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2014 ; 78
(3
): 544-71
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Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and
potential alternative drug targets
#MMPMID25184565
Ünal CM
; Steinert M
Microbiol Mol Biol Rev
2014[Sep]; 78
(3
): 544-71
PMID25184565
show ga
Initially discovered in the context of immunomodulation, peptidyl-prolyl
cis/trans isomerases (PPIases) were soon identified as enzymes catalyzing the
rate-limiting protein folding step at peptidyl bonds preceding proline residues.
Intense searches revealed that PPIases are a superfamily of proteins consisting
of three structurally distinguishable families with representatives in every
described species of prokaryote and eukaryote and, recently, even in some giant
viruses. Despite the clear-cut enzymatic activity and ubiquitous distribution of
PPIases, reports on solely PPIase-dependent biological roles remain scarce.
Nevertheless, they have been found to be involved in a plethora of biological
processes, such as gene expression, signal transduction, protein secretion,
development, and tissue regeneration, underscoring their general importance.
Hence, it is not surprising that PPIases have also been identified as
virulence-associated proteins. The extent of contribution to virulence is highly
variable and dependent on the pleiotropic roles of a single PPIase in the
respective pathogen. The main objective of this review is to discuss this variety
in virulence-related bacterial and protozoan PPIases as well as the involvement
of host PPIases in infectious processes. Moreover, a special focus is given to
Legionella pneumophila macrophage infectivity potentiator (Mip) and Mip-like
PPIases of other pathogens, as the best-characterized virulence-related
representatives of this family. Finally, the potential of PPIases as alternative
drug targets and first tangible results are highlighted.
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