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Mycoplasma pulmonis Vsa proteins and polysaccharide modulate adherence to pulmonary epithelial cells

Jeffrey R Bolland1, Kevin Dybvig

  • 1Department of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294-0024, USA.

FEMS Microbiology Letters
|March 21, 2012
PubMed

Insights

Mycoplasma pulmonis Vsa proteins of longer length poorly attach to lung cells. Conversely, shorter Vsa proteins enhance mycoplasma adherence, impacting colonization and biofilm formation.

Area of Science:

  • Microbiology
  • Cell Biology
  • Immunology

Background:

  • Mycoplasma pulmonis Vsa proteins are lipoproteins that vary in size and phase.
  • Longer Vsa proteins are associated with poor hemadsorption but efficient colonization in rodents.
  • The impact of Vsa protein length on epithelial cell attachment was previously unexplored.

Purpose of the Study:

  • To investigate the effect of Vsa protein length on the adherence of Mycoplasma pulmonis to murine epithelial cells.
  • To determine the role of the EPS-I polysaccharide in M. pulmonis adherence.

Main Methods:

  • Utilized murine MLE-12 cells for in vitro adherence assays.
  • Compared adherence of M. pulmonis strains producing long versus short Vsa proteins.
  • Examined adherence of M. pulmonis mutants lacking the EPS-I polysaccharide.

Main Results:

  • Mycoplasmas producing long Vsa proteins exhibited significantly poorer adherence to MLE-12 cells compared to those with short Vsa proteins.
  • The length of the Vsa protein, irrespective of isotype, correlated with adherence levels.
  • Mutants lacking the EPS-I polysaccharide showed decreased adherence to MLE-12 cells, contrasting with their enhanced biofilm formation.

Conclusions:

  • Vsa protein length is a critical factor influencing Mycoplasma pulmonis adherence to respiratory epithelial cells.
  • Shorter Vsa proteins promote greater adherence to MLE-12 cells.
  • The EPS-I polysaccharide plays a role in M. pulmonis attachment to epithelial cells, independent of its role in biofilm formation.

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