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Related Experiment Videos

Antigenic differences among Campylobacter fetus S-layer proteins.

J D Dubreuil1, M Kostrzynska, J W Austin

  • 1Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.

Journal of Bacteriology
|September 1, 1990
PubMed
Summary
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Campylobacter fetus S-layer proteins exhibit diverse molecular weights and antigenic specificities, suggesting antigenic variation. Their highly organized lattice structure confers unusual heat resistance to surface epitopes.

Area of Science:

  • Microbiology
  • Structural Biology
  • Immunology

Background:

  • Campylobacter fetus is a pathogen known for its surface layer (S-layer) proteins.
  • S-layer proteins form a crystalline outer layer on the cell surface, contributing to cell structure and potentially virulence.
  • Understanding the heterogeneity and properties of C. fetus S-layer proteins is crucial for developing effective diagnostics and therapeutics.

Purpose of the Study:

  • To characterize the molecular weight, structure, antigenicity, and stability of S-layer proteins from different Campylobacter fetus strains.
  • To investigate the phenomenon of antigenic variation in C. fetus S-layer proteins.
  • To identify protease-resistant domains within the S-layer proteins.

Main Methods:

  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for molecular weight determination.

Related Experiment Videos

  • Electron microscopy for S-layer lattice structure analysis.
  • Amino-terminal sequencing and Western immunoblot analysis for antigenic characterization.
  • Thermal denaturation experiments for stability assessment.
  • Protease digestion to identify resistant domains.

    • Main Results:

    • Predominant S-layer proteins ranged from 90,000 to 140,000 molecular weight, forming oblique lattices (approx. 5.6 nm spacing).
    • At least four different antigenic specificities were identified among C. fetus strains.
    • Evidence of antigenic variation was observed, with some cells displaying immunoreactive lattices and others not.
    • S-layer epitopes demonstrated unusual heat resistance, attributed to the organized lattice structure.
    • Protease digestion revealed a large resistant domain (approx. 110,000 Mr) carrying most epitopes and a smaller sensitive domain.

    Conclusions:

    • Campylobacter fetus S-layer proteins are diverse in molecular weight and antigenicity, with evidence of antigenic variation.
    • The ordered S-layer lattice contributes significantly to the thermal stability of surface epitopes.
    • Protease digestion studies highlight distinct structural domains within the S-layer protein, with a major epitope-carrying domain being highly resistant to enzymatic degradation.