Role for Cell-Surface Collagen of Streptococcus pyogenes in Infections

Copyright © 2020 American Chemical Society. Group A Streptococcus (GAS) displays cell-surface proteins that resemble human collagen. We find that a fluorophore-labeled collagen mimetic peptide (CMP) labels GAS cells but not Escherichia coli or Bacillus subtilis cells, which lack such proteins. The C...

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Bibliographic Details
Main Authors: Ellison, Aubrey J, Dempwolff, Felix, Kearns, Daniel B, Raines, Ronald T
Format: Article
Language:English
Published: American Chemical Society (ACS) 2021
Online Access:https://hdl.handle.net/1721.1/132552
Description
Summary:Copyright © 2020 American Chemical Society. Group A Streptococcus (GAS) displays cell-surface proteins that resemble human collagen. We find that a fluorophore-labeled collagen mimetic peptide (CMP) labels GAS cells but not Escherichia coli or Bacillus subtilis cells, which lack such proteins. The CMP likely engages in a heterotrimeric helix with endogenous collagen, as the nonnatural d enantiomer of the CMP does not label GAS cells. To identify a molecular target, we used reverse genetics to "knock-in"the GAS genes that encode two proteins with collagen-like domains, Scl1 and Scl2, into B. subtilis. The fluorescent CMP labels the cells of these B. subtilis strains. Moreover, these strains bind tightly to a surface of mammalian collagen. These data are consistent with streptococcal collagen forming triple helices with damaged collagen in a wound bed and thus have implications for microbial virulence.