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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 Front+Cell+Infect+Microbiol
2017 ; 7
(ä): 215
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The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its
Structure and Function
#MMPMID28603700
Lasica AM
; Ksiazek M
; Madej M
; Potempa J
Front Cell Infect Microbiol
2017[]; 7
(ä): 215
PMID28603700
show ga
Protein secretion systems are vital for prokaryotic life, as they enable bacteria
to acquire nutrients, communicate with other species, defend against biological
and chemical agents, and facilitate disease through the delivery of virulence
factors. In this review, we will focus on the recently discovered type IX
secretion system (T9SS), a complex translocon found only in some species of the
Bacteroidetes phylum. T9SS plays two roles, depending on the lifestyle of the
bacteria. It provides either a means of movement (called gliding motility) for
peace-loving environmental bacteria or a weapon for pathogens. The best-studied
members of these two groups are Flavobacterium johnsoniae, a commensal
microorganism often found in water and soil, and Porphyromonas gingivalis, a
human oral pathogen that is a major causative agent of periodontitis. In P.
gingivalis and some other periodontopathogens, T9SS translocates proteins,
especially virulence factors, across the outer membrane (OM). Proteins destined
for secretion bear a conserved C-terminal domain (CTD) that directs the cargo to
the OM translocon. At least 18 proteins are involved in this still enigmatic
process, with some engaged in the post-translational modification of T9SS cargo
proteins. Upon translocation across the OM, the CTD is removed by a protease with
sortase-like activity and an anionic LPS is attached to the newly formed
C-terminus. As a result, a cargo protein could be secreted into the extracellular
milieu or covalently attached to the bacterial surface. T9SS is regulated by a
two-component system; however, the precise environmental signal that triggers it
has not been identified. Exploring unknown systems contributing to bacterial
virulence is exciting, as it may eventually lead to new therapeutic strategies.
During the past decade, the major components of T9SS were identified, as well as
hints suggesting the possible mechanism of action. In addition, the list of
characterized cargo proteins is constantly growing. The actual structure of the
translocon, situated in the OM of bacteria, remains the least explored area;
however, new technical approaches and increasing scientific attention have
resulted in a growing body of data. Therefore, we present a compact up-to-date
review of this topic.