scholarly journals Distinct colicin M-like bacteriocin-immunity pairs in Burkholderia

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Maarten G. K. Ghequire ◽  
René De Mot
Keyword(s):  
Colicin M

scholarly journals X-Ray Structure and Site-Directed Mutagenesis Analysis of the Escherichia coli Colicin M Immunity Protein

2010 ◽  
Vol 193 (1) ◽  
pp. 205-214 ◽  
Author(s):  
F. Gerard ◽  
M. A. Brooks ◽  
H. Barreteau ◽  
T. Touze ◽  
M. Graille ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Immunity Protein ◽  
X Ray ◽  
Colicin M

scholarly journals The ColM Family, Polymorphic Toxins Breaching the Bacterial Cell Wall

mBio ◽  
2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Maarten G. K. Ghequire ◽  
Susan K. Buchanan ◽  
René De Mot
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Cytoplasmic Membrane ◽  
Catalytic Domain ◽  
Gram Negative Bacteria ◽  
Antibacterial Peptides ◽  
Gram Negative ◽  
Lipid Ii ◽  
Associated Proteins ◽  
Colicin M

ABSTRACT Bacteria host an arsenal of antagonism-mediating molecules to combat for ecologic space. Bacteriocins represent a pivotal group of secreted antibacterial peptides and proteins assisting in this fight, mainly eliminating relatives. Colicin M, a model for peptidoglycan-interfering bacteriocins in Gram-negative bacteria, appears to be part of a set of polymorphic toxins equipped with such a catalytic domain (ColM) targeting lipid II. Diversifying recombination has enabled parasitism of different receptors and has also given rise to hybrid bacteriocins in which ColM is associated with another toxin module. Remarkably, ColM toxins have recruited a diverse array of immunity partners, comprising cytoplasmic membrane-associated proteins with different topologies. Together, these findings suggest that different immunity mechanisms have evolved for ColM, in contrast to bacteriocins with nuclease activities.

scholarly journals Sequence, expression, and localization of the immunity protein for colicin M.

1987 ◽  
Vol 169 (10) ◽  
pp. 4765-4769 ◽  
Author(s):  
T Olschläger ◽  
V Braun
Keyword(s):  
Immunity Protein ◽  
Colicin M

scholarly journals Broad and efficient control of major foodborne pathogenic strains ofEscherichia coliby mixtures of plant-produced colicins

2015 ◽  
Vol 112 (40) ◽  
pp. E5454-E5460 ◽  
Author(s):  
Steve Schulz ◽  
Anett Stephan ◽  
Simone Hahn ◽  
Luisa Bortesi ◽  
Franziska Jarczowski ◽  
...  
Keyword(s):  
United States ◽  
Pathogenic Bacteria ◽  
Thermal Inactivation ◽  
Bacterial Load ◽  
The United States ◽  
Broth Culture ◽  
Animal Products ◽  
E Coli ◽  
Colicin M ◽  
Very High

EnterohemorrhagicEscherichia coli(EHEC) is one of the leading causes of bacterial enteric infections worldwide, causing ∼100,000 illnesses, 3,000 hospitalizations, and 90 deaths annually in the United States alone. These illnesses have been linked to consumption of contaminated animal products and vegetables. Currently, other than thermal inactivation, there are no effective methods to eliminate pathogenic bacteria in food. Colicins are nonantibiotic antimicrobial proteins, produced byE. colistrains that kill or inhibit the growth of otherE. colistrains. Several colicins are highly effective against key EHEC strains. Here we demonstrate very high levels of colicin expression (up to 3 g/kg of fresh biomass) in tobacco and edible plants (spinach and leafy beets) at costs that will allow commercialization. Among the colicins examined, plant-expressed colicin M had the broadest antimicrobial activity against EHEC and complemented the potency of other colicins. A mixture of colicin M and colicin E7 showed very high activity against all major EHEC strains, as defined by the US Department of Agriculture/Food and Drug Administration. Treatments with low (less than 10 mg colicins per L) concentrations reduced the pathogenic bacterial load in broth culture by 2 to over 6 logs depending on the strain. In experiments using meats spiked withE. coliO157:H7, colicins efficiently reduced the population of the pathogen by at least 2 logs. Plant-produced colicins could be effectively used for the broad control of pathogenicE. coliin both plant- and animal-based food products and, in the United States, colicins could be approved using the generally recognized as safe (GRAS) regulatory approval pathway.

scholarly journals Characterization of Colicin M and its Orthologs Targeting Bacterial Cell Wall Peptidoglycan Biosynthesis

2012 ◽  
Vol 18 (3) ◽  
pp. 222-229 ◽  
Author(s):  
Hélène Barreteau ◽  
Meriem El Ghachi ◽  
Aurélie Barnéoud-Arnoulet ◽  
Emmanuelle Sacco ◽  
Thierry Touzé ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Bacterial Cell Wall ◽  
Peptidoglycan Biosynthesis ◽  
Cell Wall Peptidoglycan ◽  
Colicin M

scholarly journals Global transcriptional responses to the bacteriocin colicin M in Escherichia coli

2013 ◽  
Vol 13 (1) ◽  
pp. 42 ◽  
Author(s):  
Simona Kamenšek ◽  
Darja Žgur-Bertok
Keyword(s):  
Escherichia Coli ◽  
Transcriptional Responses ◽  
Colicin M

scholarly journals Characterization of the receptor protein for phage T5 and colicin M in the outer membrane ofE. coliB

FEBS Letters ◽  
1973 ◽  
Vol 34 (1) ◽  
pp. 77-80 ◽  
Author(s):  
V. Braun ◽  
H. Wolff
Keyword(s):  
Outer Membrane ◽  
Receptor Protein ◽  
Colicin M

Structure and uptake mechanism of bacteriocins targeting peptidoglycan renewal

2012 ◽  
Vol 40 (6) ◽  
pp. 1560-1565 ◽  
Author(s):  
Kornelius Zeth
Keyword(s):  
Outer Membrane ◽  
Periplasmic Space ◽  
Uptake Mechanism ◽  
Inner Membrane ◽  
Cytoplasmic Dna ◽  
Peptidoglycan Structure ◽  
Colicin M ◽  
Translocation Domain ◽  
Energy Dependent ◽  
Activity Domain

Bacteriocins are narrow-spectrum protein antibiotics released to kill related bacteria of the same niche. Uptake of bacteriocins depends critically on the presence of an uptake receptor in the outer membrane, a translocation pore and an energy-dependent activating system of the inner membrane. Most bacteriocins act on the inner membrane as pore-forming toxins or they target cytoplasmic DNA/RNA and ribosomal synthesis respectively. Only two bacteriocins are known to become activated in the periplasmic space and to inhibit the renewal process of the peptidoglycan structure. In Escherichia coli, the Cma (colicin M) phosphatase is activated in the periplasmic space by the FkpA chaperone and subsequently degrades the C55-PP precursor unit of the peptidoglycan. Pst (pesticin) from Yersinia pestis carries a lysozyme homology domain to degrade peptidoglycan. Import of Pst is only achieved if the N-terminal translocation domain can span the outer membrane and if extensive unfolding of the protein during membrane passage is permitted. There is considerable plasticity in the import pathway since a chimaera comprising the activity domain replaced by T4 lysozyme is also translocated and active in killing those bacteria carrying the FyuA receptor.

scholarly journals Activation of Colicin M by the FkpA ProlylCis-TransIsomerase/Chaperone

2010 ◽  
Vol 286 (8) ◽  
pp. 6280-6290 ◽  
Author(s):  
Stephanie Helbig ◽  
Silke I. Patzer ◽  
Cordelia Schiene-Fischer ◽  
Kornelius Zeth ◽  
Volkmar Braun
Keyword(s):  
Colicin M

scholarly journals Identification of receptor binding sites by competitive peptide mapping: phages T1, T5, and phi 80 and colicin M bind to the gating loop of FhuA.

1995 ◽  
Vol 177 (3) ◽  
pp. 694-698 ◽  
Author(s):  
H Killmann ◽  
G Videnov ◽  
G Jung ◽  
H Schwarz ◽  
V Braun
Keyword(s):  
Receptor Binding ◽  
Binding Sites ◽  
Peptide Mapping ◽  
Colicin M
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