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

Applied and environmental microbiology (2013-07-10)
Jian Liu, Peng Chen, Congyi Zheng, Yu-Ping Huang
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.

MATERIALS
Product Number
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Product Description

Sigma-Aldrich
Proteinase K from Tritirachium album, lyophilized powder, BioUltra, ≥30 units/mg protein, for molecular biology
Sigma-Aldrich
Proteinase K from Tritirachium album, ≥500 units/mL, buffered aqueous glycerol solution
Sigma-Aldrich
Proteinase K from Tritirachium album, ≥3.0 unit/mg solid, lyophilized powder
Sigma-Aldrich
Proteinase K from Tritirachium album, buffered aqueous glycerol solution, for molecular biology, ≥800 units/mL
Sigma-Aldrich
Proteinase K from Tritirachium album, lyophilized powder, ≥30 units/mg protein
Sigma-Aldrich
Proteinase K from Tritirachium album, Reagents designed and manufactured under current ISO 13485 certification.