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Bacteroides fragilis lipopolysaccharide and group B streptococcus serotype II glycocalyx have a common major

L Linko1, M K Viljanen

  • 1Department of Medical Microbiology, University of Turku, Finland.

Insights

A new monoclonal antibody (MAB) specifically targets a unique digalactose structure in type II Group B Streptococcus (GBS). This antibody shows potential for accurately identifying and serotyping GBS strains.

Area of Science:

  • Microbiology
  • Immunology
  • Bacteriology

Background:

  • Group B Streptococcus (GBS) is a significant pathogen, particularly in neonates.
  • Accurate serotyping of GBS is crucial for epidemiological studies and vaccine development.
  • The capsular lipocarbohydrate (LPS) of GBS contains type-specific antigens.

Purpose of the Study:

  • To develop and characterize a monoclonal antibody (MAB) targeting a specific structure in GBS.
  • To investigate the reactivity of the MAB with different GBS strains.
  • To determine the location and nature of the targeted antigen.

Main Methods:

  • Immunofluorescence technique (IF) using a MAB against a beta-1-6-linked digalactose structure.
  • Gas chromatography-mass spectrometry (GC-MS) for antigen analysis.
  • Immuno-electron microscopy (IEM) for antigen localization.

Main Results:

  • The MAB reacted with 47 out of 416 GBS strains, primarily type II GBS.
  • GC-MS confirmed the antigen contained galactose, glucose, and fatty acids, identifying it as a digalactose structure.
  • IEM localized the determinant to the GBS glycocalyx, approximately 15 nm from the cell wall.

Conclusions:

  • The MAB recognizes an integral part of the type II GBS-specific antigen.
  • The targeted digalactose structure is a key component of the type II GBS capsular lipocarbohydrate.
  • This MAB has potential utility as a serotyping reagent for GBS identification.

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