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.2013 Sep;79(18):5593-600.
doi: 10.1128/AEM.01648-13. Epub 2013 Jul 8.

Characterization of maltocin P28, a novel phage tail-like bacteriocin from Stenotrophomonas maltophilia

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Characterization of maltocin P28, a novel phage tail-like bacteriocin from Stenotrophomonas maltophilia

Jian Liu et al. Appl Environ Microbiol.2013 Sep.

Abstract

Stenotrophomonas maltophilia is an important global opportunistic pathogen for which limited therapeutics are available because of the emergence of multidrug-resistant strains. A novel bacteriocin, maltocin P28, which is produced by S. maltophilia strain P28, may be the first identified phage tail-like bacteriocin from S. maltophilia. Maltocin P28 resembles a contractile but nonflexible phage tail structure based on electron microscopy, and it is sensitive to trypsin, proteinase K, and heat. SDS-PAGE analysis of maltocin P28 revealed two major protein bands of approximately 43 and 20 kDa. The N-terminal amino acid residues of these two major subunits were sequenced, and the maltocin P28 gene cluster was located on the S. maltophilia P28 chromosome. Our sequence analysis results indicate that this maltocin gene cluster consists of 23 open reading frames (ORFs), and that its gene organization is similar to that of the P2 phage genome and R2 pyocin gene cluster. ORF17 and ORF18 encode the two major structural proteins, which correspond to gpFI (tail sheath) and gpFII (tail tube) of P2 phage, respectively. We found that maltocin P28 had bactericidal activity against 38 of 81 tested S. maltophilia strains. Therefore, maltocin P28 is a promising therapeutic substitute for antibiotics for S. maltophilia infections.

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Figures

Fig 1
Fig 1
Electron micrographs of the partially purified sample (A), the major DEAE-eluted fraction at 0.3 M NaCl (B), and the minor DEAE-eluted fraction at 0.7 M NaCl (C). The maltocin P28 particles with different structural elements, namely, empty sheath, complete form, and complete contracted form, are marked ES, CF, and CCF, respectively. The filamentous phage is marked FP.
Fig 2
Fig 2
DEAE chromatography of the partially purified maltocin P28. The partial preparation was chromatographed on a DEAE-cellulose (DEAE) column (10 by 175 mm) with a nonlinear gradient of NaCl (0, 0.3, 0.4, and 0.7 M) (thick line) in 0.01 M phosphate buffer (pH 6.8). The elution profile of the maltocin preparation was measured at an absorbance of 280 nm (thin line).
Fig 3
Fig 3
Killing of S. maltophilia c6 after addition of maltocin P28 at final concentrations of 2.6 × 104 (○), 2.6 × 103 (Δ), 2.6 × 102 (▽), and 0 (□) AU ml−1. CFU were determined in triplicate, and the mean value at each time point was used to make the curve. The experiment was repeated twice with similar results.
Fig 4
Fig 4
SDS-PAGE of the DEAE-purified maltocin P28 particles.
Fig 5
Fig 5
Comparison of genetic organization among the gene locus for the maltocin P28, pyocin R2, and P2 phage. Genes (indicated as large arrows) are not drawn to scale for simplicity. Homologous genes are connected by lines. Open reading frames encoding phage proteins involved in the tail phage synthesis are indicated by gray arrows. Open reading frames encoding phage regulators and lytic proteins are indicated by diagonal and gridding arrows separately. Open reading frames encoding proteins with unknown functions are indicated in white.
Fig 6
Fig 6
SDS-PAGE (A) and bactericidal activity (B) of partially purified maltocin sample from S. maltophilia P28 (lane 2), S. maltophilia P28 Δorf17 (lane 3), S. maltophilia P28 Δorf17/pBBR1MCSPlac-orf17 (lane 4), and S. maltophilia P28 Δorf17/pBBR1MCS (lane 5). The partially purified maltocin sample from MMC-induced S. maltophilia P28 (lane 1) is used as a maker. The tail sheath and tail tube proteins are indicated with arrows.
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References

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