Streptococcus mutans major adhesion surface protein, P1 (I/II), does not contribute to attachment to valvular vegetations or to the development of endocarditis in a rat model

Arch Oral Biol. 1996 Oct;41(10):999-1002. doi: 10.1016/s0003-9969(96)00035-0.

Abstract

Streptococcus mutans P1 antigen functions as an adhesion factor for binding to salivary pellicle on tooth surfaces. It induces increased antibody titres in patients with Strep. mutans endocarditis. A mutant of Strep. mutans deficient in the function of the gene (spa P) encoding the surface antigen P1, and its isogenic parental strain, were used in a rat endocarditis experiment. Absence of P1 did not decrease adhesion to vegetations determined l h after intravenous infection. The number of bacteria recovered from valvular vegetations after 48 h from animals with manifest endocarditis did not differ between the strains. Consequently, the Pl antigen appears to be unimportant both for adhesion and virulence in endocarditis caused by Strep. mutans.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, Bacterial / physiology*
  • Bacterial Adhesion / immunology
  • Bacterial Outer Membrane Proteins / physiology
  • Bacterial Proteins / immunology*
  • Colony Count, Microbial
  • Dental Pellicle
  • Endocarditis, Bacterial / microbiology*
  • Female
  • Heart Valves / microbiology*
  • Membrane Glycoproteins*
  • Rats
  • Rats, Wistar
  • Streptococcus mutans / immunology*
  • Streptococcus mutans / pathogenicity*
  • Virulence

Substances

  • Antigens, Bacterial
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Membrane Glycoproteins
  • S-layer proteins