Mycoplasma pulmonisVsa proteins and polysaccharide modulate adherence to pulmonary epithelial cells

Authors

  • Jeffrey R. Bolland,

    1. Department of Microbiology, The University of Alabama at Birmingham, Birmingham, AL, USA
    Current affiliation:
    1. U.S. Department of Agriculture, Agricultural Research Service, Crop Diseases, Pests, and Genetics Unit, Parlier, CA, USA
    Search for more papers by this author
  • Kevin Dybvig

    Corresponding author
    1. Department of Genetics, The University of Alabama at Birmingham, Birmingham, AL, USA
    • Department of Microbiology, The University of Alabama at Birmingham, Birmingham, AL, USA
    Search for more papers by this author

Correspondence: Kevin Dybvig, Department of Genetics, University of Alabama at Birmingham, KAUL 720, Birmingham, AL 35294-0024, USA. Tel.: +1 205 934 9141; fax: +1 205 975 4418; e-mail: dybvig@uab.edu

Abstract

The Mycoplasma pulmonisVsa proteins are a family of size- and phase-variable lipoproteins that shield the mycoplasmas from complement and modulate attachment to abiotic surfaces. Mycoplasmas producing a long Vsa protein hemadsorb poorly and yet are proficient at colonizing rats and mice. The effect of the length of the Vsa protein on the attachment of mycoplasmas to epithelial cells has not been previously explored. We find that independent of Vsa isotype, mycoplasmas producing a long Vsa protein with many tandem repeats adhere poorly to murine MLE-12 cells compared with mycoplasmas producing a short Vsa. We also find that mutants lacking the EPS-I polysaccharide of M. pulmonis exhibited decreased adherence to MLE-12 cells, even though it has been shown previously that such mutants have an enhanced ability to form a biofilm.

Ancillary