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2017 ; 103
(6
): 919-930
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Collagen-like proteins of pathogenic streptococci
#MMPMID27997716
Lukomski S
; Bachert BA
; Squeglia F
; Berisio R
Mol Microbiol
2017[Mar]; 103
(6
): 919-930
PMID27997716
show ga
The collagen domain, which is defined by the presence of the Gly-X-Y triplet
repeats, is amongst the most versatile and widespread known structures found in
proteins from organisms representing all three domains of life. The streptococcal
collagen-like (Scl) proteins are widely present in pathogenic streptococci,
including Streptococcus pyogenes, S. agalactiae, S. pneumoniae, and S. equi.
Experiments and bioinformatic analyses support the hypothesis that all Scl
proteins are homotrimeric and cell wall-anchored. These proteins contain the
rod-shaped collagenous domain proximal to cell surface, as well as a variety of
outermost non-collagenous domains that generally lack predicted functions but can
be grouped into one of six clusters based on sequence similarity. The
well-characterized Scl1 proteins of S. pyogenes show a dichotomous switch in
ligand binding between human tissue and blood environments. In tissue, Scl1
adhesin specifically recognizes the wound microenvironment, promotes adhesion and
biofilm formation, decreases bacterial killing by neutrophil extracellular traps,
and modulates S. pyogenes virulence. In blood, ligands include components of
complement and coagulation-fibrinolytic systems, as well as plasma lipoproteins.
In all, the Scl proteins signify a large family of structurally related surface
proteins, which contribute to the ability of streptococci to colonize and cause
diseases in humans and animals.
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