TY - JOUR
T1 - Staphylococcus aureus expresses a major histocompatibility complex class II analog
AU - Jönsson, Klas
AU - McDevitt, Damien
AU - McGavin, Mary Homonylo
AU - Patti, Joseph M.
AU - Höök, Magnus
PY - 1995/9/15
Y1 - 1995/9/15
N2 - 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 β 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.
AB - 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 β 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.
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U2 - 10.1074/jbc.270.37.21457
DO - 10.1074/jbc.270.37.21457
M3 - Article
C2 - 7545162
AN - SCOPUS:0029096724
SN - 0021-9258
VL - 270
SP - 21457
EP - 21460
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 37
ER -