannii.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Trauma, Burns and Combined Injury, Institute of Burn Research, Southwest Hospital, Third Military Medical University, Chongqing, China. haitao3140@sina.com.

ABSTRACT

Background: Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs. Endolysins from phages are attracting increasing interest as potential antimicrobial agents, especially for drug-resistant bacteria. We previously isolated and characterized Abp1, a virulent phage targeting the multidrug-resistant A. baumannii strain, AB1.

Methods: To evaluate the antimicrobial potential of endolysin from the Abp1 phage, the endolysin gene plyAB1 was cloned and over-expressed in Escherichia coli, and the lytic activity of the recombinant protein (PlyAB1) was tested by turbidity assessment and bacteria counting assays.

Results: PlyAB1 exhibits a marked lytic activity against A. baumannii AB1, as shown by a decrease in the number of live bacteria following treatment with the enzyme. Moreover, PlyAB1 displayed a highly specific lytic effect against all of the 48 hospital-derived pandrug-resistant A. baumannii isolates that were tested. These isolates were shown to belong to different ST clones by multilocus sequence typing.

Conclusions: The results presented here show that PlyAB1 has potential as an antibiotic against drug-resistant A. baumannii.

Show MeSH
Related in: MedlinePlus