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Related Experiment Videos

Staphylococcus aureus expresses a major histocompatibility complex class II analog

K Jönsson1, D McDevitt, M H McGavin

  • 1Center for Extracellular Matrix Biology, Texas A & M University, Houston 77030-3303, USA.

The Journal of Biological Chemistry
|September 15, 1995
PubMed
Summary

A novel Staphylococcus aureus protein shares sequence and functional similarities with mammalian MHC class II molecules. This bacterial protein binds host extracellular proteins and synthetic peptides, suggesting a potential role in host-pathogen interactions.

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Area of Science:

  • Microbiology
  • Immunology
  • Molecular Biology

Background:

  • Staphylococcus aureus possesses surface proteins that interact with host molecules.
  • A previously identified bacterial protein shows broad specificity for mammalian extracellular proteins.

Purpose of the Study:

  • To clone and sequence the gene encoding the identified bacterial protein.
  • To investigate the structural and functional characteristics of this bacterial protein.
  • To compare the bacterial protein with mammalian host molecules.

Main Methods:

  • Gene cloning and sequencing of the bacterial protein.
  • Analysis of protein sequence for conserved domains.
  • Purification of recombinant bacterial protein.
  • Binding assays with mammalian proteins and synthetic peptides.

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Main Results:

  • The bacterial protein comprises six repeated 110-residue domains.
  • Each domain contains a 31-residue subdomain homologous to the peptide-binding groove of MHC class II beta chains.
  • The purified protein binds mammalian proteins like osteopontin and a 15-amino acid synthetic peptide.

Conclusions:

  • The bacterial protein exhibits sequence homology to mammalian MHC class II molecules.
  • The protein demonstrates peptide-binding capabilities, similar to MHC class II.
  • These findings suggest functional and structural resemblance between the bacterial protein and host MHC class II molecules.