Staphylococcus aureus expresses a major histocompatibility complex class II analog. Academic Article uri icon

abstract

  • Staphylococcus aureus expresses various surface proteins which specifically recognize and bind to different host molecules. We have previously identified a bacterial protein that exhibits a broad specificity and binds to several mammalian extracellular proteins. The gene encoding this bacterial component has now been cloned and sequenced. The deduced protein consists predominantly of six repeated domains of 110 residues. Each of the repeated domains contain a subdomain of 31 residues that share striking sequence homology with a segment in the peptide binding groove of the beta chain of the major histocompatibility complex (MHC) class II proteins from different mammalian species. The purified recombinant bacterial protein bound several mammalian proteins, including recombinant osteopontin, suggesting a protein-protein interaction and also specifically recognized a 15-amino acid residue synthetic peptide. Taken together, these results suggest that the bacterial protein resembles mammalian MHC class II molecules with respect to both sequence similarities and peptide binding capabilities.

published proceedings

  • J Biol Chem

altmetric score

  • 3

author list (cited authors)

  • Jnsson, K., McDevitt, D., McGavin, M. H., Patti, J. M., & Hk, M.

citation count

  • 96

complete list of authors

  • Jönsson, K||McDevitt, D||McGavin, MH||Patti, JM||Höök, M

publication date

  • September 1995