Oligomerized backbone pilin helps piliated Lactococcus lactis to withstand shear flow

Biofouling. 2016 Sep;32(8):911-23. doi: 10.1080/08927014.2016.1213817.

Abstract

The present work focuses on the role of pili present at the cell surface of Lactococcus lactis in bacterial adhesion to abiotic (hydrophobic polystyrene) and biotic (mucin-coated polystyrene) surfaces. Native pili-displaying strains and isogenic derivatives in which pilins or sortase C structural genes had been modified were used. Surface physico-chemistry, morphology and shear-flow-induced detachment of lactococcal cells were evaluated. The involvement of pili in L. lactis adhesion was clearly demonstrated, irrespective of the surface characteristics (hydrophobic/hydrophilic, presence or not of specific binding sites). The accessory pilin, PilC, and the backbone pilin, PilB, were revealed to play a major role in adhesion, provided that the PilB was present in its polymerized form. Within the population fraction that remained attached to the surface under increasing shear flow, different association behaviors were observed, showing that pili could serve as anchoring sites thus hampering the effect of shear flow on cell orientation and detachment.

Keywords: Adhesion; Lactococcus lactis; pili; shear flow.

MeSH terms

  • Aminoacyltransferases / genetics
  • Aminoacyltransferases / metabolism*
  • Bacterial Adhesion / physiology*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cysteine Endopeptidases / genetics
  • Cysteine Endopeptidases / metabolism*
  • Fimbriae Proteins / genetics
  • Fimbriae Proteins / metabolism*
  • Fimbriae, Bacterial / metabolism*
  • Humans
  • Hydrodynamics
  • Hydrophobic and Hydrophilic Interactions
  • Lactococcus lactis / metabolism
  • Lactococcus lactis / physiology*
  • Mucins / chemistry
  • Polystyrenes / chemistry*
  • Protein Multimerization
  • Stress, Mechanical
  • Surface Properties

Substances

  • Bacterial Proteins
  • Mucins
  • Polystyrenes
  • sortase C
  • Fimbriae Proteins
  • Aminoacyltransferases
  • Cysteine Endopeptidases