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Haemagglutinating activities of oral strains of Streptococcus milleri group

T Yamaguchi1, M Taketoshi, H Eifuku-Koreeda

  • 1Department of Preventive Dentistry, Kagoshima University Dental School, Japan.

Microbios
|January 1, 1993
PubMed

Insights

Sixty-six Streptococcus intermedius strains agglutinated sheep red blood cells. Two distinct haemagglutinins were identified, with one heat-stable but trypsin-sensitive, recognizing L-arginine and L-lysine on erythrocyte surfaces.

Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Immunology

Background:

  • The Streptococcus milleri group, including Streptococcus intermedius, are opportunistic pathogens.
  • Haemagglutination by bacteria can be an important virulence factor, mediating adherence to host cells.
  • Understanding the mechanisms of bacterial adherence is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the haemagglutinating properties of Streptococcus milleri group strains.
  • To characterize the nature of the haemagglutinins involved in sheep erythrocyte agglutination by Streptococcus intermedius.
  • To identify potential receptors on sheep erythrocytes recognized by these haemagglutinins.

Main Methods:

  • Serotyping of 148 Streptococcus milleri group strains.
  • Testing for sheep erythrocyte agglutination.
  • Characterization of haemagglutinating activity using heat and trypsin treatments.
  • Inhibition assays with various substances (amino acids, glycoproteins) to identify erythrocyte receptors.

Main Results:

  • 66 out of 148 strains agglutinated sheep erythrocytes, primarily identified as Streptococcus intermedius.
  • Haemagglutinating strains lacked Lancefield group antigens and belonged to specific serotypes (g, h, i, j) or were untypeable.
  • Cell surface hydrophobicity did not differ significantly between agglutinating and non-agglutinating strains.
  • Haemagglutinating activity was partially sensitive to heat and trypsin, with complete loss after sequential treatment.
  • L-arginine, L-lysine, mucin, and fetuin inhibited haemagglutination, suggesting their role as erythrocyte receptors, particularly for the heat-stable haemagglutinin.

Conclusions:

  • At least two haemagglutinins are involved in the agglutination of Streptococcus intermedius.
  • A heat-stable, trypsin-sensitive haemagglutinin recognizes erythrocyte surface components containing L-arginine and L-lysine.
  • These findings contribute to understanding the molecular mechanisms of Streptococcus intermedius adherence and potential virulence.

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