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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 J+Bacteriol
2016 ; 198
(20
): 2784-93
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F-Type Bacteriocins of Listeria monocytogenes: a New Class of Phage Tail-Like
Structures Reveals Broad Parallel Coevolution between Tailed Bacteriophages and
High-Molecular-Weight Bacteriocins
#MMPMID27457717
Lee G
; Chakraborty U
; Gebhart D
; Govoni GR
; Zhou ZH
; Scholl D
J Bacteriol
2016[Oct]; 198
(20
): 2784-93
PMID27457717
show ga
Listeria monocytogenes is a significant foodborne human pathogen that can cause
severe disease in certain high-risk individuals. L. monocytogenes is known to
produce high-molecular-weight, phage tail-like bacteriocins, or "monocins," upon
induction of the SOS system. In this work, we purified and characterized monocins
and found them to be a new class of F-type bacteriocins. The L. monocytogenes
monocin genetic locus was cloned and expressed in Bacillus subtilis, producing
specifically targeted bactericidal particles. The receptor binding protein, which
determines target cell specificity, was identified and engineered to change the
bactericidal spectrum. Unlike the F-type pyocins of Pseudomonas aeruginosa, which
are related to lambda-like phage tails, monocins are more closely related to
TP901-1-like phage tails, structures not previously known to function as
bacteriocins. Monocins therefore represent a new class of phage tail-like
bacteriocins. It appears that multiple classes of phage tails and their related
bacteriocins have coevolved separately in parallel. IMPORTANCE: Phage tail-like
bacteriocins (PTLBs) are structures widespread among the members of the bacterial
kingdom that are evolutionarily related to the DNA delivery organelles of phages
(tails). We identified and characterized "monocins" of Listeria monocytogenes and
showed that they are related to the tail structures of TP901-1-like phages,
structures not previously known to function as bacteriocins. Our results show
that multiple types of envelope-penetrating machines have coevolved in parallel
to function either for DNA delivery (phages) or as membrane-disrupting
bacteriocins. While it has commonly been assumed that these structures were
coopted from phages, we cannot rule out the opposite possibility, that ancient
phages coopted complex bacteriocins from the cell, which then underwent
adaptations to become efficient at translocating DNA.