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. 2014 Nov 20:2:e679.
doi: 10.7717/peerj.679. eCollection 2014.

Bacillus anthracis pXO1 plasmid encodes a putative membrane-bound bacteriocin

Agata Perlińska  1 , Marcin Grynberg  2
Affiliations

Bacillus anthracis pXO1 plasmid encodes a putative membrane-bound bacteriocin

Agata Perlińska et al. PeerJ. .

Abstract

Evolutionary advantages over cousin cells in bacterial pathogens may decide about the success of a specific cell in its environment. Bacteria use a plethora of methods to defend against other cells and many devices to attack their opponents when competing for resources. Bacteriocins are antibacterial proteins that are used to eliminate competition. We report the discovery of a putative membrane-bound bacteriocin encoded by the Bacillus anthracis pathogenic pXO1 plasmid. We analyze the genomic structure of the bacteriocin operon. The proposed mechanisms of action predestine this operon as a potent competitive advantage over cohabitants of the same niche.

Keywords: BXA0140; Bacillus anthracis; Bacteriocin; Cell adherence; Cell attachment; Hemolysin II; pXO1.

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Figures

Figure 1
Figure 1. Multiple sequence alignments of (A) BXA0138, (B) BXA0139 and (C) BXA0140 with the identified similar sequences (for details see “Results” section).
(A) Adhesin repeats belong to the Actinobacillus pleuropneumoniae autotransporter adhesin [GI: 501454838]. (B) Bacillus cereus and Bacillus anthracis hemolysin II domains derive from GI: 446632026 and GI: 673614593, respectively. The star shows the nonsense mutation (TGG to TGA), instead of tryptophan 372 in B. cereus. The remaining part of the protein is reproduced using BLASTX analysis of the C-terminal part of the B. anthracis DNA sequence. (C) Comparison of BXA0140 to thuricin CD, bacteriocin AS-48 and carnocyclin A. PDB IDs are given in parentheses. Multiple sequence alignment also shows similarity of the leader sequence to the leader of Bacillus subtilis subtilosin A. Coloring of alignments is a default of the Clustal Omega program.
Figure 2
Figure 2. Structural model of BXA0140.
(A) Representation of the protein colored from N-terminus (blue) to C-terminus (red) using a rainbow color gradient; hydrogen bonds are represented as black dashed lines. (B) Van der Waals surface of the protein with hydrophobic residues colored with blue and charged residues colored with green. (C) Superposition of BXA0140 (yellow) and bacteriocin AS-48 (green; PDB ID: 1E68). N- and C-terminal ends of AS-48 are represented as sticks and colored red and blue, respectively.
Figure 3
Figure 3. Putative functions of proteins encoded by the BXA0138-BXA0140 operon.
This model predicts a combination of functions that are related to competition between bacterial strains.
See this image and copyright information in PMC

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