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<p>S protein is conserved among streptococci and contributes to group A <i>Streptococcus</i> virulence, but the mechanisms involved are unclear. Here we used genetic, biochemical, single-molecule, in vitro and in vivo analyses to show that S protein is crucial for resistance against host-derived antimicrobials by coordinating cell wall modification and repair. We observed that S protein was localized to the streptococcal septum dependent on its transmembrane domain, while S protein function was dependent on its peptidoglycan (PG)-binding LysM domain. Direct interactions between the pneumococcal S protein and the PG synthase PBP1a as well as the PG deacetylase PgdA were detected. Loss of S protein reduced the proportion of circumferentially moving PBP1a molecules, altered streptococcal morphology and increased susceptibility to cell-wall-targeting antibiotics, suggesting that S protein activates PBP1a. <i>Streptococcus pneumoniae ess</i> mutants lacking the gene encoding S protein were more susceptible to human antimicrobial peptide LL-37 and lysozyme, while their virulence was decreased compared with wild-type bacteria in zebrafish and mice. These data suggest that S protein activates the PG repair and modification complex, providing defence against host-derived and environmental antimicrobials.</p>

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Pneumococcal S protein coordinates cell wall modification and repair to resist host antimicrobials

  • 期刊论文

  • 发表日期：

    2025年12月19日

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  • Jessica Burnier,
  • Clement Gallay,
  • Kevin E. Bruce,
  • Elisabet Bjånes,
  • Louise Martin,
  • Kin Ki Jim,
  • Ho-Ching Tiffany Tsui,
  • Amelieke J. H. Cremers,
  • Johann Mignolet,
  • Daniela Vollmer,
  • Jacob Biboy,
  • Victor Nizet,
  • Waldemar Vollmer,
  • Malcolm E. Winkler,
  • Jan-Willem Veening

摘要

S protein is conserved among streptococci and contributes to group A Streptococcus virulence, but the mechanisms involved are unclear. Here we used genetic, biochemical, single-molecule, in vitro and in vivo analyses to show that S protein is crucial for resistance against host-derived antimicrobials by coordinating cell wall modification and repair. We observed that S protein was localized to the streptococcal septum dependent on its transmembrane domain, while S protein function was dependent on its peptidoglycan (PG)-binding LysM domain. Direct interactions between the pneumococcal S protein and the PG synthase PBP1a as well as the PG deacetylase PgdA were detected. Loss of S protein reduced the proportion of circumferentially moving PBP1a molecules, altered streptococcal morphology and increased susceptibility to cell-wall-targeting antibiotics, suggesting that S protein activates PBP1a. Streptococcus pneumoniae ess mutants lacking the gene encoding S protein were more susceptible to human antimicrobial peptide LL-37 and lysozyme, while their virulence was decreased compared with wild-type bacteria in zebrafish and mice. These data suggest that S protein activates the PG repair and modification complex, providing defence against host-derived and environmental antimicrobials.