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DrsG from Streptococcus dysgalactiae subsp equisimilis inhibits the antimicrobial peptide LL-37
Journal article   Open access   Peer reviewed

DrsG from Streptococcus dysgalactiae subsp equisimilis inhibits the antimicrobial peptide LL-37

Danielle Smyth, Ainslie Cameron, Mark R Davies, Celia McNeilly, Louise Hafner, K S Sriprakash and David J McMillan
Infection and immunity, Vol.82(6), pp.2337-2344
2014
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PDF - Author's Accepted Version176.01 kBDownloadView
Accepted VersionPDF - Author Accepted Version Open Access
url
https://doi.org/10.1128/IAI.01411-13View
Published Version

Abstract

Streptococcus dysgalactiae subsp. equisimilis drsG antimicrobial peptide LL-37
SIC and DRS are related proteins present in only four of the more than 200 Streptococcus pyogenes emm-types. These proteins inhibit complement mediated lysis and/or the activity of certain antimicrobial peptides. A gene encoding a homologue of these proteins, herein called DrsG, has been identified in the related bacterium Streptococcus dysgalactiae subsp equisimilis (SDSE). Here we show that geographically dispersed isolates representing 14 of 50 emm-types examined possess variants of drsG. However not all isolates within the drsG-positive emm-types possess the gene. Sequence comparisons also reveal a high degree of conservation in different SDSE emm-types. To examine the biological activity of DrsG, recombinant versions of two major DrsG variants, DrsGS and DrsGL, were expressed and purified. Western blot analysis using antisera raised to these proteins demonstrated both variants to be expressed and secreted into culture supernatant. Unlike SIC, but similar to DRS, DrsG does not inhibit complement mediated lysis. However, like both SIC and DRS, DrsG is a ligand of the cathelcidin LL-37 and is inhibitory to its bactericidal activity in in vitro assays. Conservation of prolines in this latter region also suggests these residues are important in the biology of this family of proteins. This is the first report demonstrating the activity of an AMP inhibitory protein in SDSE and suggest that inhibition of AMP activity is the primary function of this family of proteins. The acquisition of complement inhibitory activity of SIC may reflect its continuing evolution.

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