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Sortase A substrate specificity in GBS pilus 2a cell wall anchoring.

Francesca Necchi1, Vincenzo Nardi-Dei, Massimiliano Biagini

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Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Vaccine Development

Background:

  • Streptococcus agalactiae (Group B Streptococcus, GBS) causes severe infant infections.
  • Cell surface pili are key GBS virulence factors and potential vaccine targets.
  • GBS pili are assembled by sortases, with sortase A (SrtA) involved in cell wall anchoring.

Purpose of the Study:

  • To elucidate the specific role of SrtA in GBS pilus 2a anchoring.
  • To investigate the mechanism of pilus 2a assembly and cell wall attachment.

Main Methods:

  • In vivo mutagenesis to identify essential anchoring signals.
  • Production of purified recombinant SrtA (SrtA(ΔN40)).
  • In vitro enzymatic assays using synthetic peptides and recombinant proteins to test SrtA activity.

Main Results:

  • The LPXTG sorting signal of the minor ancillary protein (AP2) is crucial for pilus 2a anchoring.
  • Recombinant SrtA specifically hydrolyzed AP2-2a's sorting signal and catalyzed its transpeptidation with peptidoglycan analogues.
  • SrtA did not act on sorting signals of other pilus 2a subunits (backbone or major ancillary proteins).

Conclusions:

  • SrtA is essential for GBS pilus 2a cell wall covalent attachment.
  • SrtA exclusively targets the minor accessory pilin (AP2) for anchoring, representing the pilus's terminal subunit.
  • This specificity provides critical insight into GBS pilus assembly and potential therapeutic strategies.